ID CADM1_HUMAN Reviewed; 442 AA. AC Q9BY67; A4FVB5; F5H0J4; H0YGA7; H1ZZV9; H1ZZW1; H1ZZW2; Q86WB8; Q8N2F4; AC X5D2C8; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 2. DT 14-DEC-2022, entry version 176. DE RecName: Full=Cell adhesion molecule 1; DE AltName: Full=Immunoglobulin superfamily member 4; DE Short=IgSF4; DE AltName: Full=Nectin-like protein 2; DE Short=NECL-2; DE AltName: Full=Spermatogenic immunoglobulin superfamily; DE Short=SgIgSF; DE AltName: Full=Synaptic cell adhesion molecule; DE Short=SynCAM; DE AltName: Full=Tumor suppressor in lung cancer 1; DE Short=TSLC-1; DE Flags: Precursor; GN Name=CADM1 {ECO:0000312|HGNC:HGNC:5951}; GN Synonyms=IGSF4 {ECO:0000250|UniProtKB:Q8R5M8}, IGSF4A, NECL2 GN {ECO:0000303|PubMed:15811952}, SYNCAM {ECO:0000250|UniProtKB:Q8R5M8}, GN TSLC1 {ECO:0000303|PubMed:15811952}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF69029.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=15893517; DOI=10.1016/j.bbamem.2005.01.013; RA Zhou Y., Du G., Hu X., Yu S., Liu Y., Xu Y., Huang X., Liu J., Yin B., RA Fan M., Peng X., Qiang B., Yuan J.; RT "Nectin-like molecule 1 is a protein 4.1N associated protein and recruits RT protein 4.1N from cytoplasm to the plasma membrane."; RL Biochim. Biophys. Acta 1669:142-154(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), FUNCTION, SUBCELLULAR RP LOCATION, AND ALTERNATIVE SPLICING. RC TISSUE=Mast cell; RX PubMed=22438059; DOI=10.1007/s00018-012-0948-y; RA Moiseeva E.P., Leyland M.L., Bradding P.; RT "CADM1 isoforms differentially regulate human mast cell survival and RT homotypic adhesion."; RL Cell. Mol. Life Sci. 69:2751-2764(2012). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). RC TISSUE=Fetal brain; RX PubMed=24722188; DOI=10.1038/ncomms4650; RA Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., RA Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., RA Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A., RA Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., RA Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.; RT "Protein interaction network of alternatively spliced isoforms from brain RT links genetic risk factors for autism."; RL Nat. Commun. 5:3650-3650(2014). RN [4] {ECO:0000305, ECO:0000312|EMBL:BAC66178.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Lung {ECO:0000312|EMBL:BAC66178.1}; RA Ito A., Koma Y., Nagano T.; RT "Cloning of a secretory isoform of SgIGSF/TSLC-1."; RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000305, ECO:0000312|EMBL:BAC11657.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryo {ECO:0000312|EMBL:BAC11657.1}; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] {ECO:0000305} RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11279526; DOI=10.1038/86934; RA Kuramochi M., Fukuhara H., Nobukuni T., Kanbe T., Maruyama T., Ghosh H.P., RA Pletcher M., Isomura M., Onizuka M., Kitamura T., Sekiya T., Reeves R.H., RA Murakami Y.; RT "TSLC1 is a tumor-suppressor gene in human non-small-cell lung cancer."; RL Nat. Genet. 27:427-430(2001). RN [9] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH EPB41L3. RX PubMed=12234973; RA Yageta M., Kuramochi M., Masuda M., Fukami T., Fukuhara H., Maruyama T., RA Shibuya M., Murakami Y.; RT "Direct association of TSLC1 and DAL-1, two distinct tumor suppressor RT proteins in lung cancer."; RL Cancer Res. 62:5129-5133(2002). RN [10] {ECO:0000305} RP FUNCTION, SUBUNIT, AND GLYCOSYLATION. RX PubMed=12050160; DOI=10.1074/jbc.m203620200; RA Masuda M., Yageta M., Fukuhara H., Kuramochi M., Maruyama T., Nomoto A., RA Murakami Y.; RT "The tumor suppressor protein TSLC1 is involved in cell-cell adhesion."; RL J. Biol. Chem. 277:31014-31019(2002). RN [11] {ECO:0000305} RP DOMAIN. RX PubMed=14633730; RA Mao X., Seidlitz E., Ghosh K., Murakami Y., Ghosh H.P.; RT "The cytoplasmic domain is critical to the tumor suppressor activity of RT TSLC1 in non-small cell lung cancer."; RL Cancer Res. 63:7979-7985(2003). RN [12] {ECO:0000305} RP DISEASE. RX PubMed=12925956; DOI=10.1002/ijc.11348; RA Fukami T., Fukuhara H., Kuramochi M., Maruyama T., Isogai K., Sakamoto M., RA Takamoto S., Murakami Y.; RT "Promoter methylation of the TSLC1 gene in advanced lung tumors and various RT cancer cell lines."; RL Int. J. Cancer 107:53-59(2003). RN [13] {ECO:0000305} RP FUNCTION. RX PubMed=12920246; DOI=10.1097/01.lab.0000081391.28136.80; RA Ito A., Okada M., Uchino K., Wakayama T., Koma Y., Iseki S., Tsubota N., RA Okita Y., Kitamura Y.; RT "Expression of the TSLC1 adhesion molecule in pulmonary epithelium and its RT down-regulation in pulmonary adenocarcinoma other than bronchioloalveolar RT carcinoma."; RL Lab. Invest. 83:1175-1183(2003). RN [14] {ECO:0000305} RP INTERACTION WITH MPP3. RX PubMed=13679854; DOI=10.1038/sj.onc.1206744; RA Fukuhara H., Masuda M., Yageta M., Fukami T., Kuramochi M., Maruyama T., RA Kitamura T., Murakami Y.; RT "Association of a lung tumor suppressor TSLC1 with MPP3, a human homologue RT of Drosophila tumor suppressor Dlg."; RL Oncogene 22:6160-6165(2003). RN [15] {ECO:0000305} RP DOMAIN. RX PubMed=15184878; DOI=10.1038/sj.onc.1207756; RA Mao X., Seidlitz E., Truant R., Hitt M., Ghosh H.P.; RT "Re-expression of TSLC1 in a non-small-cell lung cancer cell line induces RT apoptosis and inhibits tumor growth."; RL Oncogene 23:5632-5642(2004). RN [16] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH CRTAM. RX PubMed=15811952; DOI=10.1182/blood-2005-02-0817; RA Boles K.S., Barchet W., Diacovo T., Cella M., Colonna M.; RT "The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell RT responses through the cell-surface receptor CRTAM."; RL Blood 106:779-786(2005). RN [17] {ECO:0000305} RP INTERACTION WITH CRTAM. RX PubMed=15781451; DOI=10.1074/jbc.m502095200; RA Galibert L., Diemer G.S., Liu Z., Johnson R.S., Smith J.L., Walzer T., RA Comeau M.R., Rauch C.T., Wolfson M.F., Sorensen R.A., RA Van der Vuurst de Vries A.-R., Branstetter D.G., Koelling R.M., RA Scholler J., Fanslow W.C., Baum P.R., Derry J.M., Yan W.; RT "Nectin-like protein 2 defines a subset of T-cell zone dendritic cells and RT is a ligand for class-I-restricted T-cell-associated molecule."; RL J. Biol. Chem. 280:21955-21964(2005). RN [18] {ECO:0000305} RP FUNCTION. RX PubMed=15905536; DOI=10.4049/jimmunol.174.11.6934; RA Furuno T., Ito A., Koma Y., Watabe K., Yokozaki H., Bienenstock J., RA Nakanishi M., Kitamura Y.; RT "The spermatogenic Ig superfamily/synaptic cell adhesion molecule mast-cell RT adhesion molecule promotes interaction with nerves."; RL J. Immunol. 174:6934-6942(2005). RN [19] {ECO:0000305} RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-113. RC TISSUE=Plasma {ECO:0000269|PubMed:16335952}; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-113. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [21] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-113. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [23] RP INTERACTION WITH HERPES VIRUS 8 PROTEINS VFLIP AND VGPCR (MICROBIAL RP INFECTION), AND FUNCTION (MICROBIAL INFECTION). RX PubMed=29698475; DOI=10.1371/journal.ppat.1006968; RA Hunte R., Alonso P., Thomas R., Bazile C.A., Ramos J.C., van der Weyden L., RA Dominguez-Bendala J., Khan W.N., Shembade N.; RT "CADM1 is essential for KSHV-encoded vGPCR-and vFLIP-mediated chronic NF- RT kappaB activation."; RL PLoS Pathog. 14:E1006968-E1006968(2018). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 400-411 IN COMPLEX WITH EPB41L3, RP MUTAGENESIS OF TYR-406 AND THR-408, AND INTERACTION WITH EPB41L3. RX PubMed=21131357; DOI=10.1074/jbc.m110.174011; RA Busam R.D., Thorsell A.G., Flores A., Hammarstrom M., Persson C., RA Obrink B., Hallberg B.M.; RT "Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding to RT differentially expressed in adenocarcinoma of the lung (DAL-1/4.1B)."; RL J. Biol. Chem. 286:4511-4516(2011). RN [25] {ECO:0007744|PDB:4H5S} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 45-144, SUBUNIT, INTERACTION WITH RP CRTAM, AND DISULFIDE BOND. RX PubMed=23871486; DOI=10.1016/j.str.2013.06.006; RA Zhang S., Lu G., Qi J., Li Y., Zhang Z., Zhang B., Fan Z., Yan J., RA Gao G.F.; RT "Competition of cell adhesion and immune recognition: insights into the RT interaction between CRTAM and nectin-like 2."; RL Structure 21:1430-1439(2013). CC -!- FUNCTION: Mediates homophilic cell-cell adhesion in a Ca(2+)- CC independent manner (PubMed:22438059, PubMed:12050160). Also mediates CC heterophilic cell-cell adhesion with CADM3 and NECTIN3 in a Ca(2+)- CC independent manner (By similarity). Interaction with CRTAM promotes CC natural killer (NK) cell cytotoxicity and interferon-gamma (IFN-gamma) CC secretion by CD8+ cells in vitro as well as NK cell-mediated rejection CC of tumors expressing CADM1 in vivo (PubMed:15811952). In mast cells, CC may mediate attachment to and promote communication with nerves CC (PubMed:15905536). CADM1, together with MITF, is essential for CC development and survival of mast cells in vivo (PubMed:22438059). By CC interacting with CRTAM and thus promoting the adhesion between CD8+ T- CC cells and CD8+ dendritic cells, regulates the retention of activated CC CD8+ T-cell within the draining lymph node (By similarity). Required CC for the intestinal retention of intraepithelial CD4+ CD8+ T-cells and, CC to a lesser extent, intraepithelial and lamina propria CD8+ T-cells and CC CD4+ T-cells (By similarity). Interaction with CRTAM promotes the CC adhesion to gut-associated CD103+ dendritic cells, which may facilitate CC the expression of gut-homing and adhesion molecules on T-cells and the CC conversion of CD4+ T-cells into CD4+ CD8+ T-cells (By similarity). Acts CC as a synaptic cell adhesion molecule and plays a role in the formation CC of dendritic spines and in synapse assembly (By similarity). May be CC involved in neuronal migration, axon growth, pathfinding, and CC fasciculation on the axons of differentiating neurons (By similarity). CC May play diverse roles in the spermatogenesis including in the adhesion CC of spermatocytes and spermatids to Sertoli cells and for their normal CC differentiation into mature spermatozoa (By similarity). Acts as a CC tumor suppressor in non-small-cell lung cancer (NSCLC) cells CC (PubMed:11279526, PubMed:12234973). May contribute to the less invasive CC phenotypes of lepidic growth tumor cells (PubMed:12920246). CC {ECO:0000250|UniProtKB:Q8R5M8, ECO:0000269|PubMed:11279526, CC ECO:0000269|PubMed:12050160, ECO:0000269|PubMed:12234973, CC ECO:0000269|PubMed:12920246, ECO:0000269|PubMed:15811952, CC ECO:0000269|PubMed:15905536, ECO:0000269|PubMed:22438059}. CC -!- SUBUNIT: Homodimer (via Ig-like V-type domain) (PubMed:12050160, CC PubMed:23871486). Interacts with FARP1 (By similarity). Interacts (via CC Ig-like V-type domain) with CRTAM (via Ig-like V-type domain); the CC interaction competes with CRTAM homodimerization and CADM1 CC homodimerization (PubMed:15811952, PubMed:15781451, PubMed:23871486). CC Interacts (via C-terminus) with EPB41L3/DAL1 (PubMed:12234973, CC PubMed:21131357). The interaction with EPB41L3/DAL1 may act to anchor CC CADM1 to the actin cytoskeleton (PubMed:12234973). Interacts (via C- CC terminus) with MPP2 (via PDZ domain) (By similarity). Interacts (via C- CC terminus) with MPP3 (via PDZ domain) (PubMed:13679854). Interacts (via CC C-terminus) with PALS2 (via PDZ domain) (By similarity). CC {ECO:0000250|UniProtKB:Q6AYP5, ECO:0000250|UniProtKB:Q8R5M8, CC ECO:0000269|PubMed:12050160, ECO:0000269|PubMed:12234973, CC ECO:0000269|PubMed:13679854, ECO:0000269|PubMed:15781451, CC ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:21131357, CC ECO:0000269|PubMed:23871486}. CC -!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8 proteins CC vFLIP and vGPCR; these interactions are essential for NF-kappa-B CC activation. {ECO:0000269|PubMed:29698475}. CC -!- INTERACTION: CC Q9BY67; O95727-1: CRTAM; NbExp=4; IntAct=EBI-5652260, EBI-16044697; CC Q9BY67; P60900: PSMA6; NbExp=3; IntAct=EBI-5652260, EBI-357793; CC Q9BY67; O35696: St8sia2; Xeno; NbExp=2; IntAct=EBI-5652260, EBI-15854779; CC Q9BY67; Q64690: ST8SIA4; Xeno; NbExp=2; IntAct=EBI-5652260, EBI-15854853; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11279526, CC ECO:0000269|PubMed:22438059}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:11279526}. Synapse {ECO:0000250|UniProtKB:Q8R5M8}. CC Note=Localized to the basolateral plasma membrane of epithelial cells CC in gall bladder. {ECO:0000250|UniProtKB:Q8R5M8}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1 {ECO:0000269|PubMed:15893517}; CC IsoId=Q9BY67-1; Sequence=Displayed; CC Name=2 {ECO:0000269|Ref.4}; CC IsoId=Q9BY67-2; Sequence=VSP_052461, VSP_052462; CC Name=3; CC IsoId=Q9BY67-3; Sequence=VSP_047406; CC Name=4; CC IsoId=Q9BY67-4; Sequence=VSP_047407; CC Name=5; Synonyms=E; CC IsoId=Q9BY67-5; Sequence=VSP_047405; CC -!- DOMAIN: The cytoplasmic domain appears to play a critical role in CC proapoptosis and tumor suppressor activity in NSCLC. CC {ECO:0000269|PubMed:14633730, ECO:0000269|PubMed:15184878}. CC -!- PTM: Glycosylation at Asn-67 and Asn-101 promotes adhesive binding and CC synapse induction. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI25103.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF132811; AAF69029.1; -; mRNA. DR EMBL; HE586496; CCD32610.1; -; mRNA. DR EMBL; HE586497; CCD32611.1; -; mRNA. DR EMBL; HE586498; CCD32612.1; -; mRNA. DR EMBL; HE586499; CCD32613.1; -; mRNA. DR EMBL; KJ534791; AHW56431.1; -; mRNA. DR EMBL; KJ534794; AHW56434.1; -; mRNA. DR EMBL; AB094146; BAC66178.1; -; mRNA. DR EMBL; AK075502; BAC11657.1; -; mRNA. DR EMBL; AP000462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003174; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003179; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005020; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC125102; AAI25103.1; ALT_FRAME; mRNA. DR CCDS; CCDS53711.1; -. [Q9BY67-5] DR CCDS; CCDS73398.1; -. [Q9BY67-4] DR CCDS; CCDS73399.1; -. [Q9BY67-3] DR CCDS; CCDS8373.1; -. [Q9BY67-1] DR RefSeq; NP_001091987.1; NM_001098517.1. [Q9BY67-5] DR RefSeq; NP_001287972.1; NM_001301043.1. [Q9BY67-3] DR RefSeq; NP_001287973.1; NM_001301044.1. [Q9BY67-4] DR RefSeq; NP_001287974.1; NM_001301045.1. DR RefSeq; NP_055148.3; NM_014333.3. [Q9BY67-1] DR PDB; 3BIN; X-ray; 2.30 A; B=400-411. DR PDB; 4H5S; X-ray; 1.70 A; B=45-144. DR PDBsum; 3BIN; -. DR PDBsum; 4H5S; -. DR AlphaFoldDB; Q9BY67; -. DR SMR; Q9BY67; -. DR BioGRID; 117218; 22. DR CORUM; Q9BY67; -. DR DIP; DIP-57599N; -. DR IntAct; Q9BY67; 19. DR MINT; Q9BY67; -. DR STRING; 9606.ENSP00000329797; -. DR GlyConnect; 1101; 11 N-Linked glycans (3 sites). DR GlyGen; Q9BY67; 12 sites, 11 N-linked glycans (3 sites). DR iPTMnet; Q9BY67; -. DR PhosphoSitePlus; Q9BY67; -. DR BioMuta; CADM1; -. DR DMDM; 150438862; -. DR CPTAC; CPTAC-1282; -. DR CPTAC; CPTAC-1283; -. DR CPTAC; CPTAC-2210; -. DR EPD; Q9BY67; -. DR jPOST; Q9BY67; -. DR MassIVE; Q9BY67; -. DR MaxQB; Q9BY67; -. DR PaxDb; Q9BY67; -. DR PeptideAtlas; Q9BY67; -. DR ProteomicsDB; 25359; -. DR ProteomicsDB; 38329; -. DR ProteomicsDB; 79594; -. [Q9BY67-1] DR ProteomicsDB; 79595; -. [Q9BY67-2] DR ABCD; Q9BY67; 13 sequenced antibodies. DR Antibodypedia; 32257; 660 antibodies from 39 providers. DR CPTC; Q9BY67; 2 antibodies. DR DNASU; 23705; -. DR Ensembl; ENST00000331581.11; ENSP00000329797.6; ENSG00000182985.18. [Q9BY67-3] DR Ensembl; ENST00000452722.7; ENSP00000395359.2; ENSG00000182985.18. [Q9BY67-1] DR Ensembl; ENST00000537058.5; ENSP00000439817.1; ENSG00000182985.18. [Q9BY67-4] DR Ensembl; ENST00000542447.6; ENSP00000439176.1; ENSG00000182985.18. [Q9BY67-5] DR GeneID; 23705; -. DR KEGG; hsa:23705; -. DR MANE-Select; ENST00000331581.11; ENSP00000329797.6; NM_001301043.2; NP_001287972.1. [Q9BY67-3] DR UCSC; uc001ppk.4; human. [Q9BY67-1] DR CTD; 23705; -. DR DisGeNET; 23705; -. DR GeneCards; CADM1; -. DR HGNC; HGNC:5951; CADM1. DR HPA; ENSG00000182985; Tissue enhanced (retina). DR MIM; 605686; gene. DR neXtProt; NX_Q9BY67; -. DR OpenTargets; ENSG00000182985; -. DR PharmGKB; PA29764; -. DR VEuPathDB; HostDB:ENSG00000182985; -. DR eggNOG; ENOG502R1KU; Eukaryota. DR GeneTree; ENSGT00940000156093; -. DR InParanoid; Q9BY67; -. DR OMA; TYDRMYT; -. DR OrthoDB; 716894at2759; -. DR PhylomeDB; Q9BY67; -. DR TreeFam; TF334317; -. DR PathwayCommons; Q9BY67; -. DR Reactome; R-HSA-418990; Adherens junctions interactions. DR Reactome; R-HSA-420597; Nectin/Necl trans heterodimerization. DR SignaLink; Q9BY67; -. DR SIGNOR; Q9BY67; -. DR BioGRID-ORCS; 23705; 8 hits in 1071 CRISPR screens. DR ChiTaRS; CADM1; human. DR EvolutionaryTrace; Q9BY67; -. DR GeneWiki; Cell_adhesion_molecule_1; -. DR GenomeRNAi; 23705; -. DR Pharos; Q9BY67; Tbio. DR PRO; PR:Q9BY67; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9BY67; protein. DR Bgee; ENSG00000182985; Expressed in paraflocculus and 216 other tissues. DR ExpressionAtlas; Q9BY67; baseline and differential. DR Genevisible; Q9BY67; HS. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB. DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0045202; C:synapse; IBA:GO_Central. DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl. DR GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0007420; P:brain development; IEA:Ensembl. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0008037; P:cell recognition; IDA:UniProtKB. DR GO; GO:0051606; P:detection of stimulus; IDA:UniProtKB. DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB. DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0120154; P:negative regulation of ERBB4 signaling pathway; IEA:Ensembl. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB. DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR GO; GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; IDA:UniProtKB. DR Gene3D; 2.60.40.10; -; 3. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR003585; Neurexin-like. DR Pfam; PF08205; C2-set_2; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00294; 4.1m; 1. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 3. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR PROSITE; PS50835; IG_LIKE; 3. DR AGR; HGNC:5951; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Cell adhesion; KW Cell membrane; Developmental protein; Differentiation; Disulfide bond; KW Glycoprotein; Host-virus interaction; Immunity; Immunoglobulin domain; KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal; KW Spermatogenesis; Synapse; Transmembrane; Transmembrane helix; KW Tumor suppressor. FT SIGNAL 1..44 FT /evidence="ECO:0000255" FT CHAIN 45..442 FT /note="Cell adhesion molecule 1" FT /evidence="ECO:0000255" FT /id="PRO_0000291968" FT TOPO_DOM 45..374 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 375..395 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 396..442 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 45..139 FT /note="Ig-like V-type" FT /evidence="ECO:0000255" FT DOMAIN 144..238 FT /note="Ig-like C2-type 1" FT /evidence="ECO:0000255" FT DOMAIN 243..329 FT /note="Ig-like C2-type 2" FT /evidence="ECO:0000255" FT MOD_RES 422 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8R5M8" FT MOD_RES 434 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8R5M8" FT CARBOHYD 67 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 101 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973" FT CARBOHYD 113 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973" FT CARBOHYD 165 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 304 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 308 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 64..124 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:23871486, ECO:0007744|PDB:4H5S" FT DISULFID 166..220 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 267..313 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 332..333 FT /note="DP -> GT (in isoform 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_052461" FT VAR_SEQ 333..360 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:24722188" FT /id="VSP_047405" FT VAR_SEQ 334..442 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_052462" FT VAR_SEQ 359 FT /note="T -> TDTTATTEPAVHGLTQLPNSAEELDSEDLS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:22438059" FT /id="VSP_047406" FT VAR_SEQ 359 FT /note="T -> TDTTATTEPAVH (in isoform 4)" FT /evidence="ECO:0000303|PubMed:22438059" FT /id="VSP_047407" FT VARIANT 285 FT /note="D -> E (in dbSNP:rs45525440)" FT /id="VAR_061309" FT MUTAGEN 406 FT /note="Y->A: Nearly abolishes EPB41L3 binding." FT /evidence="ECO:0000269|PubMed:21131357" FT MUTAGEN 408 FT /note="T->A: Strongly reduced affinity for EPB41L3." FT /evidence="ECO:0000269|PubMed:21131357" FT CONFLICT 13 FT /note="A -> V (in Ref. 2; CCD32613)" FT /evidence="ECO:0000305" FT CONFLICT 153 FT /note="K -> R (in Ref. 1; AAF69029)" FT /evidence="ECO:0000305" FT CONFLICT 333..359 FT /note="PPTTIPPPTTTTTTTTTTTTTILTIIT -> TTATTEPAVHGLTQLPNSAEE FT LDSEDLS (in Ref. 5; BAC11657)" FT /evidence="ECO:0000305" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:3BIN" SQ SEQUENCE 442 AA; 48509 MW; CDEDE1E0C08BDD3A CRC64; MASVVLPSGS QCAAAAAAAA PPGLRLRLLL LLFSAAALIP TGDGQNLFTK DVTVIEGEVA TISCQVNKSD DSVIQLLNPN RQTIYFRDFR PLKDSRFQLL NFSSSELKVS LTNVSISDEG RYFCQLYTDP PQESYTTITV LVPPRNLMID IQKDTAVEGE EIEVNCTAMA SKPATTIRWF KGNTELKGKS EVEEWSDMYT VTSQLMLKVH KEDDGVPVIC QVEHPAVTGN LQTQRYLEVQ YKPQVHIQMT YPLQGLTREG DALELTCEAI GKPQPVMVTW VRVDDEMPQH AVLSGPNLFI NNLNKTDNGT YRCEASNIVG KAHSDYMLYV YDPPTTIPPP TTTTTTTTTT TTTILTIITD SRAGEEGSIR AVDHAVIGGV VAVVVFAMLC LLIILGRYFA RHKGTYFTHE AKGADDAADA DTAIINAEGG QNNSEEKKEY FI // ID CRTAM_HUMAN Reviewed; 393 AA. AC O95727; Q59EI1; Q6IRX2; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 2. DT 14-DEC-2022, entry version 159. DE RecName: Full=Cytotoxic and regulatory T-cell molecule; DE AltName: Full=Class-I MHC-restricted T-cell-associated molecule; DE AltName: CD_antigen=CD355; DE Flags: Precursor; GN Name=CRTAM {ECO:0000312|EMBL:AAC80267.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC80267.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT RP ARG-321. RX PubMed=10811014; DOI=10.1002/jlb.67.5.725; RA Kennedy J., Vicari A.P., Saylor V., Zurawski S.M., Copeland N.G., RA Gilbert D.J., Jenkins N.A., Zlotnik A.; RT "A molecular analysis of NKT cells: identification of a class-I restricted RT T cell-associated molecule (CRTAM)."; RL J. Leukoc. Biol. 67:725-734(2000). RN [2] {ECO:0000305, ECO:0000312|EMBL:BAD93067.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain {ECO:0000312|EMBL:BAD93067.1}; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH70266.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-368. RC TISSUE=Peripheral blood {ECO:0000312|EMBL:AAH70266.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] {ECO:0000305} RP FUNCTION, INTERACTION WITH CADM1, AND TISSUE SPECIFICITY. RX PubMed=15811952; DOI=10.1182/blood-2005-02-0817; RA Boles K.S., Barchet W., Diacovo T., Cella M., Colonna M.; RT "The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell RT responses through the cell-surface receptor CRTAM."; RL Blood 106:779-786(2005). RN [5] {ECO:0000305} RP INTERACTION WITH CADM1. RX PubMed=15781451; DOI=10.1074/jbc.m502095200; RA Galibert L., Diemer G.S., Liu Z., Johnson R.S., Smith J.L., Walzer T., RA Comeau M.R., Rauch C.T., Wolfson M.F., Sorensen R.A., RA Van der Vuurst de Vries A.-R., Branstetter D.G., Koelling R.M., RA Scholler J., Fanslow W.C., Baum P.R., Derry J.M., Yan W.; RT "Nectin-like protein 2 defines a subset of T-cell zone dendritic cells and RT is a ligand for class-I-restricted T-cell-associated molecule."; RL J. Biol. Chem. 280:21955-21964(2005). RN [6] {ECO:0000305} RP TISSUE SPECIFICITY. RX PubMed=16300832; DOI=10.1016/j.jneuroim.2005.09.017; RA Patino-Lopez G., Hevezi P., Lee J., Willhite D., Verge G.M., Lechner S.M., RA Ortiz-Navarrete V., Zlotnik A.; RT "Human class-I restricted T cell associated molecule is highly expressed in RT the cerebellum and is a marker for activated NKT and CD8+ T lymphocytes."; RL J. Neuroimmunol. 171:145-155(2006). RN [7] {ECO:0007744|PDB:3RBG} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 18-117, SUBUNIT, AND DISULFIDE RP BOND. RX PubMed=23583034; DOI=10.1016/j.str.2013.02.022; RA Rubinstein R., Ramagopal U.A., Nathenson S.G., Almo S.C., Fiser A.; RT "Functional classification of immune regulatory proteins."; RL Structure 21:766-776(2013). RN [8] {ECO:0007744|PDB:4H5S} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 18-117, SUBUNIT, INTERACTION WITH RP CADM1, DISULFIDE BOND, AND MUTAGENESIS OF PHE-56; THR-57; LYS-67 AND RP TYR-101. RX PubMed=23871486; DOI=10.1016/j.str.2013.06.006; RA Zhang S., Lu G., Qi J., Li Y., Zhang Z., Zhang B., Fan Z., Yan J., RA Gao G.F.; RT "Competition of cell adhesion and immune recognition: insights into the RT interaction between CRTAM and nectin-like 2."; RL Structure 21:1430-1439(2013). CC -!- FUNCTION: Mediates heterophilic cell-cell adhesion which regulates the CC activation, differentiation and tissue retention of various T-cell CC subsets (By similarity). Interaction with CADM1 promotes natural killer CC (NK) cell cytotoxicity and IFNG/interferon-gamma secretion by CD8+ T- CC cells in vitro as well as NK cell-mediated rejection of tumors CC expressing CADM1 in vivo (PubMed:15811952). Regulates CD8+ T-cell CC proliferation in response to T-cell receptor (TCR) activation (By CC similarity). Appears to be dispensable for CD8+ T-cell-mediated CC cytotoxicity (By similarity). Interaction with SCRIB promotes the late CC phase of cellular polarization of a subset of CD4+ T-cells, which in CC turn regulates TCR-mediated proliferation and IFNG, IL17 and IL22 CC production (By similarity). By interacting with CADM1 on CD8+ dendritic CC cells, regulates the retention of activated CD8+ T-cells within the CC draining lymph node (By similarity). Required for the intestinal CC retention of intraepithelial CD4+ CD8+ T-cells and, to a lesser extent, CC intraepithelial and lamina propria CD8+ T-cells and CD4+ T-cells (By CC similarity). Interaction with CADM1 promotes the adhesion to gut- CC associated CD103+ dendritic cells, which may facilitate the expression CC of gut-homing and adhesion molecules on T-cells and the conversion of CC CD4+ T-cells into CD4+ CD8+ T-cells (By similarity). CC {ECO:0000250|UniProtKB:Q149L7, ECO:0000269|PubMed:15811952}. CC -!- SUBUNIT: Monomer (PubMed:23583034). May form homodimer (via Ig-like V- CC type domain) (PubMed:23583034, PubMed:23871486). Interacts (via Ig-like CC V-type domain) with CADM1 (via Ig-like V-type domain); the interaction CC competes with CRTAM homodimerization and CADM1 homodimerization CC (PubMed:15781451, PubMed:15811952, PubMed:23871486). Interacts (via CC PDZ-binding motif) with SCRIB (via PDZ domain 3); the interaction CC promotes CRTAM and SCRIB polarization in a subset of CD4+ T-cells (By CC similarity). {ECO:0000250|UniProtKB:Q149L7, CC ECO:0000269|PubMed:15781451, ECO:0000269|PubMed:15811952, CC ECO:0000269|PubMed:23583034, ECO:0000269|PubMed:23871486}. CC -!- INTERACTION: CC O95727-1; Q9BY67: CADM1; NbExp=4; IntAct=EBI-16044697, EBI-5652260; CC O95727-1; O95727-1: CRTAM; NbExp=5; IntAct=EBI-16044697, EBI-16044697; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q149L7}; CC Single-pass type I membrane protein {ECO:0000255}. Note=In a subset of CC CD4+ T-cells, colocalizes with SCRIB at the immunological synapse CC during the late phase of T-cell activation. CC {ECO:0000250|UniProtKB:Q149L7}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000269|PubMed:10811014}; CC IsoId=O95727-1; Sequence=Displayed; CC Name=2; CC IsoId=O95727-2; Sequence=VSP_052471, VSP_052472; CC -!- TISSUE SPECIFICITY: In the immune system, expression is restricted to CC activated class-I MHC-restricted cells, including NKT and CD8 T-cells CC (PubMed:10811014, PubMed:15811952, PubMed:16300832). Strongly expressed CC in spleen, thymus, small intestine, peripheral blood leukocyte, and in CC Purkinje neurons in cerebellum. Expressed at much lower levels in CC testis, ovary, colon, lung and lymphoid tissues (PubMed:16300832). CC {ECO:0000269|PubMed:10811014, ECO:0000269|PubMed:15811952, CC ECO:0000269|PubMed:16300832}. CC -!- DOMAIN: The extracellular domain is required for the regulation of IFNG CC and IL22 production, but is dispensable for late T-cell polarization. CC {ECO:0000250|UniProtKB:Q149L7}. CC -!- SIMILARITY: Belongs to the nectin family. CC {ECO:0000269|PubMed:16300832}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD93067.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF001622; AAC80267.1; -; mRNA. DR EMBL; AB209830; BAD93067.1; ALT_INIT; mRNA. DR EMBL; BC070266; AAH70266.1; -; mRNA. DR CCDS; CCDS76489.1; -. [O95727-2] DR CCDS; CCDS8437.1; -. [O95727-1] DR RefSeq; NP_001291711.1; NM_001304782.1. [O95727-2] DR RefSeq; NP_062550.2; NM_019604.3. [O95727-1] DR PDB; 3RBG; X-ray; 2.30 A; A/B/C/D=18-117. DR PDB; 4H5S; X-ray; 1.70 A; A=18-117. DR PDBsum; 3RBG; -. DR PDBsum; 4H5S; -. DR AlphaFoldDB; O95727; -. DR SMR; O95727; -. DR DIP; DIP-60155N; -. DR IntAct; O95727; 1. DR STRING; 9606.ENSP00000227348; -. DR GlyGen; O95727; 5 sites, 2 Thr glycans (2 sites). DR iPTMnet; O95727; -. DR PhosphoSitePlus; O95727; -. DR BioMuta; CRTAM; -. DR MassIVE; O95727; -. DR PaxDb; O95727; -. DR PeptideAtlas; O95727; -. DR ProteomicsDB; 51015; -. [O95727-1] DR ProteomicsDB; 51016; -. [O95727-2] DR Antibodypedia; 32807; 268 antibodies from 24 providers. DR DNASU; 56253; -. DR Ensembl; ENST00000227348.9; ENSP00000227348.4; ENSG00000109943.9. [O95727-1] DR Ensembl; ENST00000533709.1; ENSP00000433728.1; ENSG00000109943.9. [O95727-2] DR GeneID; 56253; -. DR KEGG; hsa:56253; -. DR MANE-Select; ENST00000227348.9; ENSP00000227348.4; NM_019604.4; NP_062550.2. DR UCSC; uc001pyj.4; human. [O95727-1] DR CTD; 56253; -. DR DisGeNET; 56253; -. DR GeneCards; CRTAM; -. DR HGNC; HGNC:24313; CRTAM. DR HPA; ENSG00000109943; Tissue enriched (brain). DR MIM; 612597; gene. DR neXtProt; NX_O95727; -. DR OpenTargets; ENSG00000109943; -. DR PharmGKB; PA145149072; -. DR VEuPathDB; HostDB:ENSG00000109943; -. DR eggNOG; ENOG502RYH2; Eukaryota. DR GeneTree; ENSGT00940000159804; -. DR HOGENOM; CLU_061397_0_0_1; -. DR InParanoid; O95727; -. DR OMA; AFLTNHT; -. DR OrthoDB; 753787at2759; -. DR PhylomeDB; O95727; -. DR TreeFam; TF326804; -. DR PathwayCommons; O95727; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR SignaLink; O95727; -. DR BioGRID-ORCS; 56253; 10 hits in 1058 CRISPR screens. DR ChiTaRS; CRTAM; human. DR EvolutionaryTrace; O95727; -. DR GenomeRNAi; 56253; -. DR Pharos; O95727; Tbio. DR PRO; PR:O95727; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; O95727; protein. DR Bgee; ENSG00000109943; Expressed in cerebellar vermis and 113 other tissues. DR Genevisible; O95727; HS. DR GO; GO:0001772; C:immunological synapse; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HGNC-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0008037; P:cell recognition; IDA:HGNC-UCL. DR GO; GO:0051606; P:detection of stimulus; IDA:HGNC-UCL. DR GO; GO:0002355; P:detection of tumor cell; IDA:HGNC-UCL. DR GO; GO:0001768; P:establishment of T cell polarity; ISS:UniProtKB. DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB. DR GO; GO:0097021; P:lymphocyte migration into lymphoid organs; ISS:UniProtKB. DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; ISS:UniProtKB. DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:HGNC-UCL. DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:HGNC-UCL. DR GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IDA:HGNC-UCL. DR GO; GO:0032729; P:positive regulation of type II interferon production; ISS:UniProtKB. DR GO; GO:2001185; P:regulation of CD8-positive, alpha-beta T cell activation; ISS:UniProtKB. DR GO; GO:0050863; P:regulation of T cell activation; ISS:UniProtKB. DR GO; GO:0045580; P:regulation of T cell differentiation; ISS:UniProtKB. DR Gene3D; 2.60.40.10; -; 2. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR Pfam; PF08205; C2-set_2; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 2. DR AGR; HGNC:24313; -. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Alternative splicing; Cell adhesion; KW Cell membrane; Disulfide bond; Glycoprotein; Immunity; KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..17 FT /evidence="ECO:0000255" FT CHAIN 18..393 FT /note="Cytotoxic and regulatory T-cell molecule" FT /id="PRO_0000292602" FT TOPO_DOM 18..287 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 288..308 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 309..393 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 18..114 FT /note="Ig-like V-type" FT /evidence="ECO:0000255" FT DOMAIN 118..210 FT /note="Ig-like C2-type" FT /evidence="ECO:0000255" FT REGION 225..273 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 328..354 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 374..393 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 390..393 FT /note="PDZ-binding" FT /evidence="ECO:0000250|UniProtKB:Q149L7" FT COMPBIAS 228..251 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 252..267 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 328..347 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 21 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 87 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 178 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 38..98 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:23583034, ECO:0000269|PubMed:23871486, FT ECO:0007744|PDB:3RBG, ECO:0007744|PDB:4H5S" FT DISULFID 141..196 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1..199 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_052471" FT VAR_SEQ 200..216 FT /note="HRGLQGRKLVAPFRFED -> MWVKLLSIVAEFCFSPF (in isoform FT 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_052472" FT VARIANT 16 FT /note="E -> A (in dbSNP:rs35411582)" FT /id="VAR_049868" FT VARIANT 78 FT /note="A -> D (in dbSNP:rs34397316)" FT /id="VAR_049869" FT VARIANT 173 FT /note="D -> G (in dbSNP:rs35136295)" FT /id="VAR_049870" FT VARIANT 321 FT /note="K -> R (in dbSNP:rs2272094)" FT /evidence="ECO:0000269|PubMed:10811014" FT /id="VAR_032999" FT VARIANT 368 FT /note="A -> G (in dbSNP:rs1916036)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_033000" FT MUTAGEN 56 FT /note="F->A: Reduced binding to CADM1. Severely impairs FT interaction with CADM1; when associated with A-57, A-67 and FT A-101." FT /evidence="ECO:0000269|PubMed:23871486" FT MUTAGEN 57 FT /note="T->A: Reduced binding to CADM1. Severely impairs FT interaction with CADM1; when associated with A-56, A-67 and FT A-101." FT /evidence="ECO:0000269|PubMed:23871486" FT MUTAGEN 67 FT /note="K->A: Reduced binding to CADM1. Severely impairs FT interaction with CADM1; when associated with A-56, A-57 and FT A-101." FT /evidence="ECO:0000269|PubMed:23871486" FT MUTAGEN 101 FT /note="Y->A: Reduced binding to CADM1. Severely impairs FT interaction with CADM1; when associated with A-56, A-57 and FT A-67." FT /evidence="ECO:0000269|PubMed:23871486" FT CONFLICT 65 FT /note="A -> V (in Ref. 3; AAH70266)" FT /evidence="ECO:0000305" FT CONFLICT 315 FT /note="A -> T (in Ref. 3; AAH70266)" FT /evidence="ECO:0000305" FT STRAND 22..29 FT /evidence="ECO:0007829|PDB:3RBG" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:3RBG" FT STRAND 47..51 FT /evidence="ECO:0007829|PDB:3RBG" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:3RBG" FT STRAND 72..77 FT /evidence="ECO:0007829|PDB:3RBG" FT STRAND 80..87 FT /evidence="ECO:0007829|PDB:3RBG" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:3RBG" FT STRAND 94..115 FT /evidence="ECO:0007829|PDB:3RBG" SQ SEQUENCE 393 AA; 44641 MW; CB8173032EE45F03 CRC64; MWWRVLSLLA WFPLQEASLT NHTETITVEE GQTLTLKCVT SLRKNSSLQW LTPSGFTIFL NEYPALKNSK YQLLHHSANQ LSITVPNVTL QDEGVYKCLH YSDSVSTKEV KVIVLATPFK PILEASVIRK QNGEEHVVLM CSTMRSKPPP QITWLLGNSM EVSGGTLHEF ETDGKKCNTT STLIIHTYGK NSTVDCIIRH RGLQGRKLVA PFRFEDLVTD EETASDALER NSLSSQDPQQ PTSTVSVTED SSTSEIDKEE KEQTTQDPDL TTEANPQYLG LARKKSGILL LTLVSFLIFI LFIIVQLFIM KLRKAHVIWK KENEVSEHTL ESYRSRSNNE ETSSEEKNGQ SSHPMRCMNY ITKLYSEAKT KRKENVQHSK LEEKHIQVPE SIV // ID FARP1_HUMAN Reviewed; 1045 AA. AC Q9Y4F1; Q5JVI9; Q6IQ29; DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 14-DEC-2022, entry version 181. DE RecName: Full=FERM, ARHGEF and pleckstrin domain-containing protein 1; DE AltName: Full=Chondrocyte-derived ezrin-like protein; DE AltName: Full=FERM, RhoGEF and pleckstrin domain-containing protein 1; DE AltName: Full=Pleckstrin homology domain-containing family C member 2; DE Short=PH domain-containing family C member 2; GN Name=FARP1; Synonyms=CDEP, PLEKHC2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND TISSUE SPECIFICITY. RC TISSUE=Cartilage; RX PubMed=9425278; DOI=10.1006/bbrc.1997.7826; RA Koyano Y., Kawamoto T., Shen M., Yan W., Noshiro M., Fujii K., Kato Y.; RT "Molecular cloning and characterization of CDEP, a novel human protein RT containing the ezrin-like domain of the band 4.1 superfamily and the Dbl RT homology domain of rho guanine nucleotide exchange factors."; RL Biochem. Biophys. Res. Commun. 241:369-375(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Brain, Placenta, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24 AND SER-340, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-889, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-427; SER-510 AND RP SER-514, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872 AND SER-889, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-403; SER-418; RP SER-427; SER-833; SER-872; THR-883 AND SER-889, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP X-RAY CRYSTALLOGRAPHY (4.09 ANGSTROMS) OF 539-1035, AND DOMAIN. RX PubMed=23375260; DOI=10.1016/j.str.2013.01.001; RA He X., Kuo Y.C., Rosche T.J., Zhang X.; RT "Structural basis for autoinhibition of the guanine nucleotide exchange RT factor FARP2."; RL Structure 21:355-364(2013). RN [16] RP VARIANT [LARGE SCALE ANALYSIS] LEU-714. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Functions as guanine nucleotide exchange factor for RAC1. May CC play a role in semaphorin signaling. Plays a role in the assembly and CC disassembly of dendritic filopodia, the formation of dendritic spines, CC regulation of dendrite length and ultimately the formation of synapses CC (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with CADM1. Interacts with RAC1 (By similarity). CC {ECO:0000250}. CC -!- INTERACTION: CC Q9Y4F1; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-5235630, EBI-357318; CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. Synapse. Synapse, synaptosome {ECO:0000250}. CC Cytoplasm, cytosol {ECO:0000250}. Cell projection, filopodium CC {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell CC projection, dendritic spine {ECO:0000250}. Note=Recruited to the cell CC membrane via interaction with CADM1. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9Y4F1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y4F1-2; Sequence=VSP_017976; CC Name=3; CC IsoId=Q9Y4F1-3; Sequence=VSP_040989, VSP_040990; CC -!- TISSUE SPECIFICITY: Detected in cAMP-treated chondrocytes, but not in CC untreated chondrocytes. Detected in fetal brain, heart and spleen, and CC in adult testis, kidney and lung. {ECO:0000269|PubMed:9425278}. CC -!- INDUCTION: Up-regulated in response to cAMP in cultured embryonic CC chondrocytes. {ECO:0000269|PubMed:9425278}. CC -!- DOMAIN: Intramolecular interaction between the DH domain and the PH CC domains can stabilize the protein in an autoinhibited conformation. CC {ECO:0000269|PubMed:23375260}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB008430; BAA24267.1; -; mRNA. DR EMBL; AL136300; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137249; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL161896; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL445223; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC041595; AAH41595.1; -; mRNA. DR EMBL; BC065020; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC071592; AAH71592.1; -; mRNA. DR CCDS; CCDS32000.1; -. [Q9Y4F1-3] DR CCDS; CCDS66572.1; -. [Q9Y4F1-2] DR CCDS; CCDS9487.1; -. [Q9Y4F1-1] DR PIR; JC5795; JC5795. DR RefSeq; NP_001001715.2; NM_001001715.3. [Q9Y4F1-3] DR RefSeq; NP_001273768.1; NM_001286839.1. DR RefSeq; NP_005757.1; NM_005766.3. [Q9Y4F1-1] DR RefSeq; XP_016875801.1; XM_017020312.1. [Q9Y4F1-1] DR PDB; 4H6Y; X-ray; 4.09 A; A/B=539-1035. DR PDBsum; 4H6Y; -. DR AlphaFoldDB; Q9Y4F1; -. DR SMR; Q9Y4F1; -. DR BioGRID; 115462; 131. DR IntAct; Q9Y4F1; 55. DR MINT; Q9Y4F1; -. DR STRING; 9606.ENSP00000471242; -. DR CarbonylDB; Q9Y4F1; -. DR iPTMnet; Q9Y4F1; -. DR PhosphoSitePlus; Q9Y4F1; -. DR BioMuta; FARP1; -. DR DMDM; 74762059; -. DR EPD; Q9Y4F1; -. DR jPOST; Q9Y4F1; -. DR MassIVE; Q9Y4F1; -. DR MaxQB; Q9Y4F1; -. DR PaxDb; Q9Y4F1; -. DR PeptideAtlas; Q9Y4F1; -. DR ProteomicsDB; 86186; -. [Q9Y4F1-1] DR ProteomicsDB; 86187; -. [Q9Y4F1-2] DR ProteomicsDB; 86188; -. [Q9Y4F1-3] DR Antibodypedia; 619; 216 antibodies from 19 providers. DR DNASU; 10160; -. DR Ensembl; ENST00000319562.11; ENSP00000322926.6; ENSG00000152767.17. [Q9Y4F1-1] DR Ensembl; ENST00000376581.9; ENSP00000365765.4; ENSG00000152767.17. [Q9Y4F1-3] DR GeneID; 10160; -. DR KEGG; hsa:10160; -. DR MANE-Select; ENST00000319562.11; ENSP00000322926.6; NM_005766.4; NP_005757.1. DR UCSC; uc001vni.5; human. [Q9Y4F1-1] DR CTD; 10160; -. DR DisGeNET; 10160; -. DR GeneCards; FARP1; -. DR HGNC; HGNC:3591; FARP1. DR HPA; ENSG00000152767; Low tissue specificity. DR MIM; 602654; gene. DR neXtProt; NX_Q9Y4F1; -. DR OpenTargets; ENSG00000152767; -. DR PharmGKB; PA28004; -. DR VEuPathDB; HostDB:ENSG00000152767; -. DR eggNOG; KOG3531; Eukaryota. DR GeneTree; ENSGT00940000155318; -. DR HOGENOM; CLU_012301_0_0_1; -. DR InParanoid; Q9Y4F1; -. DR OrthoDB; 476668at2759; -. DR PhylomeDB; Q9Y4F1; -. DR TreeFam; TF351276; -. DR PathwayCommons; Q9Y4F1; -. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9035034; RHOF GTPase cycle. DR SignaLink; Q9Y4F1; -. DR BioGRID-ORCS; 10160; 14 hits in 1069 CRISPR screens. DR ChiTaRS; FARP1; human. DR GeneWiki; FARP1; -. DR GenomeRNAi; 10160; -. DR Pharos; Q9Y4F1; Tbio. DR PRO; PR:Q9Y4F1; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q9Y4F1; protein. DR Bgee; ENSG00000152767; Expressed in renal medulla and 202 other tissues. DR ExpressionAtlas; Q9Y4F1; baseline and differential. DR Genevisible; Q9Y4F1; HS. DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0030425; C:dendrite; ISS:UniProtKB. DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell. DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB. DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IEA:Ensembl. DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl. DR GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB. DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IEA:Ensembl. DR GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl. DR GO; GO:0098942; P:retrograde trans-synaptic signaling by trans-synaptic protein complex; IEA:Ensembl. DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB. DR CDD; cd14473; FERM_B-lobe; 1. DR CDD; cd13193; FERM_C_FARP1-like; 1. DR CDD; cd00160; RhoGEF; 1. DR DisProt; DP02833; -. DR Gene3D; 1.20.80.10; -; 1. DR Gene3D; 1.20.900.10; -; 1. DR Gene3D; 2.30.29.30; -; 3. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR035899; DBL_dom_sf. DR InterPro; IPR000219; DH-domain. DR InterPro; IPR000798; Ez/rad/moesin-like. DR InterPro; IPR041788; FARP1/FARP2/FRMD7_FERM_C. DR InterPro; IPR014847; FERM-adjacent. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf. DR InterPro; IPR035963; FERM_2. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR019747; FERM_CS. DR InterPro; IPR000299; FERM_domain. DR InterPro; IPR018979; FERM_N. DR InterPro; IPR018980; FERM_PH-like_C. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR Pfam; PF08736; FA; 1. DR Pfam; PF09380; FERM_C; 1. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF09379; FERM_N; 1. DR Pfam; PF00169; PH; 2. DR Pfam; PF00621; RhoGEF; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR SMART; SM01195; FA; 1. DR SMART; SM01196; FERM_C; 1. DR SMART; SM00233; PH; 2. DR SMART; SM00325; RhoGEF; 1. DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1. DR SUPFAM; SSF47031; Second domain of FERM; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS50057; FERM_3; 1. DR PROSITE; PS50003; PH_DOMAIN; 2. DR AGR; HGNC:3591; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cell projection; KW Cytoplasm; Developmental protein; Guanine-nucleotide releasing factor; KW Membrane; Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome. FT CHAIN 1..1045 FT /note="FERM, ARHGEF and pleckstrin domain-containing FT protein 1" FT /id="PRO_0000232753" FT DOMAIN 40..320 FT /note="FERM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084" FT DOMAIN 540..730 FT /note="DH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062" FT DOMAIN 759..856 FT /note="PH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 932..1029 FT /note="PH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 361..534 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 864..903 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 16..30 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 371..401 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 460..515 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:F8VPU2" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:F8VPU2" FT MOD_RES 24 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 340 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 373 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 389 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:F8VPU2" FT MOD_RES 403 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 418 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 427 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 433 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:F8VPU2" FT MOD_RES 510 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 514 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 833 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 872 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 878 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:F8VPU2" FT MOD_RES 883 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 889 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 896 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:F8VPU2" FT MOD_RES 899 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:F8VPU2" FT VAR_SEQ 58..129 FT /note="QRAPGKVLLDAVCNHLNLVEGDYFGLEFPDHKKITVWLDLLKPIVKQIRRPK FT HVVVKFVVKFFPPDHTQLQE -> MVSSSSFLKATGSSWTGWVLRCSMKPKHHSHLIEK FT FGEDRILTHLTGSISYTNWAGSRSLAVTVTEELLNLF (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040989" FT VAR_SEQ 130..1045 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040990" FT VAR_SEQ 758 FT /note="R -> RPGSFSLMRTPHLGQARRIPCAPERRPLLLVK (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017976" FT VARIANT 8 FT /note="P -> L (in dbSNP:rs9300466)" FT /id="VAR_048362" FT VARIANT 714 FT /note="R -> L (in a breast cancer sample; somatic mutation; FT dbSNP:rs1458028855)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035851" FT CONFLICT 644 FT /note="H -> Y (in Ref. 3; AAH71592)" FT /evidence="ECO:0000305" SQ SEQUENCE 1045 AA; 118633 MW; 0E8B2D61C0F58417 CRC64; MGEIEQRPTP GSRLGAPENS GISTLERGQK PPPTPSGKLV SIKIQMLDDT QEAFEVPQRA PGKVLLDAVC NHLNLVEGDY FGLEFPDHKK ITVWLDLLKP IVKQIRRPKH VVVKFVVKFF PPDHTQLQEE LTRYLFALQV KQDLAQGRLT CNDTSAALLI SHIVQSEIGD FDEALDREHL AKNKYIPQQD ALEDKIVEFH HNHIGQTPAE SDFQLLEIAR RLEMYGIRLH PAKDREGTKI NLAVANTGIL VFQGFTKINA FNWAKVRKLS FKRKRFLIKL RPDANSAYQD TLEFLMASRD FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY VKEGGHKKVQ FERKHSKIHS IRSLASQPTE LNSEVLEQSQ QSTSLTFGEG AESPGGQSCR RGKEPKVSAG EPGSHPSPAP RRSPAGNKQA DGAASAPTEE EEEVVKDRTQ QSKPQPPQPS TGSLTGSPHL SELSVNSQGG VAPANVTLSP NLSPDTKQAS PLISPLLNDQ ACPRTDDEDE GRRKRFPTDK AYFIAKEVST TERTYLKDLE VITSWFQSTV SKEDAMPEAL KSLIFPNFEP LHKFHTNFLK EIEQRLALWE GRSNAQIRDY QRIGDVMLKN IQGMKHLAAH LWKHSEALEA LENGIKSSRR LENFCRDFEL QKVCYLPLNT FLLRPLHRLM HYKQVLERLC KHHPPSHADF RDCRAALAEI TEMVAQLHGT MIKMENFQKL HELKKDLIGI DNLVVPGREF IRLGSLSKLS GKGLQQRMFF LFNDVLLYTS RGLTASNQFK VHGQLPLYGM TIEESEDEWG VPHCLTLRGQ RQSIIVAASS RSEMEKWVED IQMAIDLAEK SSSPAPEFLA SSPPDNKSPD EATAADQESE DDLSASRTSL ERQAPHRGNT MVHVCWHRNT SVSMVDFSIA VENQLSGNLL RKFKNSNGWQ KLWVVFTNFC LFFYKSHQDN HPLASLPLLG YSLTIPSESE NIQKDYVFKL HFKSHVYYFR AESEYTFERW MEVIRSATSS ASRPHVLSHK ESLVY // ID MPP2_HUMAN Reviewed; 576 AA. AC Q14168; B4DGE9; B4DRJ0; B7Z3G8; E7EV80; E7EV91; E7EX01; Q53ES9; Q5CZB9; AC Q9BQJ2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 02-MAR-2010, sequence version 3. DT 14-DEC-2022, entry version 197. DE RecName: Full=MAGUK p55 subfamily member 2; DE AltName: Full=Discs large homolog 2; DE AltName: Full=Protein MPP2; GN Name=MPP2 {ECO:0000312|HGNC:HGNC:7220}; Synonyms=DLG2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=7590743; DOI=10.1006/geno.1995.1101; RA Mazoyer S., Gayther S.A., Nagai M.A., Smith S.A., Dunning A., RA van Rensburg E.J., Albertsen H., White R., Ponder B.A.J.; RT "A gene (DLG2) located at 17q12-q21 encodes a new homologue of the RT Drosophila tumor suppressor dlg-A."; RL Genomics 28:25-31(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Amygdala; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6). RC TISSUE=Amygdala, and Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Salivary gland; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [9] RP FUNCTION, INTERACTION WITH SRC, SUBCELLULAR LOCATION, MUTAGENESIS OF RP TYR-363, AND PHOSPHORYLATION. RX PubMed=19665017; DOI=10.1016/j.yexcr.2009.07.028; RA Baumgartner M., Weiss A., Fritzius T., Heinrich J., Moelling K.; RT "The PDZ protein MPP2 interacts with c-Src in epithelial cells."; RL Exp. Cell Res. 315:2888-2898(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP STRUCTURE BY NMR OF 163-240. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the PDZ domain from human maguk p55 subfamily member RT 2."; RL Submitted (JAN-2008) to the PDB data bank. CC -!- FUNCTION: Postsynaptic MAGUK scaffold protein that links CADM1 cell CC adhesion molecules to core components of the postsynaptic density (By CC similarity). In CA1 pyramidal neurons, required for synaptic KCNN2- CC containing channel function and long-term potentiation expression (By CC similarity). Seems to negatively regulate SRC function in epithelial CC cells (PubMed:19665017). {ECO:0000250|UniProtKB:D3ZAA9, CC ECO:0000250|UniProtKB:Q9WV34, ECO:0000269|PubMed:19665017}. CC -!- SUBUNIT: Can homomultimerise. Interacts with CACNG2. Interacts (via the CC SH3-Guanylate kinase-like sub-module) with DLG4/PSD95 and DLGAP1/GKAP. CC Interacts (via the PDZ domain) with CADM1 (via C-terminus) (By CC similarity). Interacts with KCNN2/SK2 (via N-terminal domain) (By CC similarity). Interacts with SRC (PubMed:19665017). CC {ECO:0000250|UniProtKB:D3ZAA9, ECO:0000250|UniProtKB:Q9WV34, CC ECO:0000269|PubMed:19665017}. CC -!- INTERACTION: CC Q14168-2; O14910: LIN7A; NbExp=4; IntAct=EBI-10181752, EBI-2513988; CC Q14168-4; O14910: LIN7A; NbExp=7; IntAct=EBI-14385193, EBI-2513988; CC Q14168-4; Q9HAP6: LIN7B; NbExp=3; IntAct=EBI-14385193, EBI-821335; CC Q14168-4; Q9NUP9: LIN7C; NbExp=7; IntAct=EBI-14385193, EBI-1171517; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:19665017}. Membrane {ECO:0000269|PubMed:19665017}. CC Cell projection, dendrite {ECO:0000250|UniProtKB:Q9WV34}. Postsynaptic CC density {ECO:0000250|UniProtKB:Q9WV34}. Note=Prominently expressed in CC the postsynaptic densities of dendritic spines, is also detected in CC dendritic shafts. {ECO:0000250|UniProtKB:Q9WV34}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q14168-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14168-2; Sequence=VSP_003156; CC Name=3; CC IsoId=Q14168-3; Sequence=VSP_022951, VSP_003156; CC Name=4; CC IsoId=Q14168-4; Sequence=VSP_055138, VSP_003156; CC Name=5; CC IsoId=Q14168-5; Sequence=VSP_055136; CC Name=6; CC IsoId=Q14168-6; Sequence=VSP_055137, VSP_003156; CC -!- PTM: Phosphorylated by SRC. {ECO:0000269|PubMed:19665017}. CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X82895; CAA58067.1; -; mRNA. DR EMBL; AL136554; CAB66489.1; -; mRNA. DR EMBL; AK294564; BAG57760.1; -; mRNA. DR EMBL; AK295858; BAH12204.1; -; mRNA. DR EMBL; AK299286; BAG61302.1; -; mRNA. DR EMBL; CR936598; CAI56746.1; -; mRNA. DR EMBL; AK223560; BAD97280.1; -; mRNA. DR EMBL; AC007993; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC030287; AAH30287.1; -; mRNA. DR CCDS; CCDS11471.1; -. [Q14168-2] DR CCDS; CCDS62206.1; -. [Q14168-5] DR CCDS; CCDS62207.1; -. [Q14168-6] DR CCDS; CCDS62208.1; -. [Q14168-3] DR CCDS; CCDS62209.1; -. [Q14168-1] DR CCDS; CCDS62210.1; -. [Q14168-4] DR PIR; A57653; A57653. DR RefSeq; NP_001265299.1; NM_001278370.1. DR RefSeq; NP_001265300.1; NM_001278371.1. DR RefSeq; NP_001265301.1; NM_001278372.1. DR RefSeq; NP_001265302.1; NM_001278373.1. DR RefSeq; NP_001265303.1; NM_001278374.1. [Q14168-5] DR RefSeq; NP_001265304.1; NM_001278375.1. DR RefSeq; NP_001265305.2; NM_001278376.2. DR RefSeq; NP_001265310.1; NM_001278381.1. DR RefSeq; NP_005365.4; NM_005374.4. DR PDB; 2E7K; NMR; -; A=163-240. DR PDBsum; 2E7K; -. DR AlphaFoldDB; Q14168; -. DR BMRB; Q14168; -. DR SMR; Q14168; -. DR BioGRID; 110495; 36. DR IntAct; Q14168; 17. DR MINT; Q14168; -. DR STRING; 9606.ENSP00000428182; -. DR iPTMnet; Q14168; -. DR PhosphoSitePlus; Q14168; -. DR SwissPalm; Q14168; -. DR BioMuta; MPP2; -. DR DMDM; 290457681; -. DR EPD; Q14168; -. DR jPOST; Q14168; -. DR MassIVE; Q14168; -. DR MaxQB; Q14168; -. DR PaxDb; Q14168; -. DR PeptideAtlas; Q14168; -. DR ProteomicsDB; 18580; -. DR ProteomicsDB; 18587; -. DR ProteomicsDB; 18952; -. DR ProteomicsDB; 59895; -. [Q14168-1] DR ProteomicsDB; 59896; -. [Q14168-2] DR ProteomicsDB; 59897; -. [Q14168-3] DR TopDownProteomics; Q14168-2; -. [Q14168-2] DR Antibodypedia; 17305; 222 antibodies from 25 providers. DR DNASU; 4355; -. DR Ensembl; ENST00000520305.5; ENSP00000428136.1; ENSG00000108852.16. [Q14168-5] DR GeneID; 4355; -. DR KEGG; hsa:4355; -. DR UCSC; uc010win.3; human. [Q14168-1] DR CTD; 4355; -. DR DisGeNET; 4355; -. DR GeneCards; MPP2; -. DR HGNC; HGNC:7220; MPP2. DR HPA; ENSG00000108852; Tissue enhanced (brain). DR MIM; 600723; gene. DR neXtProt; NX_Q14168; -. DR OpenTargets; ENSG00000108852; -. DR PharmGKB; PA30925; -. DR VEuPathDB; HostDB:ENSG00000108852; -. DR eggNOG; KOG0609; Eukaryota. DR GeneTree; ENSGT00940000155348; -. DR HOGENOM; CLU_001715_5_1_1; -. DR InParanoid; Q14168; -. DR OrthoDB; 847888at2759; -. DR PhylomeDB; Q14168; -. DR TreeFam; TF314263; -. DR PathwayCommons; Q14168; -. DR SignaLink; Q14168; -. DR BioGRID-ORCS; 4355; 22 hits in 1073 CRISPR screens. DR ChiTaRS; MPP2; human. DR EvolutionaryTrace; Q14168; -. DR GeneWiki; MPP2; -. DR GenomeRNAi; 4355; -. DR Pharos; Q14168; Tbio. DR PRO; PR:Q14168; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q14168; protein. DR Bgee; ENSG00000108852; Expressed in C1 segment of cervical spinal cord and 147 other tissues. DR ExpressionAtlas; Q14168; baseline and differential. DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB. DR GO; GO:0032590; C:dendrite membrane; ISS:UniProtKB. DR GO; GO:0043198; C:dendritic shaft; ISS:UniProtKB. DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB. DR GO; GO:0060079; P:excitatory postsynaptic potential; ISS:UniProtKB. DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB. DR CDD; cd12037; SH3_MPP2; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR014775; L27_C. DR InterPro; IPR004172; L27_dom. DR InterPro; IPR036892; L27_dom_sf. DR InterPro; IPR035602; MPP2_SH3. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF02828; L27; 2. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF07653; SH3_2; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM00569; L27; 2. DR SMART; SM00228; PDZ; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF101288; L27 domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS51022; L27; 2. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50002; SH3; 1. DR AGR; HGNC:7220; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm; KW Cytoskeleton; Membrane; Phosphoprotein; Reference proteome; Repeat; KW SH3 domain; Synapse. FT CHAIN 1..576 FT /note="MAGUK p55 subfamily member 2" FT /id="PRO_0000094573" FT DOMAIN 8..60 FT /note="L27 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365" FT DOMAIN 84..142 FT /note="L27 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365" FT DOMAIN 185..240 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 249..317 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 374..561 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100" FT MOD_RES 42 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:D3ZAA9" FT MOD_RES 141 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 145 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WV34" FT VAR_SEQ 1..163 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055136" FT VAR_SEQ 1..11 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055137" FT VAR_SEQ 1..10 FT /note="MPVAATNSET -> MAGSPGSGVSLEGISLESSEEAELQRE (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_022951" FT VAR_SEQ 1 FT /note="M -> MSWAPPPQVGQNLRSQTVLRILNGMEDLMWVAMEERRFRALASFTM FT (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055138" FT VAR_SEQ 51..74 FT /note="Missing (in isoform 2, isoform 3, isoform 4 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:11230166, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.5" FT /id="VSP_003156" FT MUTAGEN 363 FT /note="Y->A: Enhances association with the cytoskeleton. FT Diminishes the inhibitory effect on SRC." FT /evidence="ECO:0000269|PubMed:19665017" FT MUTAGEN 363 FT /note="Y->D: Enhances association with the cytoskeleton." FT /evidence="ECO:0000269|PubMed:19665017" FT CONFLICT 80 FT /note="E -> G (in Ref. 4; CAI56746)" FT /evidence="ECO:0000305" FT CONFLICT 104..105 FT /note="HV -> QL (in Ref. 1; CAA58067, 2; BAD97280, 5; FT CAB66489, 4; CAI56746, 7; AAH30287 and 3; FT BAG61302/BAH12204)" FT /evidence="ECO:0000305" FT CONFLICT 242 FT /note="S -> N (in Ref. 1; CAA58067)" FT /evidence="ECO:0000305" FT CONFLICT 531 FT /note="R -> C (in Ref. 3; BAG57760)" FT /evidence="ECO:0000305" FT CONFLICT 554 FT /note="R -> C (in Ref. 3; BAG61302)" FT /evidence="ECO:0000305" FT STRAND 177..191 FT /evidence="ECO:0007829|PDB:2E7K" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:2E7K" FT HELIX 196..200 FT /evidence="ECO:0007829|PDB:2E7K" FT STRAND 208..212 FT /evidence="ECO:0007829|PDB:2E7K" FT HELIX 221..229 FT /evidence="ECO:0007829|PDB:2E7K" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:2E7K" FT STRAND 237..240 FT /evidence="ECO:0007829|PDB:2E7K" SQ SEQUENCE 576 AA; 64581 MW; A08E858EA646A305 CRC64; MPVAATNSET AMQQVLDNLG SLPSATGAAE LDLIFLRGIM ESPIVRSLAK VIMVLWFMQQ NVFVPMKYML KYFGAHERLE ETKLEAVRDN NLELVQEILR DLAHVAEQSS TAAELAHILQ EPHFQSLLET HDSVASKTYE TPPPSPGLDP TFSNQPVPPD AVRMVGIRKT AGEHLGVTFR VEGGELVIAR ILHGGMVAQQ GLLHVGDIIK EVNGQPVGSD PRALQELLRN ASGSVILKIL PSYQEPHLPR QVFVKCHFDY DPARDSLIPC KEAGLRFNAG DLLQIVNQDD ANWWQACHVE GGSAGLIPSQ LLEEKRKAFV KRDLELTPNS GTLCGSLSGK KKKRMMYLTT KNAEFDRHEL LIYEEVARMP PFRRKTLVLI GAQGVGRRSL KNKLIMWDPD RYGTTVPYTS RRPKDSEREG QGYSFVSRGE MEADVRAGRY LEHGEYEGNL YGTRIDSIRG VVAAGKVCVL DVNPQAVKVL RTAEFVPYVV FIEAPDFETL RAMNRAALES GISTKQLTEA DLRRTVEESS RIQRGYGHYF DLCLVNSNLE RTFRELQTAM EKLRTEPQWV PVSWVY // ID E41L3_HUMAN Reviewed; 1087 AA. AC Q9Y2J2; B7Z4I5; F5GX05; O95713; Q9BRP5; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2001, sequence version 2. DT 14-DEC-2022, entry version 205. DE RecName: Full=Band 4.1-like protein 3; DE AltName: Full=4.1B; DE AltName: Full=Differentially expressed in adenocarcinoma of the lung protein 1; DE Short=DAL-1; DE AltName: Full=Erythrocyte membrane protein band 4.1-like 3 {ECO:0000312|HGNC:HGNC:3380}; DE Contains: DE RecName: Full=Band 4.1-like protein 3, N-terminally processed; GN Name=EPB41L3 {ECO:0000312|HGNC:HGNC:3380}; GN Synonyms=DAL1 {ECO:0000312|HGNC:HGNC:3380}, KIAA0987 GN {ECO:0000312|HGNC:HGNC:3380}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RC TISSUE=Lung; RX PubMed=9892180; RA Tran Y.K., Boegler O., Gorse K.M., Wieland I., Green M.R., Newsham I.F.; RT "A novel member of the NF2/ERM/4.1 superfamily with growth suppressing RT properties in lung cancer."; RL Cancer Res. 59:35-43(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16177791; DOI=10.1038/nature03983; RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J., RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.; RT "DNA sequence and analysis of human chromosome 18."; RL Nature 437:551-555(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP INTERACTION WITH CADM1. RX PubMed=12234973; RA Yageta M., Kuramochi M., Masuda M., Fukami T., Fukuhara H., Maruyama T., RA Shibuya M., Murakami Y.; RT "Direct association of TSLC1 and DAL-1, two distinct tumor suppressor RT proteins in lung cancer."; RL Cancer Res. 62:5129-5133(2002). RN [7] RP FUNCTION, AND INTERACTION WITH PRMT3; PRMT5 AND PRMT6. RX PubMed=15334060; DOI=10.1038/sj.onc.1208057; RA Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A., RA Gutmann D.H., Herschman H.R., Clarke S., Newsham I.F.; RT "DAL-1/4.1B tumor suppressor interacts with protein arginine N- RT methyltransferase 3 (PRMT3) and inhibits its ability to methylate RT substrates in vitro and in vivo."; RL Oncogene 23:7761-7771(2004). RN [8] RP FUNCTION, AND INTERACTION WITH PRMT5. RX PubMed=15737618; DOI=10.1016/j.bbrc.2005.01.153; RA Jiang W., Roemer M.E., Newsham I.F.; RT "The tumor suppressor DAL-1/4.1B modulates protein arginine N- RT methyltransferase 5 activity in a substrate-specific manner."; RL Biochem. Biophys. Res. Commun. 329:522-530(2005). RN [9] RP FUNCTION. RX PubMed=16420693; DOI=10.1186/1476-4598-5-4; RA Jiang W., Newsham I.F.; RT "The tumor suppressor DAL-1/4.1B and protein methylation cooperate in RT inducing apoptosis in MCF-7 breast cancer cells."; RL Mol. Cancer 5:4-4(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND THR-469, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND SER-962, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 108-390 IN COMPLEX WITH CADM1, AND RP INTERACTION WITH CADM1. RX PubMed=21131357; DOI=10.1074/jbc.m110.174011; RA Busam R.D., Thorsell A.G., Flores A., Hammarstrom M., Persson C., RA Obrink B., Hallberg B.M.; RT "Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding to RT differentially expressed in adenocarcinoma of the lung (DAL-1/4.1B)."; RL J. Biol. Chem. 286:4511-4516(2011). CC -!- FUNCTION: Tumor suppressor that inhibits cell proliferation and CC promotes apoptosis. Modulates the activity of protein arginine N- CC methyltransferases, including PRMT3 and PRMT5. CC {ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:15737618, CC ECO:0000269|PubMed:16420693, ECO:0000269|PubMed:9892180}. CC -!- SUBUNIT: Interacts (via FERM domain) with CADM1 (PubMed:12234973, CC PubMed:21131357). Interacts (via FERM domain) with PRMT3; the CC interaction is direct and inhibits the protein-arginine N- CC methyltransferase activity of PRMT3 (PubMed:15334060). Interacts with CC PRMT5 (PubMed:15334060, PubMed:15737618). Interacts with PRMT6 CC (PubMed:15334060). {ECO:0000269|PubMed:12234973, CC ECO:0000269|PubMed:15334060, ECO:0000269|PubMed:15737618, CC ECO:0000269|PubMed:21131357}. CC -!- INTERACTION: CC Q9Y2J2-2; Q5MJ10: SPANXN2; NbExp=3; IntAct=EBI-11100740, EBI-12023934; CC Q9Y2J2-3; P15884: TCF4; NbExp=3; IntAct=EBI-10326138, EBI-533224; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell CC junction {ECO:0000269|PubMed:9892180}. Cell membrane CC {ECO:0000269|PubMed:9892180}; Peripheral membrane protein CC {ECO:0000269|PubMed:9892180}; Cytoplasmic side CC {ECO:0000269|PubMed:9892180}. Cytoplasm {ECO:0000269|PubMed:9892180}. CC Note=Detected in the cytoplasm of actively dividing cells. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=Q9Y2J2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y2J2-2; Sequence=VSP_000482, VSP_000483, VSP_000484, CC VSP_000485; CC Name=3; CC IsoId=Q9Y2J2-3; Sequence=VSP_000482, VSP_000483, VSP_000484, CC VSP_000485, VSP_000486; CC Name=4; CC IsoId=Q9Y2J2-4; Sequence=VSP_000482, VSP_000483, VSP_054819, CC VSP_054820; CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, with lower CC levels in kidney, intestine, and testis. Detected in lung. CC {ECO:0000269|PubMed:9892180}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC79806.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA76831.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40458/epb41l3-(erythrocyte-membrane-protein-band-4-1-like-3)"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF069072; AAC79806.1; ALT_FRAME; mRNA. DR EMBL; AB023204; BAA76831.1; ALT_INIT; mRNA. DR EMBL; AK297406; BAH12571.1; -; mRNA. DR EMBL; AP001032; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005059; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005671; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC006141; AAH06141.1; -; mRNA. DR CCDS; CCDS11838.1; -. [Q9Y2J2-1] DR CCDS; CCDS62381.1; -. [Q9Y2J2-2] DR CCDS; CCDS62382.1; -. [Q9Y2J2-4] DR RefSeq; NP_001268462.1; NM_001281533.1. [Q9Y2J2-4] DR RefSeq; NP_001268463.1; NM_001281534.1. [Q9Y2J2-2] DR RefSeq; NP_001268464.1; NM_001281535.1. DR RefSeq; NP_036439.2; NM_012307.3. [Q9Y2J2-1] DR RefSeq; XP_016881125.1; XM_017025636.1. DR PDB; 2HE7; X-ray; 2.00 A; A=108-390. DR PDB; 3BIN; X-ray; 2.30 A; A=109-390. DR PDB; 5RYM; X-ray; 1.64 A; A=107-390. DR PDB; 5RYN; X-ray; 1.88 A; A=107-390. DR PDB; 5RYO; X-ray; 1.58 A; A=107-390. DR PDB; 5RYP; X-ray; 1.63 A; A=107-390. DR PDB; 5RYQ; X-ray; 1.64 A; A=107-390. DR PDB; 5RYR; X-ray; 1.87 A; A=107-390. DR PDB; 5RYS; X-ray; 1.75 A; A=107-390. DR PDB; 5RYT; X-ray; 1.72 A; A=107-390. DR PDB; 5RYU; X-ray; 1.63 A; A=107-390. DR PDB; 5RYV; X-ray; 1.69 A; A=107-390. DR PDB; 5RYW; X-ray; 1.66 A; A=107-390. DR PDB; 5RYX; X-ray; 1.63 A; A=107-390. DR PDB; 5RYY; X-ray; 1.69 A; A=107-390. DR PDB; 5RYZ; X-ray; 1.61 A; A=107-390. DR PDB; 5RZ0; X-ray; 1.74 A; A=107-390. DR PDB; 5RZ1; X-ray; 1.62 A; A=107-390. DR PDB; 5RZ2; X-ray; 1.77 A; A=107-390. DR PDB; 5RZ3; X-ray; 1.74 A; A=107-390. DR PDB; 5RZ4; X-ray; 1.61 A; A=107-390. DR PDB; 5RZ5; X-ray; 1.63 A; A=107-390. DR PDB; 5RZ6; X-ray; 1.64 A; A=107-390. DR PDB; 5RZ7; X-ray; 1.76 A; A=107-390. DR PDB; 5RZ8; X-ray; 1.66 A; A=107-390. DR PDB; 5RZ9; X-ray; 1.79 A; A=107-390. DR PDB; 5RZA; X-ray; 1.89 A; A=107-390. DR PDB; 5RZB; X-ray; 1.59 A; A=107-390. DR PDB; 5RZC; X-ray; 1.75 A; A=107-390. DR PDB; 5RZD; X-ray; 1.81 A; A=107-390. DR PDB; 5RZE; X-ray; 1.69 A; A=107-390. DR PDB; 5RZF; X-ray; 1.76 A; A=107-390. DR PDB; 5RZG; X-ray; 1.70 A; A=107-390. DR PDB; 5RZH; X-ray; 1.88 A; A=107-390. DR PDB; 5RZI; X-ray; 2.09 A; A=107-390. DR PDB; 5RZJ; X-ray; 1.68 A; A=107-390. DR PDB; 5RZK; X-ray; 1.84 A; A=107-390. DR PDB; 5RZL; X-ray; 1.71 A; A=107-390. DR PDB; 5RZM; X-ray; 1.71 A; A=107-390. DR PDB; 5RZN; X-ray; 1.83 A; A=107-390. DR PDB; 5RZO; X-ray; 1.97 A; A=107-390. DR PDB; 5RZP; X-ray; 1.70 A; A=107-390. DR PDB; 5RZQ; X-ray; 1.88 A; A=107-390. DR PDB; 5RZR; X-ray; 1.78 A; A=107-390. DR PDB; 5RZS; X-ray; 1.69 A; A=107-390. DR PDB; 5RZT; X-ray; 1.79 A; A=107-390. DR PDB; 5RZU; X-ray; 1.66 A; A=107-390. DR PDB; 5RZV; X-ray; 1.75 A; A=107-390. DR PDB; 5RZW; X-ray; 1.62 A; A=107-390. DR PDB; 5RZX; X-ray; 1.74 A; A=107-390. DR PDB; 5RZY; X-ray; 1.75 A; A=107-390. DR PDB; 5RZZ; X-ray; 1.76 A; A=107-390. DR PDB; 5S00; X-ray; 1.77 A; A=107-390. DR PDB; 6IBE; X-ray; 1.45 A; A=107-390. DR PDBsum; 2HE7; -. DR PDBsum; 3BIN; -. DR PDBsum; 5RYM; -. DR PDBsum; 5RYN; -. DR PDBsum; 5RYO; -. DR PDBsum; 5RYP; -. DR PDBsum; 5RYQ; -. DR PDBsum; 5RYR; -. DR PDBsum; 5RYS; -. DR PDBsum; 5RYT; -. DR PDBsum; 5RYU; -. DR PDBsum; 5RYV; -. DR PDBsum; 5RYW; -. DR PDBsum; 5RYX; -. DR PDBsum; 5RYY; -. DR PDBsum; 5RYZ; -. DR PDBsum; 5RZ0; -. DR PDBsum; 5RZ1; -. DR PDBsum; 5RZ2; -. DR PDBsum; 5RZ3; -. DR PDBsum; 5RZ4; -. DR PDBsum; 5RZ5; -. DR PDBsum; 5RZ6; -. DR PDBsum; 5RZ7; -. DR PDBsum; 5RZ8; -. DR PDBsum; 5RZ9; -. DR PDBsum; 5RZA; -. DR PDBsum; 5RZB; -. DR PDBsum; 5RZC; -. DR PDBsum; 5RZD; -. DR PDBsum; 5RZE; -. DR PDBsum; 5RZF; -. DR PDBsum; 5RZG; -. DR PDBsum; 5RZH; -. DR PDBsum; 5RZI; -. DR PDBsum; 5RZJ; -. DR PDBsum; 5RZK; -. DR PDBsum; 5RZL; -. DR PDBsum; 5RZM; -. DR PDBsum; 5RZN; -. DR PDBsum; 5RZO; -. DR PDBsum; 5RZP; -. DR PDBsum; 5RZQ; -. DR PDBsum; 5RZR; -. DR PDBsum; 5RZS; -. DR PDBsum; 5RZT; -. DR PDBsum; 5RZU; -. DR PDBsum; 5RZV; -. DR PDBsum; 5RZW; -. DR PDBsum; 5RZX; -. DR PDBsum; 5RZY; -. DR PDBsum; 5RZZ; -. DR PDBsum; 5S00; -. DR PDBsum; 6IBE; -. DR AlphaFoldDB; Q9Y2J2; -. DR SMR; Q9Y2J2; -. DR BioGRID; 116753; 211. DR CORUM; Q9Y2J2; -. DR DIP; DIP-17035N; -. DR IntAct; Q9Y2J2; 119. DR MINT; Q9Y2J2; -. DR STRING; 9606.ENSP00000343158; -. DR GlyConnect; 1025; 11 N-Linked glycans (1 site). DR GlyGen; Q9Y2J2; 3 sites, 11 N-linked glycans (1 site), 1 O-linked glycan (2 sites). DR iPTMnet; Q9Y2J2; -. DR PhosphoSitePlus; Q9Y2J2; -. DR SwissPalm; Q9Y2J2; -. DR BioMuta; EPB41L3; -. DR DMDM; 17433099; -. DR EPD; Q9Y2J2; -. DR jPOST; Q9Y2J2; -. DR MassIVE; Q9Y2J2; -. DR MaxQB; Q9Y2J2; -. DR PaxDb; Q9Y2J2; -. DR PeptideAtlas; Q9Y2J2; -. DR ProteomicsDB; 24274; -. DR ProteomicsDB; 85811; -. [Q9Y2J2-1] DR ProteomicsDB; 85812; -. [Q9Y2J2-2] DR ProteomicsDB; 85813; -. [Q9Y2J2-3] DR Antibodypedia; 21920; 252 antibodies from 30 providers. DR DNASU; 23136; -. DR Ensembl; ENST00000341928.7; ENSP00000343158.2; ENSG00000082397.18. [Q9Y2J2-1] DR Ensembl; ENST00000540638.6; ENSP00000442091.2; ENSG00000082397.18. [Q9Y2J2-2] DR Ensembl; ENST00000544123.5; ENSP00000441174.1; ENSG00000082397.18. [Q9Y2J2-4] DR GeneID; 23136; -. DR KEGG; hsa:23136; -. DR MANE-Select; ENST00000341928.7; ENSP00000343158.2; NM_012307.5; NP_036439.2. DR UCSC; uc002kmt.3; human. [Q9Y2J2-1] DR CTD; 23136; -. DR DisGeNET; 23136; -. DR GeneCards; EPB41L3; -. DR HGNC; HGNC:3380; EPB41L3. DR HPA; ENSG00000082397; Low tissue specificity. DR MIM; 605331; gene. DR neXtProt; NX_Q9Y2J2; -. DR OpenTargets; ENSG00000082397; -. DR PharmGKB; PA27813; -. DR VEuPathDB; HostDB:ENSG00000082397; -. DR eggNOG; KOG3527; Eukaryota. DR GeneTree; ENSGT00940000157047; -. DR HOGENOM; CLU_003623_3_0_1; -. DR InParanoid; Q9Y2J2; -. DR OMA; NDYVSEF; -. DR OrthoDB; 193911at2759; -. DR PhylomeDB; Q9Y2J2; -. DR TreeFam; TF351626; -. DR PathwayCommons; Q9Y2J2; -. DR Reactome; R-HSA-6794361; Neurexins and neuroligins. DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea. DR SignaLink; Q9Y2J2; -. DR SIGNOR; Q9Y2J2; -. DR BioGRID-ORCS; 23136; 21 hits in 1071 CRISPR screens. DR ChiTaRS; EPB41L3; human. DR EvolutionaryTrace; Q9Y2J2; -. DR GeneWiki; EPB41L3; -. DR GenomeRNAi; 23136; -. DR Pharos; Q9Y2J2; Tbio. DR PRO; PR:Q9Y2J2; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; Q9Y2J2; protein. DR Bgee; ENSG00000082397; Expressed in pons and 196 other tissues. DR ExpressionAtlas; Q9Y2J2; baseline and differential. DR Genevisible; Q9Y2J2; HS. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005911; C:cell-cell junction; IDA:HGNC-UCL. DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0044224; C:juxtaparanode region of axon; ISS:BHF-UCL. DR GO; GO:0033270; C:paranode region of axon; ISS:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; TAS:BHF-UCL. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:BHF-UCL. DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro. DR GO; GO:0030865; P:cortical cytoskeleton organization; TAS:BHF-UCL. DR GO; GO:0043217; P:myelin maintenance; ISS:BHF-UCL. DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:BHF-UCL. DR GO; GO:0030913; P:paranodal junction assembly; ISS:BHF-UCL. DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISS:BHF-UCL. DR GO; GO:0002175; P:protein localization to paranode region of axon; ISS:BHF-UCL. DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL. DR GO; GO:0001558; P:regulation of cell growth; IEA:InterPro. DR GO; GO:0008360; P:regulation of cell shape; ISS:BHF-UCL. DR CDD; cd14473; FERM_B-lobe; 1. DR Gene3D; 1.20.80.10; -; 1. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR030691; Band4.1-L3. DR InterPro; IPR008379; Band_4.1_C. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR000798; Ez/rad/moesin-like. DR InterPro; IPR014847; FERM-adjacent. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf. DR InterPro; IPR035963; FERM_2. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR019747; FERM_CS. DR InterPro; IPR000299; FERM_domain. DR InterPro; IPR018979; FERM_N. DR InterPro; IPR018980; FERM_PH-like_C. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR007477; SAB_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR23280:SF20; BAND 4.1-LIKE PROTEIN 3; 1. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF08736; FA; 1. DR Pfam; PF09380; FERM_C; 1. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF09379; FERM_N; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR SMART; SM01195; FA; 1. DR SMART; SM01196; FERM_C; 1. DR SUPFAM; SSF47031; Second domain of FERM; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. DR AGR; HGNC:3380; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; Apoptosis; KW Cell junction; Cell membrane; Cytoplasm; Cytoskeleton; Membrane; KW Phosphoprotein; Reference proteome; Tumor suppressor. FT CHAIN 1..1087 FT /note="Band 4.1-like protein 3" FT /id="PRO_0000219399" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..1087 FT /note="Band 4.1-like protein 3, N-terminally processed" FT /id="PRO_0000423194" FT DOMAIN 110..391 FT /note="FERM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 394..513 FT /note="Hydrophilic" FT REGION 459..529 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 514..860 FT /note="Spectrin--actin-binding" FT /evidence="ECO:0000255" FT REGION 541..563 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 675..715 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 861..1083 FT /note="C-terminal (CTD)" FT REGION 937..965 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 470..496 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 510..524 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 2 FT /note="N-acetylthreonine; in Band 4.1-like protein 3, N- FT terminally processed" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 88 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WV92" FT MOD_RES 420 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 443 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WV92" FT MOD_RES 460 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 469 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 492 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9WV92" FT MOD_RES 706 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9WV92" FT MOD_RES 708 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WV92" FT MOD_RES 960 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WV92" FT MOD_RES 962 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1081 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9WV92" FT VAR_SEQ 446 FT /note="G -> GASVNENHEIYMKDSMSAA (in isoform 2, isoform 3 FT and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9892180" FT /id="VSP_000482" FT VAR_SEQ 503..689 FT /note="Missing (in isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9892180" FT /id="VSP_000483" FT VAR_SEQ 708..719 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9892180" FT /id="VSP_000484" FT VAR_SEQ 784..824 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9892180" FT /id="VSP_000485" FT VAR_SEQ 835..1087 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9892180" FT /id="VSP_000486" FT VAR_SEQ 1052 FT /note="A -> E (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054819" FT VAR_SEQ 1053..1087 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054820" FT VARIANT 555 FT /note="A -> T (in dbSNP:rs9966357)" FT /id="VAR_048353" FT VARIANT 575 FT /note="Y -> C (in dbSNP:rs8082898)" FT /id="VAR_048354" FT VARIANT 859 FT /note="E -> Q (in dbSNP:rs8096452)" FT /id="VAR_048355" FT CONFLICT 12 FT /note="K -> E (in Ref. 3; BAH12571)" FT /evidence="ECO:0000305" FT CONFLICT 32 FT /note="Missing (in Ref. 1; AAC79806)" FT /evidence="ECO:0000305" FT CONFLICT 498 FT /note="R -> Q (in Ref. 1; AAC79806)" FT /evidence="ECO:0000305" FT STRAND 109..115 FT /evidence="ECO:0007829|PDB:6IBE" FT STRAND 121..127 FT /evidence="ECO:0007829|PDB:6IBE" FT HELIX 132..142 FT /evidence="ECO:0007829|PDB:6IBE" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:6IBE" FT STRAND 151..156 FT /evidence="ECO:0007829|PDB:6IBE" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:6IBE" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:6IBE" FT HELIX 172..175 FT /evidence="ECO:0007829|PDB:6IBE" FT STRAND 180..188 FT /evidence="ECO:0007829|PDB:6IBE" FT HELIX 193..195 FT /evidence="ECO:0007829|PDB:6IBE" FT HELIX 199..214 FT /evidence="ECO:0007829|PDB:6IBE" FT HELIX 222..237 FT /evidence="ECO:0007829|PDB:6IBE" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:6IBE" FT TURN 249..252 FT /evidence="ECO:0007829|PDB:5RZ8" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:6IBE" FT HELIX 261..272 FT /evidence="ECO:0007829|PDB:6IBE" FT TURN 273..276 FT /evidence="ECO:0007829|PDB:6IBE" FT HELIX 279..290 FT /evidence="ECO:0007829|PDB:6IBE" FT TURN 294..297 FT /evidence="ECO:0007829|PDB:6IBE" FT STRAND 299..305 FT /evidence="ECO:0007829|PDB:6IBE" FT STRAND 310..315 FT /evidence="ECO:0007829|PDB:6IBE" FT STRAND 317..333 FT /evidence="ECO:0007829|PDB:6IBE" FT HELIX 334..336 FT /evidence="ECO:0007829|PDB:6IBE" FT STRAND 337..343 FT /evidence="ECO:0007829|PDB:6IBE" FT STRAND 346..351 FT /evidence="ECO:0007829|PDB:6IBE" FT TURN 354..357 FT /evidence="ECO:0007829|PDB:2HE7" FT STRAND 361..366 FT /evidence="ECO:0007829|PDB:6IBE" FT HELIX 370..389 FT /evidence="ECO:0007829|PDB:6IBE" SQ SEQUENCE 1087 AA; 120678 MW; 0A33CA4A43F12620 CRC64; MTTESGSDSE SKPDQEAEPQ EAAGAQGRAG APVPEPPKEE QQQALEQFAA AAAHSTPVRR EVTDKEQEFA ARAAKQLEYQ QLEDDKLSQK SSSSKLSRSP LKIVKKPKSM QCKVILLDGS EYTCDVEKRS RGQVLFDKVC EHLNLLEKDY FGLTYRDAEN QKNWLDPAKE IKKQVRSGAW HFSFNVKFYP PDPAQLSEDI TRYYLCLQLR DDIVSGRLPC SFVTLALLGS YTVQSELGDY DPDECGSDYI SEFRFAPNHT KELEDKVIEL HKSHRGMTPA EAEMHFLENA KKLSMYGVDL HHAKDSEGVE IMLGVCASGL LIYRDRLRIN RFAWPKVLKI SYKRNNFYIK IRPGEFEQFE STIGFKLPNH RAAKRLWKVC VEHHTFFRLL LPEAPPKKFL TLGSKFRYSG RTQAQTRRAS ALIDRPAPYF ERSSSKRYTM SRSLDGEVGT GQYATTKGIS QTNLITTVTP EKKAEEERDE EEDKRRKGEE VTPISAIRHE GKSPGLGTDS CPLSPPSTHC APTSPTELRR RCKENDCKLP GYEPSRAEHL PGEPALDSDG PGRPYLGDQD VAFSYRQQTG KGTTLFSFSL QLPESFPSLL DDDGYLSFPN LSETNLLPQS LQHYLPIRSP SLVPCFLFIF FFLLSASFSV PYALTLSFPL ALCLCYLEPK AASLSASLDN DPSDSSEEET DSERTDTAAD GETTATESDQ EEDAELKAQE LEKTQDDLMK HQTNISELKR TFLETSTDTA VTNEWEKRLS TSPVRLAARQ EDAPMIEPLV PEETKQSSGE KLMDGSEIFS LLESARKPTE FIGGVTSTSQ SWVQKMETKT ESSGIETEPT VHHLPLSTEK VVQETVLVEE RRVVHASGDA SYSAGDSGDA AAQPAFTGIK GKEGSALTEG AKEEGGEEVA KAVLEQEETA AASRERQEEQ SAAIHISETL EQKPHFESST VKTETISFGS VSPGGVKLEI STKEVPVVHT ETKTITYESS QVDPGTDLEP GVLMSAQTIT SETTSTTTTT HITKTVKGGI SETRIEKRIV ITGDADIDHD QALAQAIKEA KEQHPDMSVT KVVVHKETEI TPEDGED // ID PSA6_HUMAN Reviewed; 246 AA. AC P60900; B2R7J9; B4DQR4; B4DXJ9; P34062; Q6IB60; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2004, sequence version 1. DT 14-DEC-2022, entry version 197. DE RecName: Full=Proteasome subunit alpha type-6; DE AltName: Full=27 kDa prosomal protein; DE Short=PROS-27; DE Short=p27K; DE AltName: Full=Macropain iota chain; DE AltName: Full=Multicatalytic endopeptidase complex iota chain; DE AltName: Full=Proteasome iota chain; GN Name=PSMA6; Synonyms=PROS27; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=7681138; DOI=10.1007/bf00282801; RA Bey F., Pereira I.S., Coux O., Viegas-Pequignot E., Targa F.R., RA Nothwang H.G., Dutrillaux B., Scherrer K.; RT "The prosomal RNA-binding protein p27K is a member of the alpha-type human RT prosomal gene family."; RL Mol. Gen. Genet. 237:193-205(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Cerebellum, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Lymph, Skeletal muscle, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 12-43; 60-88; 105-116; 154-164; 172-181 AND 229-246, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-246 (ISOFORM 1), AND PARTIAL PROTEIN RP SEQUENCE. RX PubMed=1888762; DOI=10.1016/0167-4838(91)90020-z; RA DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z., Moomaw C.R., RA Dawson P.A., Slaughter C.A.; RT "The primary structures of four subunits of the human, high-molecular- RT weight proteinase, macropain (proteasome), are distinct but homologous."; RL Biochim. Biophys. Acta 1079:29-38(1991). RN [9] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=7811265; DOI=10.1006/bbrc.1994.2876; RA Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.; RT "Human proteasome subunits from 2-dimensional gels identified by partial RT sequencing."; RL Biochem. Biophys. Res. Commun. 205:1785-1789(1994). RN [10] RP FUNCTION IN ANTIGEN PRESENTATION. RX PubMed=8610016; DOI=10.1038/381166a0; RA Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H., RA Rammensee H.G., Koszinowski U.H., Kloetzel P.M.; RT "A role for the proteasome regulator PA28alpha in antigen presentation."; RL Nature 381:166-168(1996). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=12181345; DOI=10.1091/mbc.e02-03-0122; RA Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D., RA Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.; RT "Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes, RT ubiquitin, and protein substrates of proteasome."; RL Mol. Biol. Cell 13:2771-2782(2002). RN [12] RP FUNCTION. RX PubMed=15244466; DOI=10.1021/bm049957a; RA Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.; RT "20S proteasome prevents aggregation of heat-denatured proteins without RT PA700 regulatory subcomplex like a molecular chaperone."; RL Biomacromolecules 5:1465-1469(2004). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17323924; DOI=10.1021/bi061994u; RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; RT "Mass spectrometric characterization of the affinity-purified human 26S RT proteasome complex."; RL Biochemistry 46:3553-3565(2007). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-104, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP INTERACTION WITH ALKBH4. RX PubMed=23145062; DOI=10.1371/journal.pone.0049045; RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., RA Falnes P.O.; RT "Human ALKBH4 interacts with proteins associated with transcription."; RL PLoS ONE 7:E49045-E49045(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-63 AND SER-64, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=27176742; DOI=10.1515/hsz-2016-0176; RA Rut W., Drag M.; RT "Human 20S proteasome activity towards fluorogenic peptides of various RT chain lengths."; RL Biol. Chem. 397:921-926(2016). RN [20] RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT. RX PubMed=26133119; DOI=10.1038/ncomms8573; RA da Fonseca P.C., Morris E.P.; RT "Cryo-EM reveals the conformation of a substrate analogue in the human 20S RT proteasome core."; RL Nat. Commun. 6:7573-7573(2015). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-245, AND SUBUNIT. RX PubMed=25599644; DOI=10.1016/j.str.2014.11.017; RA Harshbarger W., Miller C., Diedrich C., Sacchettini J.; RT "Crystal structure of the human 20S proteasome in complex with RT carfilzomib."; RL Structure 23:418-424(2015). RN [22] RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT. RX PubMed=27428775; DOI=10.1038/nsmb.3273; RA Huang X., Luan B., Wu J., Shi Y.; RT "An atomic structure of the human 26S proteasome."; RL Nat. Struct. Mol. Biol. 23:778-785(2016). RN [23] RP STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS), AND SUBUNIT. RX PubMed=27342858; DOI=10.1073/pnas.1608050113; RA Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G., RA Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.; RT "Structure of the human 26S proteasome at a resolution of 3.9 Aa."; RL Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT. RX PubMed=27493187; DOI=10.1126/science.aaf8993; RA Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R., RA Stark H., Bourenkov G., Chari A.; RT "The inhibition mechanism of human 20S proteasomes enables next-generation RT inhibitor design."; RL Science 353:594-598(2016). RN [25] RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH AKIRIN2, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=34711951; DOI=10.1038/s41586-021-04035-8; RA de Almeida M., Hinterndorfer M., Brunner H., Grishkovskaya I., Singh K., RA Schleiffer A., Jude J., Deswal S., Kalis R., Vunjak M., Lendl T., Imre R., RA Roitinger E., Neumann T., Kandolf S., Schutzbier M., Mechtler K., RA Versteeg G.A., Haselbach D., Zuber J.; RT "AKIRIN2 controls the nuclear import of proteasomes in vertebrates."; RL Nature 599:491-496(2021). CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the CC proteolytic degradation of most intracellular proteins. This complex CC plays numerous essential roles within the cell by associating with CC different regulatory particles. Associated with two 19S regulatory CC particles, forms the 26S proteasome and thus participates in the ATP- CC dependent degradation of ubiquitinated proteins. The 26S proteasome CC plays a key role in the maintenance of protein homeostasis by removing CC misfolded or damaged proteins that could impair cellular functions, and CC by removing proteins whose functions are no longer required. Associated CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin- CC independent protein degradation. This type of proteolysis is required CC in several pathways including spermatogenesis (20S-PA200 complex) or CC generation of a subset of MHC class I-presented antigenic peptides CC (20S-PA28 complex). {ECO:0000269|PubMed:15244466, CC ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}. CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two CC 19S regulatory subunits (PubMed:25599644, PubMed:26133119, CC PubMed:27342858, PubMed:27428775, PubMed:27493187, PubMed:34711951). CC The 20S proteasome core is a barrel-shaped complex made of 28 subunits CC that are arranged in four stacked rings (PubMed:25599644, CC PubMed:26133119, PubMed:27342858, PubMed:27428775, PubMed:27493187, CC PubMed:34711951). The two outer rings are each formed by seven alpha CC subunits, and the two inner rings are formed by seven beta subunits CC (PubMed:25599644, PubMed:26133119, PubMed:27342858, PubMed:27428775, CC PubMed:27493187, PubMed:34711951). The proteolytic activity is exerted CC by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:25599644, CC PubMed:26133119, PubMed:27342858, PubMed:27428775, PubMed:27493187, CC PubMed:34711951). Interacts with ALKBH4 (PubMed:23145062). CC {ECO:0000269|PubMed:23145062, ECO:0000269|PubMed:25599644, CC ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858, CC ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187, CC ECO:0000269|PubMed:34711951}. CC -!- INTERACTION: CC P60900; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-357793, EBI-741210; CC P60900; Q8N9M1-2: C19orf47; NbExp=3; IntAct=EBI-357793, EBI-10979594; CC P60900; Q9BY67: CADM1; NbExp=3; IntAct=EBI-357793, EBI-5652260; CC P60900; P84090: ERH; NbExp=3; IntAct=EBI-357793, EBI-711389; CC P60900; P42858: HTT; NbExp=4; IntAct=EBI-357793, EBI-466029; CC P60900; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-357793, EBI-10172511; CC P60900; Q9BT23: LIMD2; NbExp=3; IntAct=EBI-357793, EBI-2805292; CC P60900; P62875: POLR2L; NbExp=3; IntAct=EBI-357793, EBI-359527; CC P60900; P25787: PSMA2; NbExp=6; IntAct=EBI-357793, EBI-603262; CC P60900; P25788: PSMA3; NbExp=10; IntAct=EBI-357793, EBI-348380; CC P60900; P25789: PSMA4; NbExp=5; IntAct=EBI-357793, EBI-359310; CC P60900; O14818: PSMA7; NbExp=11; IntAct=EBI-357793, EBI-603272; CC P60900; O43242: PSMD3; NbExp=3; IntAct=EBI-357793, EBI-357622; CC P60900; Q96K19: RNF170; NbExp=3; IntAct=EBI-357793, EBI-2130336; CC P60900; Q14D33: RTP5; NbExp=3; IntAct=EBI-357793, EBI-10217913; CC P60900; A2RU48: SMCO3; NbExp=3; IntAct=EBI-357793, EBI-10173195; CC P60900; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-357793, EBI-11139477; CC P60900; Q9HCM9: TRIM39; NbExp=3; IntAct=EBI-357793, EBI-739510; CC P60900; Q9HCM9-2: TRIM39; NbExp=5; IntAct=EBI-357793, EBI-11523450; CC P60900; Q6FI91: TSPYL; NbExp=3; IntAct=EBI-357793, EBI-723389; CC P60900; Q9Y5K5: UCHL5; NbExp=4; IntAct=EBI-357793, EBI-1051183; CC P60900; Q8NCP5: ZBTB44; NbExp=3; IntAct=EBI-357793, EBI-5658292; CC P60900; Q969J2: ZKSCAN4; NbExp=3; IntAct=EBI-357793, EBI-2818641; CC P60900; Q8TC21: ZNF596; NbExp=3; IntAct=EBI-357793, EBI-3923453; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QUM9, CC ECO:0000269|PubMed:12181345}. Nucleus {ECO:0000269|PubMed:12181345, CC ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into CC the nucleus following interaction with AKIRIN2, which bridges the CC proteasome with the nuclear import receptor IPO9 (PubMed:34711951). CC Colocalizes with TRIM5 in cytoplasmic bodies (By similarity). CC {ECO:0000250|UniProtKB:Q9QUM9, ECO:0000269|PubMed:34711951}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P60900-1; Sequence=Displayed; CC Name=2; CC IsoId=P60900-2; Sequence=VSP_054587; CC Name=3; CC IsoId=P60900-3; Sequence=VSP_054586; CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE- CC ProRule:PRU00808}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X59417; CAA42052.1; -; mRNA. DR EMBL; CR456944; CAG33225.1; -; mRNA. DR EMBL; AK298920; BAG61026.1; -; mRNA. DR EMBL; AK302008; BAG63411.1; -; mRNA. DR EMBL; AK313011; BAG35846.1; -; mRNA. DR EMBL; AK316223; BAH14594.1; -; mRNA. DR EMBL; AL121594; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL133163; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471078; EAW65876.1; -; Genomic_DNA. DR EMBL; CH471078; EAW65877.1; -; Genomic_DNA. DR EMBL; BC002979; AAH02979.1; -; mRNA. DR EMBL; BC017882; AAH17882.1; -; mRNA. DR EMBL; BC022354; AAH22354.1; -; mRNA. DR EMBL; BC023659; AAH23659.1; -; mRNA. DR EMBL; BC070137; AAH70137.1; -; mRNA. DR EMBL; X61972; CAA43964.1; -; mRNA. DR CCDS; CCDS61437.1; -. [P60900-2] DR CCDS; CCDS61438.1; -. [P60900-3] DR CCDS; CCDS9655.1; -. [P60900-1] DR PIR; S30274; S30274. DR RefSeq; NP_001269161.1; NM_001282232.1. [P60900-3] DR RefSeq; NP_001269162.1; NM_001282233.1. [P60900-3] DR RefSeq; NP_001269163.1; NM_001282234.1. [P60900-2] DR RefSeq; NP_002782.1; NM_002791.2. [P60900-1] DR RefSeq; XP_016876957.1; XM_017021468.1. [P60900-3] DR PDB; 4R3O; X-ray; 2.60 A; A/O=2-245. DR PDB; 4R67; X-ray; 2.89 A; A/O/c/q=2-245. DR PDB; 5A0Q; EM; 3.50 A; A/O=1-246. DR PDB; 5GJQ; EM; 4.50 A; B/h=1-246. DR PDB; 5GJR; EM; 3.50 A; B/h=1-246. DR PDB; 5L4G; EM; 4.02 A; A/N=1-246. DR PDB; 5LE5; X-ray; 1.80 A; G/U=1-246. DR PDB; 5LEX; X-ray; 2.20 A; G/U=1-246. DR PDB; 5LEY; X-ray; 1.90 A; G/U=1-246. DR PDB; 5LEZ; X-ray; 2.19 A; G/U=1-246. DR PDB; 5LF0; X-ray; 2.41 A; G/U=1-246. DR PDB; 5LF1; X-ray; 2.00 A; G/U=1-246. DR PDB; 5LF3; X-ray; 2.10 A; G/U=1-246. DR PDB; 5LF4; X-ray; 1.99 A; G/U=1-246. DR PDB; 5LF6; X-ray; 2.07 A; G/U=1-246. DR PDB; 5LF7; X-ray; 2.00 A; G/U=1-246. DR PDB; 5LN3; EM; 6.80 A; A=1-246. DR PDB; 5M32; EM; 3.80 A; G/U=1-246. DR PDB; 5T0C; EM; 3.80 A; AG/BG=2-246. DR PDB; 5T0G; EM; 4.40 A; G=2-246. DR PDB; 5T0H; EM; 6.80 A; G=2-246. DR PDB; 5T0I; EM; 8.00 A; G=2-246. DR PDB; 5T0J; EM; 8.00 A; G=2-246. DR PDB; 5VFO; EM; 3.50 A; G/g=5-244. DR PDB; 5VFP; EM; 4.20 A; G/g=5-244. DR PDB; 5VFQ; EM; 4.20 A; G/g=5-244. DR PDB; 5VFR; EM; 4.90 A; G/g=5-244. DR PDB; 5VFS; EM; 3.60 A; G/g=5-244. DR PDB; 5VFT; EM; 7.00 A; G/g=5-244. DR PDB; 5VFU; EM; 5.80 A; G/g=5-244. DR PDB; 6AVO; EM; 3.80 A; K/R=1-246. DR PDB; 6E5B; X-ray; 2.77 A; G/U=1-246. DR PDB; 6KWY; EM; 2.72 A; G/U=1-246. DR PDB; 6MSB; EM; 3.00 A; G/g=2-246. DR PDB; 6MSD; EM; 3.20 A; G/g=2-246. DR PDB; 6MSG; EM; 3.50 A; G/g=2-246. DR PDB; 6MSH; EM; 3.60 A; G/g=2-246. DR PDB; 6MSK; EM; 3.20 A; G/g=2-246. DR PDB; 6R70; EM; 3.50 A; G/U=2-245. DR PDB; 6REY; EM; 3.00 A; A/O=1-246. DR PDB; 6RGQ; EM; 2.60 A; A/O=1-246. DR PDB; 6WJD; EM; 4.80 A; G/g=2-246. DR PDB; 6WJN; EM; 5.70 A; G/g=5-244. DR PDB; 6XMJ; EM; 3.00 A; A=2-245. DR PDB; 7AWE; X-ray; 2.29 A; A/O=4-245. DR PDB; 7B12; X-ray; 2.43 A; A/O=4-245. DR PDB; 7LXV; EM; 3.40 A; G/U=1-246. DR PDB; 7NHT; EM; 2.80 A; G=1-246. DR PDB; 7PG9; EM; 3.70 A; A/O=1-246. DR PDB; 7V5G; EM; 4.47 A; O/V=1-246. DR PDB; 7V5M; EM; 3.88 A; A/O=1-246. DR PDB; 7W37; EM; 3.00 A; G/g=1-246. DR PDB; 7W38; EM; 3.10 A; G/g=1-246. DR PDB; 7W39; EM; 3.20 A; G/g=1-246. DR PDB; 7W3A; EM; 3.50 A; G/g=1-246. DR PDB; 7W3B; EM; 3.60 A; G/g=1-246. DR PDB; 7W3C; EM; 3.40 A; G/g=1-246. DR PDB; 7W3F; EM; 3.30 A; G/g=1-246. DR PDB; 7W3G; EM; 3.20 A; G/g=1-246. DR PDB; 7W3H; EM; 3.20 A; G/g=1-246. DR PDB; 7W3I; EM; 3.50 A; G/g=1-246. DR PDB; 7W3J; EM; 3.50 A; G/g=1-246. DR PDB; 7W3K; EM; 3.60 A; G/g=1-246. DR PDB; 7W3M; EM; 3.50 A; G/g=1-246. DR PDBsum; 4R3O; -. DR PDBsum; 4R67; -. DR PDBsum; 5A0Q; -. DR PDBsum; 5GJQ; -. DR PDBsum; 5GJR; -. DR PDBsum; 5L4G; -. DR PDBsum; 5LE5; -. DR PDBsum; 5LEX; -. DR PDBsum; 5LEY; -. DR PDBsum; 5LEZ; -. DR PDBsum; 5LF0; -. DR PDBsum; 5LF1; -. DR PDBsum; 5LF3; -. DR PDBsum; 5LF4; -. DR PDBsum; 5LF6; -. DR PDBsum; 5LF7; -. DR PDBsum; 5LN3; -. DR PDBsum; 5M32; -. DR PDBsum; 5T0C; -. DR PDBsum; 5T0G; -. DR PDBsum; 5T0H; -. DR PDBsum; 5T0I; -. DR PDBsum; 5T0J; -. DR PDBsum; 5VFO; -. DR PDBsum; 5VFP; -. DR PDBsum; 5VFQ; -. DR PDBsum; 5VFR; -. DR PDBsum; 5VFS; -. DR PDBsum; 5VFT; -. DR PDBsum; 5VFU; -. DR PDBsum; 6AVO; -. DR PDBsum; 6E5B; -. DR PDBsum; 6KWY; -. DR PDBsum; 6MSB; -. DR PDBsum; 6MSD; -. DR PDBsum; 6MSG; -. DR PDBsum; 6MSH; -. DR PDBsum; 6MSK; -. DR PDBsum; 6R70; -. DR PDBsum; 6REY; -. DR PDBsum; 6RGQ; -. DR PDBsum; 6WJD; -. DR PDBsum; 6WJN; -. DR PDBsum; 6XMJ; -. DR PDBsum; 7AWE; -. DR PDBsum; 7B12; -. DR PDBsum; 7LXV; -. DR PDBsum; 7NHT; -. DR PDBsum; 7PG9; -. DR PDBsum; 7V5G; -. DR PDBsum; 7V5M; -. DR PDBsum; 7W37; -. DR PDBsum; 7W38; -. DR PDBsum; 7W39; -. DR PDBsum; 7W3A; -. DR PDBsum; 7W3B; -. DR PDBsum; 7W3C; -. DR PDBsum; 7W3F; -. DR PDBsum; 7W3G; -. DR PDBsum; 7W3H; -. DR PDBsum; 7W3I; -. DR PDBsum; 7W3J; -. DR PDBsum; 7W3K; -. DR PDBsum; 7W3M; -. DR AlphaFoldDB; P60900; -. DR SMR; P60900; -. DR BioGRID; 111660; 273. DR ComplexPortal; CPX-5993; 26S Proteasome complex. DR CORUM; P60900; -. DR DIP; DIP-29367N; -. DR IntAct; P60900; 82. DR MINT; P60900; -. DR STRING; 9606.ENSP00000261479; -. DR BindingDB; P60900; -. DR ChEMBL; CHEMBL2364701; -. DR ChEMBL; CHEMBL3831201; -. DR DrugBank; DB08515; (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE. DR MEROPS; T01.971; -. DR GlyGen; P60900; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P60900; -. DR MetOSite; P60900; -. DR PhosphoSitePlus; P60900; -. DR SwissPalm; P60900; -. DR BioMuta; PSMA6; -. DR DMDM; 46397659; -. DR REPRODUCTION-2DPAGE; IPI00029623; -. DR SWISS-2DPAGE; P60900; -. DR UCD-2DPAGE; P60900; -. DR EPD; P60900; -. DR jPOST; P60900; -. DR MassIVE; P60900; -. DR MaxQB; P60900; -. DR PaxDb; P60900; -. DR PeptideAtlas; P60900; -. DR ProteomicsDB; 4898; -. DR ProteomicsDB; 5443; -. DR ProteomicsDB; 57236; -. [P60900-1] DR TopDownProteomics; P60900-1; -. [P60900-1] DR Antibodypedia; 155; 503 antibodies from 33 providers. DR DNASU; 5687; -. DR Ensembl; ENST00000261479.9; ENSP00000261479.4; ENSG00000100902.11. [P60900-1] DR Ensembl; ENST00000540871.5; ENSP00000444844.1; ENSG00000100902.11. [P60900-2] DR Ensembl; ENST00000555764.5; ENSP00000452566.1; ENSG00000100902.11. [P60900-3] DR Ensembl; ENST00000622405.4; ENSP00000479620.1; ENSG00000100902.11. [P60900-3] DR GeneID; 5687; -. DR KEGG; hsa:5687; -. DR MANE-Select; ENST00000261479.9; ENSP00000261479.4; NM_002791.3; NP_002782.1. DR UCSC; uc001wtd.5; human. [P60900-1] DR CTD; 5687; -. DR DisGeNET; 5687; -. DR GeneCards; PSMA6; -. DR HGNC; HGNC:9535; PSMA6. DR HPA; ENSG00000100902; Low tissue specificity. DR MalaCards; PSMA6; -. DR MIM; 602855; gene. DR neXtProt; NX_P60900; -. DR OpenTargets; ENSG00000100902; -. DR PharmGKB; PA33880; -. DR VEuPathDB; HostDB:ENSG00000100902; -. DR eggNOG; KOG0182; Eukaryota. DR GeneTree; ENSGT00550000074807; -. DR HOGENOM; CLU_035750_6_0_1; -. DR InParanoid; P60900; -. DR PhylomeDB; P60900; -. DR TreeFam; TF106210; -. DR PathwayCommons; P60900; -. DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. DR Reactome; R-HSA-1236974; ER-Phagosome pathway. DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1. DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin. DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4. DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G. DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21. DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation. DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1. DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC). DR Reactome; R-HSA-382556; ABC-family proteins mediated transport. DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA. DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins. DR Reactome; R-HSA-4641257; Degradation of AXIN. DR Reactome; R-HSA-4641258; Degradation of DVL. DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis. DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD. DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling. DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome. DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome. DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome. DR Reactome; R-HSA-5632684; Hedgehog 'on' state. DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs. DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway. DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling. DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis. DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-HSA-5689603; UCH proteinases. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex. DR Reactome; R-HSA-68949; Orc1 removal from chromatin. DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-HSA-69481; G2/M Checkpoints. DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D. DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis. DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity. DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity. DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR Reactome; R-HSA-9020702; Interleukin-1 signaling. DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling. DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway. DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; P60900; -. DR SIGNOR; P60900; -. DR BioGRID-ORCS; 5687; 793 hits in 1055 CRISPR screens. DR ChiTaRS; PSMA6; human. DR GeneWiki; PSMA6; -. DR GenomeRNAi; 5687; -. DR Pharos; P60900; Tbio. DR PRO; PR:P60900; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; P60900; protein. DR Bgee; ENSG00000100902; Expressed in left testis and 101 other tissues. DR ExpressionAtlas; P60900; baseline and differential. DR Genevisible; P60900; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0030016; C:myofibril; ISS:BHF-UCL. DR GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000932; C:P-body; ISS:UniProtKB. DR GO; GO:0005844; C:polysome; IDA:BHF-UCL. DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB. DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB. DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:UniProtKB. DR GO; GO:0030017; C:sarcomere; ISS:BHF-UCL. DR GO; GO:0004175; F:endopeptidase activity; NAS:UniProtKB. DR GO; GO:0051059; F:NF-kappaB binding; IPI:BHF-UCL. DR GO; GO:0035639; F:purine ribonucleoside triphosphate binding; NAS:BHF-UCL. DR GO; GO:0003723; F:RNA binding; IDA:BHF-UCL. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL. DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; NAS:ComplexPortal. DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP:BHF-UCL. DR GO; GO:0050727; P:regulation of inflammatory response; IC:BHF-UCL. DR CDD; cd03754; proteasome_alpha_type_6; 1. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR023332; Proteasome_alpha-type. DR InterPro; IPR000426; Proteasome_asu_N. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR034642; Proteasome_subunit_alpha6. DR Pfam; PF00227; Proteasome; 1. DR Pfam; PF10584; Proteasome_A_N; 1. DR SMART; SM00948; Proteasome_A_N; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1. DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1. DR AGR; HGNC:9535; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Direct protein sequencing; Glycoprotein; Nucleus; Phosphoprotein; KW Proteasome; Reference proteome. FT CHAIN 1..246 FT /note="Proteasome subunit alpha type-6" FT /id="PRO_0000124130" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 63 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 64 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 102 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 104 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 159 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9QUM9" FT CARBOHYD 5 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT VAR_SEQ 1..79 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054586" FT VAR_SEQ 1..25 FT /note="MSRGSSAGFDRHITIFSPEGRLYQV -> MAGLRR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054587" FT CONFLICT 59 FT /note="K -> C (in Ref. 8; CAA43964)" FT /evidence="ECO:0000305" FT TURN 8..12 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:7AWE" FT STRAND 18..20 FT /evidence="ECO:0007829|PDB:5VFO" FT HELIX 23..34 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 38..42 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 49..53 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:5LF0" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 68..73 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 76..82 FT /evidence="ECO:0007829|PDB:5LE5" FT HELIX 84..105 FT /evidence="ECO:0007829|PDB:5LE5" FT HELIX 111..125 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:4R3O" FT STRAND 135..144 FT /evidence="ECO:0007829|PDB:5LE5" FT TURN 145..147 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 148..154 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 156..158 FT /evidence="ECO:0007829|PDB:4R3O" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:5A0Q" FT STRAND 163..169 FT /evidence="ECO:0007829|PDB:5LE5" FT HELIX 172..185 FT /evidence="ECO:0007829|PDB:5LE5" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:5LE5" FT HELIX 194..206 FT /evidence="ECO:0007829|PDB:5LE5" FT HELIX 212..214 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 215..219 FT /evidence="ECO:0007829|PDB:5LE5" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:6E5B" FT HELIX 232..243 FT /evidence="ECO:0007829|PDB:5LE5" SQ SEQUENCE 246 AA; 27399 MW; 94D1FD3C0A7CC72A CRC64; MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN WKYKYGYEIP VDMLCKRIAD ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ VYKCDPAGYY CGFKATAAGV KQTESTSFLE KKVKKKFDWT FEQTVETAIT CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV ALAERD // ID ITB4_HUMAN Reviewed; 1822 AA. AC P16144; A0AVL6; O14690; O14691; O15339; O15340; O15341; Q0VF97; Q9UIQ4; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 5. DT 14-DEC-2022, entry version 257. DE RecName: Full=Integrin beta-4; DE AltName: Full=GP150; DE AltName: CD_antigen=CD104; DE Flags: Precursor; GN Name=ITGB4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-4A), AND VARIANT PRO-1779. RX PubMed=2311577; DOI=10.1002/j.1460-2075.1990.tb08170.x; RA Suzuki S., Naitoh Y.; RT "Amino acid sequence of a novel integrin beta 4 subunit and primary RT expression of the mRNA in epithelial cells."; RL EMBO J. 9:757-763(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-4B), AND VARIANT PRO-1779. RX PubMed=2311578; DOI=10.1002/j.1460-2075.1990.tb08171.x; RA Hogervorst F., Kuikman I., von Dem Borne A.E.G.K., Sonnenberg A.; RT "Cloning and sequence analysis of beta-4 cDNA: an integrin subunit that RT contains a unique 118 kd cytoplasmic domain."; RL EMBO J. 9:765-770(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-4C). RC TISSUE=Pancreas; RX PubMed=1976638; DOI=10.1083/jcb.111.4.1593; RA Tamura R.N., Rozzo C., Starr L., Chambers J., Reichardt L.F., Cooper H.M., RA Quaranta V.; RT "Epithelial integrin alpha 6 beta 4: complete primary structure of alpha 6 RT and variant forms of beta 4."; RL J. Cell Biol. 111:1593-1604(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS BETA-4A; BETA-4B AND RP BETA-4C), AND VARIANTS SER-1764 AND PRO-1779. RX PubMed=9194858; RA Pulkkinen L., Kurtz K.S., Xu Y., Bruckner-Tuderman L., Uitto J.; RT "Genomic organization of the integrin beta 4 gene (ITGB4): a homozygous RT splice-site mutation in a patient with junctional epidermolysis bullosa RT associated with pyloric atresia."; RL Lab. Invest. 76:823-833(1997). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS BETA-4A; BETA-4B AND BETA-4C), RP AND VARIANTS SER-1764 AND PRO-1779. RC TISSUE=Lung; RX PubMed=9166594; DOI=10.1007/s003359900467; RA Iacovacci S., Gagnoux-Palacios L., Zambruno G., Meneguzzi G., D'Alessio M.; RT "Genomic organization of the human integrin beta 4 gene."; RL Mamm. Genome 8:448-450(1997). RN [6] RP SEQUENCE REVISION. RA D'Alessio M.; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM BETA-4E), AND VARIANT RP PRO-1779. RX PubMed=9207246; DOI=10.1006/bbrc.1997.6892; RA van Leusden M.R., Kuikman I., Sonnenberg A.; RT "The unique cytoplasmic domain of the human integrin variant beta4E is RT produced by partial retention of intronic sequences."; RL Biochem. Biophys. Res. Commun. 235:826-830(1997). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-4A), AND VARIANT RP PRO-1779. RC TISSUE=Cerebellum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP PROTEIN SEQUENCE OF 28-46. RX PubMed=2542022; DOI=10.1002/j.1460-2075.1989.tb03425.x; RA Kajiji S., Tamura R.N., Quaranta V.; RT "A novel integrin (alpha E beta 4) from human epithelial cells suggests a RT fourth family of integrin adhesion receptors."; RL EMBO J. 8:673-680(1989). RN [12] RP ALTERNATIVE SPLICING (ISOFORM BETA-4D). RX PubMed=7982032; DOI=10.3109/15419069409014197; RA Clarke A.S., Lotz M.M., Mercurio A.M.; RT "A novel structural variant of the human beta 4 integrin cDNA."; RL Cell Adhes. Commun. 2:1-6(1994). RN [13] RP INTERACTION WITH DSP. RX PubMed=10637308; DOI=10.1091/mbc.11.1.277; RA Hopkinson S.B., Jones J.C.; RT "The N terminus of the transmembrane protein BP180 interacts with the N- RT terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage RT to the cell surface at the site of the hemidesmosome."; RL Mol. Biol. Cell 11:277-286(2000). RN [14] RP INTERACTION WITH DST. RX PubMed=11375975; DOI=10.1074/jbc.m011005200; RA Favre B., Fontao L., Koster J., Shafaatian R., Jaunin F., Saurat J.-H., RA Sonnenberg A., Borradori L.; RT "The hemidesmosomal protein bullous pemphigoid antigen 1 and the integrin RT beta 4 subunit bind to ERBIN. Molecular cloning of multiple alternative RT splice variants of ERBIN and analysis of their tissue expression."; RL J. Biol. Chem. 276:32427-32436(2001). RN [15] RP INVOLVEMENT IN JEB5A. RX PubMed=12485428; DOI=10.1046/j.1523-1747.2002.19609.x; RA Jonkman M.F., Pas H.H., Nijenhuis M., Kloosterhuis G., Steege G.; RT "Deletion of a cytoplasmic domain of integrin beta4 causes epidermolysis RT bullosa simplex."; RL J. Invest. Dermatol. 119:1275-1281(2002). RN [16] RP FUNCTION, INTERACTION WITH COL17A1 AND DST, CHARACTERIZATION OF VARIANT RP TRP-1281, AND SUBCELLULAR LOCATION. RX PubMed=12482924; DOI=10.1242/jcs.00241; RA Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A.; RT "Analysis of the interactions between BP180, BP230, plectin and the RT integrin alpha6beta4 important for hemidesmosome assembly."; RL J. Cell Sci. 116:387-399(2003). RN [17] RP PALMITOYLATION. RX PubMed=15611341; DOI=10.1083/jcb.200404100; RA Yang X., Kovalenko O.V., Tang W., Claas C., Stipp C.S., Hemler M.E.; RT "Palmitoylation supports assembly and function of integrin-tetraspanin RT complexes."; RL J. Cell Biol. 167:1231-1240(2004). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-695. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1530, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [21] RP FUNCTION, INTERACTION WITH RAC1, AND SUBCELLULAR LOCATION. RX PubMed=19403692; DOI=10.1091/mbc.e09-01-0051; RA Hamill K.J., Hopkinson S.B., DeBiase P., Jones J.C.; RT "BPAG1e maintains keratinocyte polarity through beta4 integrin-mediated RT modulation of Rac1 and cofilin activities."; RL Mol. Biol. Cell 20:2954-2962(2009). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [23] RP FUNCTION, BINDING TO NRG1, IDENTIFICATION IN A COMPLEX WITH NRG1 AND ERBB3, RP AND NRG1-BINDING REGION. RX PubMed=20682778; DOI=10.1074/jbc.m110.113878; RA Ieguchi K., Fujita M., Ma Z., Davari P., Taniguchi Y., Sekiguchi K., RA Wang B., Takada Y.K., Takada Y.; RT "Direct binding of the EGF-like domain of neuregulin-1 to integrins RT ({alpha}v{beta}3 and {alpha}6{beta}4) is involved in neuregulin-1/ErbB RT signaling."; RL J. Biol. Chem. 285:31388-31398(2010). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [25] RP PALMITOYLATION BY DHHC3, AND SUBCELLULAR LOCATION. RX PubMed=22314500; DOI=10.1007/s00018-012-0924-6; RA Sharma C., Rabinovitz I., Hemler M.E.; RT "Palmitoylation by DHHC3 is critical for the function, expression, and RT stability of integrin alpha6beta4."; RL Cell. Mol. Life Sci. 69:2233-2244(2012). RN [26] RP FUNCTION, BINDING TO IGF1, IDENTIFICATION IN A COMPLEX WITH IGF1 AND IGF1R, RP AND IGF1-BINDING REGION. RX PubMed=22351760; DOI=10.1074/jbc.m111.304170; RA Fujita M., Ieguchi K., Davari P., Yamaji S., Taniguchi Y., Sekiguchi K., RA Takada Y.K., Takada Y.; RT "Cross-talk between integrin alpha6beta4 and insulin-like growth factor-1 RT receptor (IGF1R) through direct alpha6beta4 binding to IGF1 and subsequent RT alpha6beta4-IGF1-IGF1R ternary complex formation in anchorage-independent RT conditions."; RL J. Biol. Chem. 287:12491-12500(2012). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1069; SER-1454; SER-1457; RP SER-1474; THR-1487 AND THR-1530, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [28] RP FUNCTION, AND INTERACTION WITH IGF2. RX PubMed=28873464; DOI=10.1371/journal.pone.0184285; RA Cedano Prieto D.M., Cheng Y., Chang C.C., Yu J., Takada Y.K., Takada Y.; RT "Direct integrin binding to insulin-like growth factor-2 through the C- RT domain is required for insulin-like growth factor receptor type 1 (IGF1R) RT signaling."; RL PLoS ONE 12:E0184285-E0184285(2017). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1126-1320. RX PubMed=10428948; DOI=10.1093/emboj/18.15.4087; RA de Pereda J.M., Wiche G., Liddington R.C.; RT "Crystal structure of a tandem pair of fibronectin type III domains from RT the cytoplasmic tail of integrin alpha6beta4."; RL EMBO J. 18:4087-4095(1999). RN [30] RP STRUCTURE BY NMR OF 1515-1622. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the fibronectin type III domain of human integrin RT beta-4."; RL Submitted (APR-2008) to the PDB data bank. RN [31] RP VARIANTS JEB5B TYR-61; CYS-252; ARG-562 AND TRP-1281. RX PubMed=9792864; DOI=10.1086/302116; RA Pulkkinen L., Rouan F., Bruckner-Tuderman L., Wallerstein R., Garzon M., RA Brown T., Smith L., Carter W.G., Uitto J.; RT "Novel ITGB4 mutations in lethal and nonlethal variants of epidermolysis RT bullosa with pyloric atresia: missense versus nonsense."; RL Am. J. Hum. Genet. 63:1376-1387(1998). RN [32] RP VARIANT JEB5B GLY-245. RX PubMed=9422533; RA Pulkkinen L., Kim D.U., Uitto J.; RT "Epidermolysis bullosa with pyloric atresia: novel mutations in the beta-4 RT integrin gene (ITGB4)."; RL Am. J. Pathol. 152:157-166(1998). RN [33] RP VARIANT JEB5B PRO-156. RX PubMed=9546354; RA Pulkkinen L., Bruckner-Tuderman L., August C., Uitto J.; RT "Compound heterozygosity for missense (L156P) and nonsense (R554X) RT mutations in the beta-4 integrin gene (ITGB4) underlies mild, nonlethal RT phenotype of epidermolysis bullosa with pyloric atresia."; RL Am. J. Pathol. 152:935-941(1998). RN [34] RP VARIANT JEB5B ARG-38. RX PubMed=9892956; DOI=10.1046/j.1365-2133.1998.02515.x; RA Mellerio J.E., Pulkkinen L., McMillan J.R., Lake B.D., Horn H.M., RA Tidman M.J., Harper J.I., McGrath J.A., Uitto J., Eady R.A.J.; RT "Pyloric atresia-junctional epidermolysis bullosa syndrome: mutations in RT the integrin beta4 gene (ITGB4) in two unrelated patients with mild RT disease."; RL Br. J. Dermatol. 139:862-871(1998). RN [35] RP VARIANT JEB5B TRP-1281. RX PubMed=10873890; DOI=10.1053/ajkd.2000.8293; RA Kambham N., Tanji N., Seigle R.L., Markowitz G.S., Pulkkinen L., Uitto J., RA D'Agati V.D.; RT "Congenital focal segmental glomerulosclerosis associated with beta4 RT integrin mutation and epidermolysis bullosa."; RL Am. J. Kidney Dis. 36:190-196(2000). RN [36] RP VARIANT JEB5A ASP-931. RX PubMed=10792571; DOI=10.1046/j.1523-1747.2000.00960-3.x; RA Inoue M., Tamai K., Shimizu H., Owaribe K., Nakama T., Hashimoto T., RA McGrath J.A.; RT "A homozygous missense mutation in the cytoplasmic tail of beta4 integrin, RT G931D, that disrupts hemidesmosome assembly and underlies non-Herlitz RT junctional epidermolysis bullosa without pyloric atresia?"; RL J. Invest. Dermatol. 114:1061-1064(2000). RN [37] RP VARIANTS JEB5B. RX PubMed=11251584; DOI=10.1046/j.1365-2133.2001.04038.x; RA Ashton G.H.S., Sorelli P., Mellerio J.E., Keane F.M., Eady R.A.J., RA McGrath J.A.; RT "Alpha 6 beta 4 integrin abnormalities in junctional epidermolysis bullosa RT with pyloric atresia."; RL Br. J. Dermatol. 144:408-414(2001). RN [38] RP VARIANTS HIS-98 AND LEU-844. RX PubMed=11289717; DOI=10.1007/s100380170122; RA Hirano A., Nagai H., Harada H., Terada Y., Haga S., Kajiwara T., Emi M.; RT "Nine novel single-nucleotide polymorphisms in the integrin beta4 (ITGB4) RT gene in the Japanese population."; RL J. Hum. Genet. 46:35-37(2001). RN [39] RP VARIANTS JEB5B TYR-131; CYS-252; ASP-273; CYS-283; ASP-325; PRO-336 AND RP HIS-1225, AND VARIANT GLN-1216. RX PubMed=11328943; DOI=10.1203/00006450-200105000-00003; RA Nakano A., Pulkkinen L., Murrell D., Rico J., Lucky A.W., Garzon M., RA Stevens C.A., Robertson S., Pfendner E., Uitto J.; RT "Epidermolysis bullosa with congenital pyloric atresia: novel mutations in RT the beta 4 integrin gene (ITGB4) and genotype/phenotype correlations."; RL Pediatr. Res. 49:618-626(2001). CC -!- FUNCTION: Integrin alpha-6/beta-4 is a receptor for laminin. Plays a CC critical structural role in the hemidesmosome of epithelial cells. Is CC required for the regulation of keratinocyte polarity and motility. CC ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is CC essential for NRG1-ERBB signaling (PubMed:20682778). ITGA6:ITGB4 binds CC to IGF1 and this binding is essential for IGF1 signaling CC (PubMed:22351760). ITGA6:ITGB4 binds to IGF2 and this binding is CC essential for IGF2 signaling (PubMed:28873464). CC {ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692, CC ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:22351760, CC ECO:0000269|PubMed:28873464}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-4 associates CC with alpha-6. Interacts (via cytoplasmic region) with COL17A1 (via CC cytoplasmic region). Interacts (via cytoplasmic region) with DST CC isoform 3 (via N-terminus). Isoform beta-4a interacts (via cytoplasmic CC domain) with DST (via N-terminus). Interacts with RAC1. ITGA6:ITGB4 is CC found in a ternary complex with NRG1 and ERBB3 (PubMed:20682778). CC ITGA6:ITGB4 is found in a ternary complex with IGF1 and IGF1R CC (PubMed:22351760). ITGA6:ITGB4 interacts with IGF2 (PubMed:28873464). CC {ECO:0000269|PubMed:10637308, ECO:0000269|PubMed:11375975, CC ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:19403692, CC ECO:0000269|PubMed:20682778, ECO:0000269|PubMed:22351760, CC ECO:0000269|PubMed:28873464}. CC -!- INTERACTION: CC P16144; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-948678, EBI-2875665; CC P16144; P23229: ITGA6; NbExp=3; IntAct=EBI-948678, EBI-2436548; CC P16144; Q15149: PLEC; NbExp=7; IntAct=EBI-948678, EBI-297903; CC P16144; Q05397: PTK2; NbExp=7; IntAct=EBI-948678, EBI-702142; CC P16144; O95136: S1PR2; NbExp=2; IntAct=EBI-948678, EBI-10634606; CC P16144; Q99500: S1PR3; NbExp=3; IntAct=EBI-948678, EBI-10634734; CC P16144; Q8R5M8-2: Cadm1; Xeno; NbExp=3; IntAct=EBI-948678, EBI-5651941; CC P16144; Q9QXS1-3: Plec; Xeno; NbExp=4; IntAct=EBI-948678, EBI-16145475; CC P16144-2; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-11051601, EBI-10173507; CC P16144-2; Q92624: APPBP2; NbExp=3; IntAct=EBI-11051601, EBI-743771; CC P16144-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11051601, EBI-3867333; CC P16144-2; Q16610: ECM1; NbExp=3; IntAct=EBI-11051601, EBI-947964; CC P16144-2; P49639: HOXA1; NbExp=3; IntAct=EBI-11051601, EBI-740785; CC P16144-2; Q5T749: KPRP; NbExp=3; IntAct=EBI-11051601, EBI-10981970; CC P16144-2; Q15323: KRT31; NbExp=3; IntAct=EBI-11051601, EBI-948001; CC P16144-2; Q6A162: KRT40; NbExp=3; IntAct=EBI-11051601, EBI-10171697; CC P16144-2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-11051601, EBI-11959885; CC P16144-2; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-11051601, EBI-11749135; CC P16144-2; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-11051601, EBI-10172290; CC P16144-2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-11051601, EBI-10171774; CC P16144-2; P60411: KRTAP10-9; NbExp=5; IntAct=EBI-11051601, EBI-10172052; CC P16144-2; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-11051601, EBI-11953334; CC P16144-2; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-11051601, EBI-11992140; CC P16144-2; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-11051601, EBI-11988175; CC P16144-2; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-11051601, EBI-14065470; CC P16144-2; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-11051601, EBI-9996449; CC P16144-2; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-11051601, EBI-10172511; CC P16144-2; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-11051601, EBI-11962084; CC P16144-2; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-11051601, EBI-1044640; CC P16144-2; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-11051601, EBI-1043191; CC P16144-2; Q99750: MDFI; NbExp=3; IntAct=EBI-11051601, EBI-724076; CC P16144-2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-11051601, EBI-10172526; CC P16144-2; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-11051601, EBI-11522433; CC P16144-2; P13349: MYF5; NbExp=3; IntAct=EBI-11051601, EBI-17491620; CC P16144-2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-11051601, EBI-22310682; CC P16144-2; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-11051601, EBI-769257; CC P16144-2; Q16633: POU2AF1; NbExp=3; IntAct=EBI-11051601, EBI-943588; CC P16144-2; P22735: TGM1; NbExp=3; IntAct=EBI-11051601, EBI-2562368; CC P16144-2; Q15654: TRIP6; NbExp=3; IntAct=EBI-11051601, EBI-742327; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Cell membrane; Lipid-anchor. Cell junction, hemidesmosome. CC Note=Colocalizes with DST at the leading edge of migrating CC keratinocytes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=Beta-4C; CC IsoId=P16144-1; Sequence=Displayed; CC Name=Beta-4A; CC IsoId=P16144-2; Sequence=VSP_002749; CC Name=Beta-4B; CC IsoId=P16144-3; Sequence=VSP_002749, VSP_002750; CC Name=Beta-4D; CC IsoId=P16144-4; Sequence=VSP_002749, VSP_002751; CC Name=Beta-4E; CC IsoId=P16144-5; Sequence=VSP_002747, VSP_002748; CC -!- TISSUE SPECIFICITY: Integrin alpha-6/beta-4 is predominantly expressed CC by epithelia. Isoform beta-4D is also expressed in colon and placenta. CC Isoform beta-4E is also expressed in epidermis, lung, duodenum, heart, CC spleen and stomach. CC -!- DOMAIN: The fibronectin type-III-like domains bind BPAG1 and plectin CC and probably also recruit BP230. CC -!- PTM: Palmitoylated by DHHC3 at several cysteines of the membrane- CC proximal region, enhancing stability and cell surface expression. CC Palmitoylation also promotes secondary association with tertaspanins. CC {ECO:0000269|PubMed:15611341, ECO:0000269|PubMed:22314500}. CC -!- DISEASE: Epidermolysis bullosa, junctional 5A, intermediate (JEB5A) CC [MIM:619816]: A form of epidermolysis bullosa, a genodermatosis CC characterized by recurrent blistering, fragility of the skin and CC mucosal epithelia, and erosions caused by minor mechanical trauma. CC JEB5A is an autosomal recessive, intermediate form in which blistering CC lesions occur between the epidermis and the dermis at the lamina lucida CC level of the basement membrane zone. In intermediate forms of CC junctional epidermolysis bullosa, blistering does not lead to the CC formation of chronic granulation tissue and does not affect the CC lifespan of affected individuals. Nail dystrophy and dental enamel CC defects are present. Scarring or non-scarring alopecia and diffuse hair CC loss may occur. {ECO:0000269|PubMed:10792571, CC ECO:0000269|PubMed:12485428}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Epidermolysis bullosa, junctional 5B, with pyloric atresia CC (JEB5B) [MIM:226730]: A form of epidermolysis bullosa, a genodermatosis CC characterized by recurrent blistering, fragility of the skin and CC mucosal epithelia, and erosions caused by minor mechanical trauma. CC Junctional epidermolysis bullosa is characterized by blistering that CC occurs at the level of the lamina lucida in the skin basement membrane. CC JEB5B is an autosomal recessive, severe, frequently lethal form with CC variable involvement of skin, nails, mucosa, and with variable effects CC on the digestive system. It is characterized by mucocutaneous CC fragility, aplasia cutis congenita, and gastrointestinal atresia, which CC most commonly affects the pylorus. Pyloric atresia is a primary CC manifestation rather than a scarring process secondary to epidermolysis CC bullosa. {ECO:0000269|PubMed:10873890, ECO:0000269|PubMed:11251584, CC ECO:0000269|PubMed:11328943, ECO:0000269|PubMed:9422533, CC ECO:0000269|PubMed:9546354, ECO:0000269|PubMed:9792864, CC ECO:0000269|PubMed:9892956}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA37656.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X51841; CAA36134.1; -; mRNA. DR EMBL; X52186; CAA36433.1; -; mRNA. DR EMBL; X53587; CAA37656.1; ALT_FRAME; mRNA. DR EMBL; U66541; AAC51634.1; -; Genomic_DNA. DR EMBL; U66530; AAC51634.1; JOINED; Genomic_DNA. DR EMBL; U66531; AAC51634.1; JOINED; Genomic_DNA. DR EMBL; U66532; AAC51634.1; JOINED; Genomic_DNA. DR EMBL; U66533; AAC51634.1; JOINED; Genomic_DNA. DR EMBL; U66534; AAC51634.1; JOINED; Genomic_DNA. DR EMBL; U66535; AAC51634.1; JOINED; Genomic_DNA. DR EMBL; U66536; AAC51634.1; JOINED; Genomic_DNA. DR EMBL; U66537; AAC51634.1; JOINED; Genomic_DNA. DR EMBL; U66538; AAC51634.1; JOINED; Genomic_DNA. DR EMBL; U66539; AAC51634.1; JOINED; Genomic_DNA. DR EMBL; U66540; AAC51634.1; JOINED; Genomic_DNA. DR EMBL; U66541; AAC51633.1; -; Genomic_DNA. DR EMBL; U66530; AAC51633.1; JOINED; Genomic_DNA. DR EMBL; U66531; AAC51633.1; JOINED; Genomic_DNA. DR EMBL; U66532; AAC51633.1; JOINED; Genomic_DNA. DR EMBL; U66533; AAC51633.1; JOINED; Genomic_DNA. DR EMBL; U66534; AAC51633.1; JOINED; Genomic_DNA. DR EMBL; U66535; AAC51633.1; JOINED; Genomic_DNA. DR EMBL; U66536; AAC51633.1; JOINED; Genomic_DNA. DR EMBL; U66537; AAC51633.1; JOINED; Genomic_DNA. DR EMBL; U66538; AAC51633.1; JOINED; Genomic_DNA. DR EMBL; U66539; AAC51633.1; JOINED; Genomic_DNA. DR EMBL; U66540; AAC51633.1; JOINED; Genomic_DNA. DR EMBL; U66541; AAC51632.1; -; Genomic_DNA. DR EMBL; U66530; AAC51632.1; JOINED; Genomic_DNA. DR EMBL; U66531; AAC51632.1; JOINED; Genomic_DNA. DR EMBL; U66532; AAC51632.1; JOINED; Genomic_DNA. DR EMBL; U66533; AAC51632.1; JOINED; Genomic_DNA. DR EMBL; U66534; AAC51632.1; JOINED; Genomic_DNA. DR EMBL; U66535; AAC51632.1; JOINED; Genomic_DNA. DR EMBL; U66536; AAC51632.1; JOINED; Genomic_DNA. DR EMBL; U66537; AAC51632.1; JOINED; Genomic_DNA. DR EMBL; U66538; AAC51632.1; JOINED; Genomic_DNA. DR EMBL; U66539; AAC51632.1; JOINED; Genomic_DNA. DR EMBL; U66540; AAC51632.1; JOINED; Genomic_DNA. DR EMBL; AC087749; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471099; EAW89305.1; -; Genomic_DNA. DR EMBL; BC118916; AAI18917.1; -; mRNA. DR EMBL; BC126411; AAI26412.1; -; mRNA. DR EMBL; AJ251004; CAB61345.1; -; Genomic_DNA. DR EMBL; Y11107; CAB61345.1; JOINED; Genomic_DNA. DR EMBL; AF011375; AAB65421.1; -; mRNA. DR EMBL; AF011376; AAB65422.1; -; Genomic_DNA. DR CCDS; CCDS11727.1; -. [P16144-1] DR CCDS; CCDS32736.1; -. [P16144-3] DR CCDS; CCDS58599.1; -. [P16144-2] DR PIR; JC5545; JC5545. DR PIR; S12380; A36429. DR RefSeq; NP_000204.3; NM_000213.4. [P16144-1] DR RefSeq; NP_001005619.1; NM_001005619.1. [P16144-3] DR RefSeq; NP_001005731.1; NM_001005731.2. [P16144-2] DR RefSeq; NP_001308052.1; NM_001321123.1. [P16144-2] DR PDB; 1QG3; X-ray; 2.15 A; A/B=1126-1320. DR PDB; 2YRZ; NMR; -; A=1518-1622. DR PDB; 3F7P; X-ray; 2.75 A; C/D/E=1126-1369. DR PDB; 3F7Q; X-ray; 1.75 A; A/B=1126-1355. DR PDB; 3F7R; X-ray; 2.04 A; A=1126-1369. DR PDB; 3FQ4; X-ray; 1.49 A; A/B=989-1107. DR PDB; 3FSO; X-ray; 1.41 A; A/B=989-1107. DR PDB; 3H6A; X-ray; 1.61 A; A/B=989-1107. DR PDB; 4Q58; X-ray; 4.00 A; C/D=1126-1320. DR PDB; 4WTW; X-ray; 1.61 A; A/B=1527-1618. DR PDB; 4WTX; X-ray; 1.50 A; A=1642-1736. DR PDB; 6GVK; X-ray; 1.55 A; A=1527-1736. DR PDB; 6GVL; X-ray; 2.05 A; A=1527-1736. DR PDBsum; 1QG3; -. DR PDBsum; 2YRZ; -. DR PDBsum; 3F7P; -. DR PDBsum; 3F7Q; -. DR PDBsum; 3F7R; -. DR PDBsum; 3FQ4; -. DR PDBsum; 3FSO; -. DR PDBsum; 3H6A; -. DR PDBsum; 4Q58; -. DR PDBsum; 4WTW; -. DR PDBsum; 4WTX; -. DR PDBsum; 6GVK; -. DR PDBsum; 6GVL; -. DR AlphaFoldDB; P16144; -. DR SASBDB; P16144; -. DR SMR; P16144; -. DR BioGRID; 109897; 112. DR ComplexPortal; CPX-1822; Integrin alpha6-beta4 complex. DR CORUM; P16144; -. DR DIP; DIP-40182N; -. DR ELM; P16144; -. DR IntAct; P16144; 118. DR MINT; P16144; -. DR STRING; 9606.ENSP00000200181; -. DR DrugBank; DB05122; R1295. DR GlyConnect; 1417; 1 N-Linked glycan (1 site). DR GlyGen; P16144; 7 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P16144; -. DR PhosphoSitePlus; P16144; -. DR SwissPalm; P16144; -. DR BioMuta; ITGB4; -. DR DMDM; 317373584; -. DR CPTAC; CPTAC-530; -. DR CPTAC; CPTAC-531; -. DR EPD; P16144; -. DR jPOST; P16144; -. DR MassIVE; P16144; -. DR MaxQB; P16144; -. DR PaxDb; P16144; -. DR PeptideAtlas; P16144; -. DR ProteomicsDB; 53292; -. [P16144-1] DR ProteomicsDB; 53293; -. [P16144-2] DR ProteomicsDB; 53294; -. [P16144-3] DR ProteomicsDB; 53295; -. [P16144-4] DR ProteomicsDB; 53296; -. [P16144-5] DR ABCD; P16144; 3 sequenced antibodies. DR Antibodypedia; 3934; 1070 antibodies from 43 providers. DR DNASU; 3691; -. DR Ensembl; ENST00000200181.8; ENSP00000200181.3; ENSG00000132470.14. [P16144-1] DR Ensembl; ENST00000449880.6; ENSP00000400217.2; ENSG00000132470.14. [P16144-3] DR Ensembl; ENST00000450894.7; ENSP00000405536.3; ENSG00000132470.14. [P16144-2] DR Ensembl; ENST00000579662.5; ENSP00000463651.1; ENSG00000132470.14. [P16144-2] DR GeneID; 3691; -. DR KEGG; hsa:3691; -. DR MANE-Select; ENST00000200181.8; ENSP00000200181.3; NM_000213.5; NP_000204.3. DR UCSC; uc002jpg.3; human. [P16144-1] DR CTD; 3691; -. DR DisGeNET; 3691; -. DR GeneCards; ITGB4; -. DR GeneReviews; ITGB4; -. DR HGNC; HGNC:6158; ITGB4. DR HPA; ENSG00000132470; Tissue enhanced (salivary gland, skin). DR MalaCards; ITGB4; -. DR MIM; 147557; gene. DR MIM; 226730; phenotype. DR MIM; 619816; phenotype. DR neXtProt; NX_P16144; -. DR OpenTargets; ENSG00000132470; -. DR Orphanet; 1114; Aplasia cutis congenita. DR Orphanet; 158684; Epidermolysis bullosa simplex with pyloric atresia. DR Orphanet; 79402; Intermediate generalized junctional epidermolysis bullosa. DR Orphanet; 79403; Junctional epidermolysis bullosa with pyloric atresia. DR Orphanet; 251393; Localized junctional epidermolysis bullosa. DR PharmGKB; PA29957; -. DR VEuPathDB; HostDB:ENSG00000132470; -. DR eggNOG; KOG1226; Eukaryota. DR GeneTree; ENSGT00980000198528; -. DR HOGENOM; CLU_237558_0_0_1; -. DR InParanoid; P16144; -. DR OMA; YGPVNED; -. DR OrthoDB; 473040at2759; -. DR PhylomeDB; P16144; -. DR TreeFam; TF105392; -. DR PathwayCommons; P16144; -. DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures. DR Reactome; R-HSA-3000157; Laminin interactions. DR Reactome; R-HSA-3000170; Syndecan interactions. DR Reactome; R-HSA-446107; Type I hemidesmosome assembly. DR SignaLink; P16144; -. DR SIGNOR; P16144; -. DR BioGRID-ORCS; 3691; 12 hits in 1080 CRISPR screens. DR ChiTaRS; ITGB4; human. DR EvolutionaryTrace; P16144; -. DR GeneWiki; ITGB4; -. DR GenomeRNAi; 3691; -. DR Pharos; P16144; Tbio. DR PRO; PR:P16144; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P16144; protein. DR Bgee; ENSG00000132470; Expressed in tibial nerve and 186 other tissues. DR ExpressionAtlas; P16144; baseline and differential. DR Genevisible; P16144; HS. DR GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl. DR GO; GO:0005604; C:basement membrane; IEA:Ensembl. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central. DR GO; GO:0030056; C:hemidesmosome; IDA:UniProtKB. DR GO; GO:0008305; C:integrin complex; TAS:ProtInc. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0043235; C:receptor complex; IDA:MGI. DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:UniProtKB. DR GO; GO:0005178; F:integrin binding; IBA:GO_Central. DR GO; GO:0006914; P:autophagy; IMP:UniProtKB. DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc. DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central. DR GO; GO:0016477; P:cell migration; IBA:GO_Central. DR GO; GO:0048870; P:cell motility; IMP:UniProtKB. DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB. DR GO; GO:0046847; P:filopodium assembly; IEA:Ensembl. DR GO; GO:0031581; P:hemidesmosome assembly; IDA:UniProtKB. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB. DR GO; GO:0035878; P:nail development; IMP:UniProtKB. DR GO; GO:0032290; P:peripheral nervous system myelin formation; IEA:Ensembl. DR GO; GO:0009611; P:response to wounding; IDA:UniProtKB. DR GO; GO:0043589; P:skin morphogenesis; IMP:UniProtKB. DR GO; GO:0061450; P:trophoblast cell migration; IEA:Ensembl. DR CDD; cd00063; FN3; 4. DR Gene3D; 2.60.40.10; -; 4. DR Gene3D; 2.60.40.2030; -; 1. DR Gene3D; 3.40.50.410; -; 1. DR InterPro; IPR038081; CalX-like_sf. DR InterPro; IPR003644; Calx_beta. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR013111; EGF_extracell. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR040622; I-EGF_1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR033760; Integrin_beta_N. DR InterPro; IPR015812; Integrin_bsu. DR InterPro; IPR012013; Integrin_bsu-4. DR InterPro; IPR012896; Integrin_bsu_tail. DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf. DR InterPro; IPR002369; Integrin_bsu_VWA. DR InterPro; IPR016201; PSI. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 2. DR PANTHER; PTHR10082:SF42; INTEGRIN BETA-4; 2. DR Pfam; PF03160; Calx-beta; 1. DR Pfam; PF07974; EGF_2; 1. DR Pfam; PF00041; fn3; 4. DR Pfam; PF18372; I-EGF_1; 1. DR Pfam; PF07965; Integrin_B_tail; 1. DR Pfam; PF00362; Integrin_beta; 1. DR Pfam; PF17205; PSI_integrin; 1. DR PIRSF; PIRSF002513; Integrin_B4; 1. DR PRINTS; PR01186; INTEGRINB. DR SMART; SM00237; Calx_beta; 1. DR SMART; SM00060; FN3; 4. DR SMART; SM00187; INB; 1. DR SMART; SM01242; Integrin_B_tail; 1. DR SMART; SM00423; PSI; 1. DR SUPFAM; SSF141072; CalX-like; 1. DR SUPFAM; SSF49265; Fibronectin type III; 2. DR SUPFAM; SSF69687; Integrin beta tail domain; 1. DR SUPFAM; SSF53300; vWA-like; 1. DR PROSITE; PS00022; EGF_1; 2. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50853; FN3; 4. DR PROSITE; PS00243; INTEGRIN_BETA; 2. DR AGR; HGNC:6158; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction; KW Cell membrane; Direct protein sequencing; Disease variant; Disulfide bond; KW Epidermolysis bullosa; Glycoprotein; Integrin; Lipoprotein; Membrane; KW Palmitate; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..27 FT /evidence="ECO:0000269|PubMed:2542022" FT CHAIN 28..1822 FT /note="Integrin beta-4" FT /id="PRO_0000016346" FT TOPO_DOM 28..710 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 711..733 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 734..1822 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 29..73 FT /note="PSI" FT DOMAIN 131..329 FT /note="VWFA" FT REPEAT 456..502 FT /note="I" FT REPEAT 503..542 FT /note="II" FT REPEAT 543..581 FT /note="III" FT REPEAT 582..619 FT /note="IV" FT DOMAIN 979..1084 FT /note="Calx-beta" FT DOMAIN 1129..1218 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1222..1321 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1530..1625 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1643..1739 FT /note="Fibronectin type-III 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 194..199 FT /note="Involved in NRG1- and IGF1-binding" FT /evidence="ECO:0000269|PubMed:20682778, FT ECO:0000269|PubMed:22351760" FT REGION 456..619 FT /note="Cysteine-rich tandem repeats" FT REGION 732..749 FT /note="Palmitoylated on several cysteines" FT REGION 1113..1140 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1400..1444 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1495..1525 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 771 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q64632" FT MOD_RES 1069 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1119 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q64632" FT MOD_RES 1454 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1457 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1474 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1487 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1494 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q64632" FT MOD_RES 1530 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1791 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q64632" FT CARBOHYD 327 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 491 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 579 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 617 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 695 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT DISULFID 30..455 FT /evidence="ECO:0000250" FT DISULFID 38..48 FT /evidence="ECO:0000250" FT DISULFID 41..72 FT /evidence="ECO:0000250" FT DISULFID 51..61 FT /evidence="ECO:0000250" FT DISULFID 245..288 FT /evidence="ECO:0000250" FT DISULFID 424..671 FT /evidence="ECO:0000250" FT DISULFID 452..457 FT /evidence="ECO:0000250" FT DISULFID 468..479 FT /evidence="ECO:0000250" FT DISULFID 476..512 FT /evidence="ECO:0000250" FT DISULFID 481..490 FT /evidence="ECO:0000250" FT DISULFID 492..503 FT /evidence="ECO:0000250" FT DISULFID 518..523 FT /evidence="ECO:0000250" FT DISULFID 520..551 FT /evidence="ECO:0000250" FT DISULFID 525..536 FT /evidence="ECO:0000250" FT DISULFID 557..562 FT /evidence="ECO:0000250" FT DISULFID 564..573 FT /evidence="ECO:0000250" FT DISULFID 575..582 FT /evidence="ECO:0000250" FT DISULFID 596..601 FT /evidence="ECO:0000250" FT DISULFID 598..648 FT /evidence="ECO:0000250" FT DISULFID 603..614 FT /evidence="ECO:0000250" FT DISULFID 626..635 FT /evidence="ECO:0000250" FT DISULFID 632..706 FT /evidence="ECO:0000250" FT DISULFID 651..680 FT /evidence="ECO:0000250" FT VAR_SEQ 851..964 FT /note="LNEVYRQISGVHKLQQTKFRQQPNAGKKQDHTIVDTVLMAPRSAKPALLKLT FT EKQVEQRAFHDLKVAPGYYTLTADQDARGMVEFQEGVELVDVRVPLFIRPEDDDEKQLL FT VEA -> VRTQELGLAGDVAERGLQADLRCTQAPADQVPAAAQCREKARPHHCGHSADG FT APLGQAGPAEAYREAGGTEGLPRPQGGPRLLHPHCRPGRPGHGGVPGGRGAGGRTGAPL FT YPA (in isoform Beta-4E)" FT /evidence="ECO:0000303|PubMed:9207246" FT /id="VSP_002747" FT VAR_SEQ 965..1822 FT /note="Missing (in isoform Beta-4E)" FT /evidence="ECO:0000303|PubMed:9207246" FT /id="VSP_002748" FT VAR_SEQ 1370..1439 FT /note="Missing (in isoform Beta-4A, isoform Beta-4B and FT isoform Beta-4D)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:2311577, ECO:0000303|PubMed:2311578, FT ECO:0000303|PubMed:9194858" FT /id="VSP_002749" FT VAR_SEQ 1519 FT /note="H -> HGLPPIWEHGRSRLPLSWALGSRSRAQMKGFPPSRGPRDSIILAGRP FT AAPSWGP (in isoform Beta-4B)" FT /evidence="ECO:0000303|PubMed:2311578, FT ECO:0000303|PubMed:9194858" FT /id="VSP_002750" FT VAR_SEQ 1678..1685 FT /note="CEMAQGGG -> W (in isoform Beta-4D)" FT /evidence="ECO:0000305" FT /id="VSP_002751" FT VARIANT 38 FT /note="C -> R (in JEB5B; dbSNP:rs121912465)" FT /evidence="ECO:0000269|PubMed:9892956" FT /id="VAR_010652" FT VARIANT 61 FT /note="C -> Y (in JEB5B; dbSNP:rs80338755)" FT /evidence="ECO:0000269|PubMed:9792864" FT /id="VAR_004006" FT VARIANT 98 FT /note="R -> H (in dbSNP:rs143114124)" FT /evidence="ECO:0000269|PubMed:11289717" FT /id="VAR_011292" FT VARIANT 131 FT /note="D -> Y (in JEB5B)" FT /evidence="ECO:0000269|PubMed:11328943" FT /id="VAR_011293" FT VARIANT 156 FT /note="L -> P (in JEB5B; dbSNP:rs121912461)" FT /evidence="ECO:0000269|PubMed:9546354" FT /id="VAR_004007" FT VARIANT 245 FT /note="C -> G (in JEB5B)" FT /evidence="ECO:0000269|PubMed:9422533" FT /id="VAR_004008" FT VARIANT 252 FT /note="R -> C (in JEB5B; dbSNP:rs201494421)" FT /evidence="ECO:0000269|PubMed:11328943, FT ECO:0000269|PubMed:9792864" FT /id="VAR_004009" FT VARIANT 273 FT /note="G -> D (in JEB5B; dbSNP:rs1476568580)" FT /evidence="ECO:0000269|PubMed:11328943" FT /id="VAR_011294" FT VARIANT 283 FT /note="R -> C (in JEB5B; dbSNP:rs1422797135)" FT /evidence="ECO:0000269|PubMed:11328943" FT /id="VAR_011295" FT VARIANT 325 FT /note="V -> D (in JEB5B; dbSNP:rs1304888529)" FT /evidence="ECO:0000269|PubMed:11328943" FT /id="VAR_011296" FT VARIANT 336 FT /note="L -> P (in JEB5B)" FT /evidence="ECO:0000269|PubMed:11328943" FT /id="VAR_011297" FT VARIANT 478 FT /note="Q -> H (in dbSNP:rs8079267)" FT /id="VAR_027803" FT VARIANT 562 FT /note="C -> R (in JEB5B; dbSNP:rs121912463)" FT /evidence="ECO:0000269|PubMed:9792864" FT /id="VAR_004010" FT VARIANT 844 FT /note="R -> L (in dbSNP:rs140819116)" FT /evidence="ECO:0000269|PubMed:11289717" FT /id="VAR_011298" FT VARIANT 931 FT /note="G -> D (in JEB5A; dbSNP:rs121912466)" FT /evidence="ECO:0000269|PubMed:10792571" FT /id="VAR_011299" FT VARIANT 1216 FT /note="H -> Q (in dbSNP:rs149284152)" FT /evidence="ECO:0000269|PubMed:11328943" FT /id="VAR_011300" FT VARIANT 1225 FT /note="R -> H (in JEB5B; dbSNP:rs121912468)" FT /evidence="ECO:0000269|PubMed:11328943" FT /id="VAR_011301" FT VARIANT 1281 FT /note="R -> W (in JEB5B; abolishes interaction with FT PLEC and reduces interaction with COL17A1; FT dbSNP:rs121912467)" FT /evidence="ECO:0000269|PubMed:10873890, FT ECO:0000269|PubMed:12482924, ECO:0000269|PubMed:9792864" FT /id="VAR_004011" FT VARIANT 1764 FT /note="T -> S (in dbSNP:rs1051486)" FT /evidence="ECO:0000269|PubMed:9166594, FT ECO:0000269|PubMed:9194858" FT /id="VAR_055971" FT VARIANT 1779 FT /note="L -> P (in dbSNP:rs871443)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:2311577, ECO:0000269|PubMed:2311578, FT ECO:0000269|PubMed:9166594, ECO:0000269|PubMed:9194858, FT ECO:0000269|PubMed:9207246" FT /id="VAR_027804" FT CONFLICT 27 FT /note="Missing (in Ref. 5; CAB61345)" FT /evidence="ECO:0000305" FT CONFLICT 43 FT /note="R -> Y (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 46 FT /note="K -> P (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 621..704 FT /note="IHPGLCEDLRSCVQCQAWGTGEKKGRTCEECNFKVKMVDELKRAEEVVVRCS FT FRDEDDDCTYSYTMEGDGAPGPNSTVLVHKKK -> STRASARTYAPACSARRGAPARR FT RGARVRNATSRSRWWTSLREARRWWCAAPSGTRMTTAPTATPWKVTAPLGPTALSWCTR FT RR (in Ref. 5; CAB61345)" FT /evidence="ECO:0000305" FT CONFLICT 802..804 FT /note="GFA -> WLC (in Ref. 8; AAB65422)" FT /evidence="ECO:0000305" FT CONFLICT 1414..1429 FT /note="HGPPDDGGAGGKGGSL -> TAPRTTAARAGRAAAV (in Ref. 3; FT CAA37656)" FT /evidence="ECO:0000305" FT CONFLICT 1755 FT /note="P -> L (in Ref. 10; AAI18917)" FT /evidence="ECO:0000305" FT CONFLICT 1777 FT /note="Missing (in Ref. 5; CAB61345)" FT /evidence="ECO:0000305" FT STRAND 990..995 FT /evidence="ECO:0007829|PDB:3FSO" FT STRAND 997..1002 FT /evidence="ECO:0007829|PDB:3FSO" FT HELIX 1003..1005 FT /evidence="ECO:0007829|PDB:3FSO" FT STRAND 1006..1016 FT /evidence="ECO:0007829|PDB:3FSO" FT STRAND 1022..1033 FT /evidence="ECO:0007829|PDB:3FSO" FT TURN 1035..1037 FT /evidence="ECO:0007829|PDB:3FSO" FT STRAND 1043..1048 FT /evidence="ECO:0007829|PDB:3FSO" FT STRAND 1054..1061 FT /evidence="ECO:0007829|PDB:3FSO" FT TURN 1070..1073 FT /evidence="ECO:0007829|PDB:3FQ4" FT STRAND 1076..1087 FT /evidence="ECO:0007829|PDB:3FSO" FT STRAND 1096..1103 FT /evidence="ECO:0007829|PDB:3FSO" FT STRAND 1131..1137 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1139..1141 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1143..1148 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1156..1163 FT /evidence="ECO:0007829|PDB:3F7Q" FT HELIX 1168..1170 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1172..1183 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1191..1200 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1203..1207 FT /evidence="ECO:0007829|PDB:3F7P" FT STRAND 1211..1214 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1227..1230 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1232..1234 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1236..1239 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1252..1260 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1262..1264 FT /evidence="ECO:0007829|PDB:3F7R" FT STRAND 1266..1268 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1271..1275 FT /evidence="ECO:0007829|PDB:1QG3" FT STRAND 1282..1286 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1294..1302 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1310..1314 FT /evidence="ECO:0007829|PDB:3F7Q" FT HELIX 1316..1318 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1334..1336 FT /evidence="ECO:0007829|PDB:3F7Q" FT STRAND 1344..1348 FT /evidence="ECO:0007829|PDB:3F7P" FT STRAND 1522..1524 FT /evidence="ECO:0007829|PDB:2YRZ" FT STRAND 1532..1540 FT /evidence="ECO:0007829|PDB:6GVK" FT STRAND 1543..1549 FT /evidence="ECO:0007829|PDB:6GVK" FT STRAND 1558..1566 FT /evidence="ECO:0007829|PDB:6GVK" FT TURN 1567..1569 FT /evidence="ECO:0007829|PDB:6GVK" FT STRAND 1573..1577 FT /evidence="ECO:0007829|PDB:6GVK" FT STRAND 1584..1587 FT /evidence="ECO:0007829|PDB:6GVK" FT STRAND 1595..1604 FT /evidence="ECO:0007829|PDB:6GVK" FT STRAND 1612..1620 FT /evidence="ECO:0007829|PDB:6GVK" FT TURN 1632..1635 FT /evidence="ECO:0007829|PDB:6GVK" FT STRAND 1636..1639 FT /evidence="ECO:0007829|PDB:6GVK" FT STRAND 1648..1653 FT /evidence="ECO:0007829|PDB:4WTX" FT STRAND 1656..1662 FT /evidence="ECO:0007829|PDB:4WTX" FT STRAND 1671..1680 FT /evidence="ECO:0007829|PDB:4WTX" FT STRAND 1683..1685 FT /evidence="ECO:0007829|PDB:4WTX" FT STRAND 1688..1694 FT /evidence="ECO:0007829|PDB:4WTX" FT STRAND 1697..1703 FT /evidence="ECO:0007829|PDB:4WTX" FT STRAND 1712..1722 FT /evidence="ECO:0007829|PDB:4WTX" FT STRAND 1724..1732 FT /evidence="ECO:0007829|PDB:4WTX" SQ SEQUENCE 1822 AA; 202167 MW; 09710FFBBD719469 CRC64; MAGPRPSPWA RLLLAALISV SLSGTLANRC KKAPVKSCTE CVRVDKDCAY CTDEMFRDRR CNTQAELLAA GCQRESIVVM ESSFQITEET QIDTTLRRSQ MSPQGLRVRL RPGEERHFEL EVFEPLESPV DLYILMDFSN SMSDDLDNLK KMGQNLARVL SQLTSDYTIG FGKFVDKVSV PQTDMRPEKL KEPWPNSDPP FSFKNVISLT EDVDEFRNKL QGERISGNLD APEGGFDAIL QTAVCTRDIG WRPDSTHLLV FSTESAFHYE ADGANVLAGI MSRNDERCHL DTTGTYTQYR TQDYPSVPTL VRLLAKHNII PIFAVTNYSY SYYEKLHTYF PVSSLGVLQE DSSNIVELLE EAFNRIRSNL DIRALDSPRG LRTEVTSKMF QKTRTGSFHI RRGEVGIYQV QLRALEHVDG THVCQLPEDQ KGNIHLKPSF SDGLKMDAGI ICDVCTCELQ KEVRSARCSF NGDFVCGQCV CSEGWSGQTC NCSTGSLSDI QPCLREGEDK PCSGRGECQC GHCVCYGEGR YEGQFCEYDN FQCPRTSGFL CNDRGRCSMG QCVCEPGWTG PSCDCPLSNA TCIDSNGGIC NGRGHCECGR CHCHQQSLYT DTICEINYSA IHPGLCEDLR SCVQCQAWGT GEKKGRTCEE CNFKVKMVDE LKRAEEVVVR CSFRDEDDDC TYSYTMEGDG APGPNSTVLV HKKKDCPPGS FWWLIPLLLL LLPLLALLLL LCWKYCACCK ACLALLPCCN RGHMVGFKED HYMLRENLMA SDHLDTPMLR SGNLKGRDVV RWKVTNNMQR PGFATHAASI NPTELVPYGL SLRLARLCTE NLLKPDTREC AQLRQEVEEN LNEVYRQISG VHKLQQTKFR QQPNAGKKQD HTIVDTVLMA PRSAKPALLK LTEKQVEQRA FHDLKVAPGY YTLTADQDAR GMVEFQEGVE LVDVRVPLFI RPEDDDEKQL LVEAIDVPAG TATLGRRLVN ITIIKEQARD VVSFEQPEFS VSRGDQVARI PVIRRVLDGG KSQVSYRTQD GTAQGNRDYI PVEGELLFQP GEAWKELQVK LLELQEVDSL LRGRQVRRFH VQLSNPKFGA HLGQPHSTTI IIRDPDELDR SFTSQMLSSQ PPPHGDLGAP QNPNAKAAGS RKIHFNWLPP SGKPMGYRVK YWIQGDSESE AHLLDSKVPS VELTNLYPYC DYEMKVCAYG AQGEGPYSSL VSCRTHQEVP SEPGRLAFNV VSSTVTQLSW AEPAETNGEI TAYEVCYGLV NDDNRPIGPM KKVLVDNPKN RMLLIENLRE SQPYRYTVKA RNGAGWGPER EAIINLATQP KRPMSIPIIP DIPIVDAQSG EDYDSFLMYS DDVLRSPSGS QRPSVSDDTG CGWKFEPLLG EELDLRRVTW RLPPELIPRL SASSGRSSDA EAPHGPPDDG GAGGKGGSLP RSATPGPPGE HLVNGRMDFA FPGSTNSLHR MTTTSAAAYG THLSPHVPHR VLSTSSTLTR DYNSLTRSEH SHSTTLPRDY STLTSVSSHD SRLTAGVPDT PTRLVFSALG PTSLRVSWQE PRCERPLQGY SVEYQLLNGG ELHRLNIPNP AQTSVVVEDL LPNHSYVFRV RAQSQEGWGR EREGVITIES QVHPQSPLCP LPGSAFTLST PSAPGPLVFT ALSPDSLQLS WERPRRPNGD IVGYLVTCEM AQGGGPATAF RVDGDSPESR LTVPGLSENV PYKFKVQART TEGFGPEREG IITIESQDGG PFPQLGSRAG LFQHPLQSEY SSITTTHTSA TEPFLVDGLT LGAQHLEAGG SLTRHVTQEF VSRTLTTSGT LSTHMDQQFF QT // ID PALS2_HUMAN Reviewed; 540 AA. AC Q9NZW5; A4D157; Q9H0E1; DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-FEB-2004, sequence version 2. DT 14-DEC-2022, entry version 175. DE RecName: Full=Protein PALS2 {ECO:0000305}; DE AltName: Full=MAGUK p55 subfamily member 6; DE AltName: Full=Membrane protein, palmitoylated 6; DE AltName: Full=Veli-associated MAGUK 1 {ECO:0000303|PubMed:11311936}; DE Short=VAM-1 {ECO:0000303|PubMed:11311936}; GN Name=PALS2 {ECO:0000312|HGNC:HGNC:18167}; Synonyms=MPP6, VAM1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11311936; DOI=10.1016/s0167-4781(01)00191-9; RA Tseng T.-C., Marfatia S.M., Bryant P.J., Pack S., Zhuang Z., O'Brien J.E., RA Lin L., Hanada T., Chishti A.H.; RT "VAM-1: a new member of the MAGUK family binds to human Veli-1 through a RT conserved domain."; RL Biochim. Biophys. Acta 1518:249-259(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-500, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- SUBUNIT: Interacts with CADM1 (By similarity). Interacts with the LIN7 CC proteins. {ECO:0000250}. CC -!- INTERACTION: CC Q9NZW5; O14910: LIN7A; NbExp=4; IntAct=EBI-2683764, EBI-2513988; CC Q9NZW5; Q9HAP6: LIN7B; NbExp=5; IntAct=EBI-2683764, EBI-821335; CC Q9NZW5; Q9NUP9: LIN7C; NbExp=6; IntAct=EBI-2683764, EBI-1171517; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane CC protein {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Abundant in testis, brain, and kidney with lower CC levels detectable in other tissues. CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF162130; AAD45919.2; -; mRNA. DR EMBL; AL136836; CAB66770.1; -; mRNA. DR EMBL; AC005084; AAQ96847.1; -; Genomic_DNA. DR EMBL; CH236948; EAL24247.1; -; Genomic_DNA. DR EMBL; CH471073; EAW93810.1; -; Genomic_DNA. DR EMBL; BC023638; AAH23638.1; -; mRNA. DR CCDS; CCDS5388.1; -. DR RefSeq; NP_001289966.1; NM_001303037.1. DR RefSeq; NP_057531.2; NM_016447.3. DR RefSeq; XP_006715801.1; XM_006715738.3. DR RefSeq; XP_006715802.1; XM_006715739.3. DR RefSeq; XP_006715803.1; XM_006715740.3. DR RefSeq; XP_011513727.1; XM_011515425.2. DR RefSeq; XP_016867804.1; XM_017012315.1. DR RefSeq; XP_016867805.1; XM_017012316.1. DR RefSeq; XP_016867806.1; XM_017012317.1. DR AlphaFoldDB; Q9NZW5; -. DR SMR; Q9NZW5; -. DR BioGRID; 119675; 68. DR CORUM; Q9NZW5; -. DR IntAct; Q9NZW5; 20. DR STRING; 9606.ENSP00000222644; -. DR GlyGen; Q9NZW5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NZW5; -. DR MetOSite; Q9NZW5; -. DR PhosphoSitePlus; Q9NZW5; -. DR SwissPalm; Q9NZW5; -. DR BioMuta; MPP6; -. DR DMDM; 42560556; -. DR EPD; Q9NZW5; -. DR jPOST; Q9NZW5; -. DR MassIVE; Q9NZW5; -. DR MaxQB; Q9NZW5; -. DR PaxDb; Q9NZW5; -. DR PeptideAtlas; Q9NZW5; -. DR ProteomicsDB; 83523; -. DR Antibodypedia; 12204; 250 antibodies from 34 providers. DR DNASU; 51678; -. DR Ensembl; ENST00000222644.10; ENSP00000222644.4; ENSG00000105926.16. DR Ensembl; ENST00000396475.6; ENSP00000379737.2; ENSG00000105926.16. DR GeneID; 51678; -. DR KEGG; hsa:51678; -. DR MANE-Select; ENST00000222644.10; ENSP00000222644.4; NM_001303037.2; NP_001289966.1. DR UCSC; uc003swx.4; human. DR CTD; 51678; -. DR DisGeNET; 51678; -. DR GeneCards; PALS2; -. DR HGNC; HGNC:18167; PALS2. DR HPA; ENSG00000105926; Tissue enhanced (brain, testis). DR MIM; 606959; gene. DR neXtProt; NX_Q9NZW5; -. DR OpenTargets; ENSG00000105926; -. DR VEuPathDB; HostDB:ENSG00000105926; -. DR eggNOG; KOG0609; Eukaryota. DR GeneTree; ENSGT00940000158500; -. DR InParanoid; Q9NZW5; -. DR OMA; NPTTPHK; -. DR OrthoDB; 847888at2759; -. DR PhylomeDB; Q9NZW5; -. DR TreeFam; TF314263; -. DR PathwayCommons; Q9NZW5; -. DR SignaLink; Q9NZW5; -. DR BioGRID-ORCS; 51678; 33 hits in 1079 CRISPR screens. DR ChiTaRS; MPP6; human. DR GeneWiki; MPP6; -. DR GenomeRNAi; 51678; -. DR Pharos; Q9NZW5; Tbio. DR PRO; PR:Q9NZW5; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9NZW5; protein. DR Bgee; ENSG00000105926; Expressed in calcaneal tendon and 116 other tissues. DR ExpressionAtlas; Q9NZW5; baseline and differential. DR Genevisible; Q9NZW5; HS. DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0065003; P:protein-containing complex assembly; NAS:UniProtKB. DR CDD; cd12038; SH3_MPP6; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR014775; L27_C. DR InterPro; IPR004172; L27_dom. DR InterPro; IPR036892; L27_dom_sf. DR InterPro; IPR035603; MPP6_SH3. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF02828; L27; 2. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF07653; SH3_2; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM00569; L27; 2. DR SMART; SM00228; PDZ; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF101288; L27 domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS51022; L27; 2. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50002; SH3; 1. DR AGR; HGNC:18167; -. PE 1: Evidence at protein level; KW Membrane; Phosphoprotein; Reference proteome; Repeat; SH3 domain. FT CHAIN 1..540 FT /note="Protein PALS2" FT /id="PRO_0000094584" FT DOMAIN 1..48 FT /note="L27 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365" FT DOMAIN 49..107 FT /note="L27 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365" FT DOMAIN 130..209 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 215..284 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 338..525 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100" FT MOD_RES 500 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT CONFLICT 41 FT /note="H -> R (in Ref. 1; AAD45919)" FT /evidence="ECO:0000305" SQ SEQUENCE 540 AA; 61117 MW; 86310E4F6AF632BD CRC64; MQQVLENLTE LPSSTGAEEI DLIFLKGIME NPIVKSLAKA HERLEDSKLE AVSDNNLELV NEILEDITPL INVDENVAEL VGILKEPHFQ SLLEAHDIVA SKCYDSPPSS PEMNNSSINN QLLPVDAIRI LGIHKRAGEP LGVTFRVENN DLVIARILHG GMIDRQGLLH VGDIIKEVNG HEVGNNPKEL QELLKNISGS VTLKILPSYR DTITPQQVFV KCHFDYNPYN DNLIPCKEAG LKFSKGEILQ IVNREDPNWW QASHVKEGGS AGLIPSQFLE EKRKAFVRRD WDNSGPFCGT ISSKKKKKMM YLTTRNAEFD RHEIQIYEEV AKMPPFQRKT LVLIGAQGVG RRSLKNRFIV LNPTRFGTTV PFTSRKPRED EKDGQAYKFV SRSEMEADIK AGKYLEHGEY EGNLYGTKID SILEVVQTGR TCILDVNPQA LKVLRTSEFM PYVVFIAAPE LETLRAMHKA VVDAGITTKL LTDSDLKKTV DESARIQRAY NHYFDLIIIN DNLDKAFEKL QTAIEKLRME PQWVPISWVY // ID MPP3_HUMAN Reviewed; 585 AA. AC Q13368; B2R7N0; D3DX47; Q4GX05; Q6PGR3; Q86SV1; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 2. DT 14-DEC-2022, entry version 176. DE RecName: Full=MAGUK p55 subfamily member 3; DE AltName: Full=Discs large homolog 3; DE AltName: Full=Protein MPP3; GN Name=MPP3; Synonyms=DLG3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8824795; DOI=10.1006/geno.1996.0025; RA Smith S.A., Holik P., Stevens J., Mazoyer S., Melis R., Williams B., RA White R., Albertsen H.; RT "Isolation of a gene (DLG3) encoding a second member of the discs-large RT family on chromosome 17q12-q21."; RL Genomics 31:145-150(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Retina; RA Kantardzhieva A., Alexeeva S., Versteeg I., de Jong P.T.V.M., Wijnholds J.; RT "Human retinal membrane palmitoylated protein 3 (mpp3): molecular cloning RT and characterization."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP INTERACTION WITH CADM1. RX PubMed=13679854; DOI=10.1038/sj.onc.1206744; RA Fukuhara H., Masuda M., Yageta M., Fukami T., Kuramochi M., Maruyama T., RA Kitamura T., Murakami Y.; RT "Association of a lung tumor suppressor TSLC1 with MPP3, a human homologue RT of Drosophila tumor suppressor Dlg."; RL Oncogene 22:6160-6165(2003). CC -!- SUBUNIT: May interact with HTR2A (By similarity). Interacts (via PDZ CC domain) with CADM1 (via C-terminus). Interacts with HTR4 (By CC similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q13368; Q9H0C5: BTBD1; NbExp=3; IntAct=EBI-716157, EBI-935503; CC Q13368; O14910: LIN7A; NbExp=5; IntAct=EBI-716157, EBI-2513988; CC Q13368; Q9HAP6: LIN7B; NbExp=8; IntAct=EBI-716157, EBI-821335; CC Q13368; Q9NUP9: LIN7C; NbExp=7; IntAct=EBI-716157, EBI-1171517; CC Q13368; P55347: PKNOX1; NbExp=3; IntAct=EBI-716157, EBI-1373569; CC Q13368; Q8N720: ZNF655; NbExp=3; IntAct=EBI-716157, EBI-625509; CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH47017.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U37707; AAB36964.1; -; mRNA. DR EMBL; AM050144; CAJ18313.1; -; mRNA. DR EMBL; AM050145; CAJ18315.1; -; mRNA. DR EMBL; AK313045; BAG35877.1; -; mRNA. DR EMBL; CH471178; EAW51664.1; -; Genomic_DNA. DR EMBL; CH471178; EAW51665.1; -; Genomic_DNA. DR EMBL; BC047017; AAH47017.1; ALT_INIT; mRNA. DR EMBL; BC056865; AAH56865.1; -; mRNA. DR CCDS; CCDS42344.1; -. DR PIR; G02165; G02165. DR RefSeq; NP_001317162.1; NM_001330233.1. DR RefSeq; NP_001923.2; NM_001932.4. DR RefSeq; XP_006721978.1; XM_006721915.2. DR AlphaFoldDB; Q13368; -. DR SMR; Q13368; -. DR BioGRID; 110496; 34. DR CORUM; Q13368; -. DR IntAct; Q13368; 34. DR STRING; 9606.ENSP00000381425; -. DR iPTMnet; Q13368; -. DR PhosphoSitePlus; Q13368; -. DR BioMuta; MPP3; -. DR DMDM; 150421601; -. DR jPOST; Q13368; -. DR MassIVE; Q13368; -. DR MaxQB; Q13368; -. DR PaxDb; Q13368; -. DR PeptideAtlas; Q13368; -. DR ProteomicsDB; 59353; -. DR Antibodypedia; 8160; 324 antibodies from 28 providers. DR DNASU; 4356; -. DR Ensembl; ENST00000398389.9; ENSP00000381425.4; ENSG00000161647.19. DR GeneID; 4356; -. DR KEGG; hsa:4356; -. DR MANE-Select; ENST00000398389.9; ENSP00000381425.4; NM_001932.6; NP_001923.2. DR UCSC; uc002iei.5; human. DR CTD; 4356; -. DR DisGeNET; 4356; -. DR GeneCards; MPP3; -. DR HGNC; HGNC:7221; MPP3. DR HPA; ENSG00000161647; Tissue enhanced (brain, heart muscle). DR MIM; 601114; gene. DR neXtProt; NX_Q13368; -. DR OpenTargets; ENSG00000161647; -. DR PharmGKB; PA30926; -. DR VEuPathDB; HostDB:ENSG00000161647; -. DR eggNOG; KOG0609; Eukaryota. DR GeneTree; ENSGT00940000157190; -. DR HOGENOM; CLU_001715_5_0_1; -. DR InParanoid; Q13368; -. DR OMA; EGYFKGH; -. DR OrthoDB; 531106at2759; -. DR PhylomeDB; Q13368; -. DR TreeFam; TF314263; -. DR PathwayCommons; Q13368; -. DR SignaLink; Q13368; -. DR BioGRID-ORCS; 4356; 23 hits in 1071 CRISPR screens. DR GenomeRNAi; 4356; -. DR Pharos; Q13368; Tbio. DR PRO; PR:Q13368; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q13368; protein. DR Bgee; ENSG00000161647; Expressed in apex of heart and 127 other tissues. DR ExpressionAtlas; Q13368; baseline and differential. DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl. DR CDD; cd12039; SH3_MPP3; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR014775; L27_C. DR InterPro; IPR004172; L27_dom. DR InterPro; IPR036892; L27_dom_sf. DR InterPro; IPR035604; MPP3_SH3. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF02828; L27; 2. DR Pfam; PF00595; PDZ; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM00569; L27; 2. DR SMART; SM00228; PDZ; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF101288; L27 domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS51022; L27; 2. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50002; SH3; 1. DR AGR; HGNC:7221; -. PE 1: Evidence at protein level; KW Phosphoprotein; Reference proteome; Repeat; SH3 domain. FT CHAIN 1..585 FT /note="MAGUK p55 subfamily member 3" FT /id="PRO_0000094575" FT DOMAIN 6..60 FT /note="L27 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365" FT DOMAIN 61..118 FT /note="L27 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365" FT DOMAIN 137..212 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 226..296 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 385..570 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100" FT MOD_RES 307 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O88954" FT VARIANT 585 FT /note="R -> G (in dbSNP:rs17742683)" FT /id="VAR_050014" FT CONFLICT 37 FT /note="V -> D (in Ref. 1; AAB36964)" FT /evidence="ECO:0000305" SQ SEQUENCE 585 AA; 66152 MW; 782DAE54096A4993 CRC64; MPVLSEDSGL HETLALLTSQ LRPDSNHKEE MGFLRDVFSE KSLSYLMKIH EKLRYYERQS PTPVLHSAVA LAEDVMEELQ AASVHSDERE LLQLLSTPHL RAVLMVHDTV AQKNFDPVLP PLPDNIDEDF DEESVKIVRL VKNKEPLGAT IRRDEHSGAV VVARIMRGGA ADRSGLVHVG DELREVNGIA VLHKRPDEIS QILAQSQGSI TLKIIPATQE EDRLKESKVF MRALFHYNPR EDRAIPCQEA GLPFQRRQVL EVVSQDDPTW WQAKRVGDTN LRAGLIPSKG FQERRLSYRR AAGTLPSPQS LRKPPYDQPC DKETCDCEGY LKGHYVAGLR RSFRLGCRER LGGSQEGKMS SGAESPELLT YEEVARYQHQ PGERPRLVVL IGSLGARLHE LKQKVVAENP QHFGVAVPHT TRPRKSHEKE GVEYHFVSKQ AFEADLHHNK FLEHGEYKEN LYGTSLEAIQ AVMAKNKVCL VDVEPEALKQ LRTSEFKPYI IFVKPAIQEK RKTPPMSPAC EDTAAPFDEQ QQEMAASAAF IDRHYGHLVD AVLVKEDLQG AYSQLKVVLE KLSKDTHWVP VSWVR // ID VGPCR_HHV8P Reviewed; 342 AA. AC Q98146; O12573; P88966; Q77Q35; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 14-DEC-2022, entry version 110. DE RecName: Full=viral G-protein coupled receptor; DE Short=vGPCR; DE AltName: Full=Protein ORF74; GN Name=ORF74; OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's OS sarcoma-associated herpesvirus). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus. OX NCBI_TaxID=868565; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8892957; DOI=10.1128/jvi.70.11.8218-8223.1996; RA Cesarman E., Nador R.G., Bai F., Bohenzky R.A., Russo J.J., Moore P.S., RA Chang Y., Knowles D.M.; RT "Kaposi's sarcoma-associated herpesvirus contains G protein-coupled RT receptor and cyclin D homologs which are expressed in Kaposi's sarcoma and RT malignant lymphoma."; RL J. Virol. 70:8218-8223(1996). RN [2] RP SEQUENCE REVISION. RA Cesarman E., Nador R.G., Bai F., Chang J., Moore P.S., Knowles D.M.; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Guo H.G., Browning P., Nicholas J., Hayward G.H., Tschachler E., RA Jiang Y.W., Sadowska M., Raffeld M., Colombini S., Gallo R.C., Reitz M.S.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=8962146; DOI=10.1073/pnas.93.25.14862; RA Russo J.J., Bohenzky R.A., Chien M.-C., Chen J., Yan M., Maddalena D., RA Parry J.P., Peruzzi D., Edelman I.S., Chang Y., Moore P.S.; RT "Nucleotide sequence of the Kaposi sarcoma-associated herpesvirus (HHV8)."; RL Proc. Natl. Acad. Sci. U.S.A. 93:14862-14867(1996). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=9151804; DOI=10.1128/jvi.71.6.4187-4192.1997; RA Neipel F., Albrecht J.-C., Fleckenstein B.; RT "Cell-homologous genes in the Kaposi's sarcoma-associated rhadinovirus RT human herpesvirus 8: determinants of its pathogenicity?"; RL J. Virol. 71:4187-4192(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16760382; DOI=10.1099/vir.0.81919-0; RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.; RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview."; RL J. Gen. Virol. 87:1781-1804(2006). RN [7] RP FUNCTION. RX PubMed=12477810; DOI=10.1128/jvi.77.1.57-67.2003; RA Cannon M., Philpott N.J., Cesarman E.; RT "The Kaposi's sarcoma-associated herpesvirus G protein-coupled receptor has RT broad signaling effects in primary effusion lymphoma cells."; RL J. Virol. 77:57-67(2003). RN [8] RP FUNCTION. RX PubMed=14724579; DOI=10.1038/sj.onc.1207021; RA Cannon M.L., Cesarman E.; RT "The KSHV G protein-coupled receptor signals via multiple pathways to RT induce transcription factor activation in primary effusion lymphoma RT cells."; RL Oncogene 23:514-523(2004). RN [9] RP INTERACTION WITH PROTEIN K7. RX PubMed=18802460; DOI=10.1371/journal.ppat.1000157; RA Feng H., Dong X., Negaard A., Feng P.; RT "Kaposi's sarcoma-associated herpesvirus K7 induces viral G protein-coupled RT receptor degradation and reduces its tumorigenicity."; RL PLoS Pathog. 4:E1000157-E1000157(2008). RN [10] RP FUNCTION, AND INTERACTION WITH HOST CADM1. RX PubMed=29698475; DOI=10.1371/journal.ppat.1006968; RA Hunte R., Alonso P., Thomas R., Bazile C.A., Ramos J.C., van der Weyden L., RA Dominguez-Bendala J., Khan W.N., Shembade N.; RT "CADM1 is essential for KSHV-encoded vGPCR-and vFLIP-mediated chronic NF- RT kappaB activation."; RL PLoS Pathog. 14:E1006968-E1006968(2018). CC -!- FUNCTION: Receptor that signals constitutively via several signaling CC pathways including PI3K/AKT as well as mitogen- and stress- CC activated/MAP kinases. Promotes host cell proliferation and survival, CC modulates cell migration, stimulates angiogenesis, and recruits CC inflammatory cells, both in expressing cells and in neighboring cells. CC Maintains chronic activation of NF-kappa-B via interaction with host CC CADM1 (PubMed:29698475). {ECO:0000269|PubMed:12477810, CC ECO:0000269|PubMed:14724579, ECO:0000269|PubMed:29698475}. CC -!- SUBUNIT: Interacts with protein K7; this interaction promotes vGPCR CC proteasomal degradation (PubMed:18802460). Interacts with host CADM1; CC this interaction is essential for chronic NF-kappa-B activation CC (PubMed:29698475). {ECO:0000269|PubMed:18802460, CC ECO:0000269|PubMed:29698475}. CC -!- INTERACTION: CC Q98146; F5HDA4: K7; NbExp=5; IntAct=EBI-7930093, EBI-9002986; CC -!- SUBCELLULAR LOCATION: Host cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U82242; AAB51506.1; -; Genomic_DNA. DR EMBL; U75698; AAC57160.1; -; Genomic_DNA. DR EMBL; U40394; AAD04749.1; -; Genomic_DNA. DR EMBL; U93872; AAB62618.1; -; Genomic_DNA. DR EMBL; AF148805; AAD46503.1; -; Genomic_DNA. DR RefSeq; YP_001129433.1; NC_009333.1. DR SMR; Q98146; -. DR BioGRID; 1776968; 21. DR IntAct; Q98146; 3. DR MINT; Q98146; -. DR GeneID; 4961460; -. DR GeneID; 4961465; -. DR KEGG; vg:4961460; -. DR Proteomes; UP000000942; Genome. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW G-protein coupled receptor; Glycoprotein; Host cell membrane; KW Host membrane; Membrane; Receptor; Reference proteome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..342 FT /note="viral G-protein coupled receptor" FT /id="PRO_0000070252" FT TOPO_DOM 1..51 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 52..72 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 73..92 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 93..113 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 114..121 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 122..142 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 143..159 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 160..180 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 181..217 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 218..238 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 239..251 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 252..272 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 273..293 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 294..314 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 315..342 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 18 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 22 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CARBOHYD 31 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255" FT CONFLICT 44 FT /note="V -> G (in Ref. 2; AAD04749)" FT /evidence="ECO:0000305" FT CONFLICT 167 FT /note="A -> P (in Ref. 2; AAD04749)" FT /evidence="ECO:0000305" FT CONFLICT 170 FT /note="L -> S (in Ref. 3; AAB51506)" FT /evidence="ECO:0000305" FT CONFLICT 322 FT /note="R -> K (in Ref. 3; AAB51506)" FT /evidence="ECO:0000305" SQ SEQUENCE 342 AA; 38669 MW; 41E4B33CA2D9F069 CRC64; MAAEDFLTIF LDDDESWNET LNMSGYDYSG NFSLEVSVCE MTTVVPYTWN VGILSLIFLI NVLGNGLVTY IFCKHRSRAG AIDILLLGIC LNSLCLSISL LAEVLMFLFP NIISTGLCRL EIFFYYLYVY LDIFSVVCVS LVRYLLVAYS TRSWPKKQSL GWVLTSAALL IALVLSGDAC RHRSRVVDPV SKQAMCYENA GNMTADWRLH VRTVSVTAGF LLPLALLILF YALTWCVVRR TKLQARRKVR GVIVAVVLLF FVFCFPYHVL NLLDTLLRRR WIRDSCYTRG LINVGLAVTS LLQALYSAVV PLIYSCLGSL FRQRMYGLFQ SLRQSFMSGA TT // ID VFLIP_HHV8P Reviewed; 188 AA. AC F5HEZ4; DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 14-DEC-2022, entry version 49. DE RecName: Full=Viral FLICE protein; DE Short=vFLIP; GN Name=ORF71; OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's OS sarcoma-associated herpesvirus). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus. OX NCBI_TaxID=868565; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999; RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.; RT "Identification of a spliced gene from Kaposi's sarcoma-associated RT herpesvirus encoding a protein with similarities to latent membrane RT proteins 1 and 2A of Epstein-Barr virus."; RL J. Virol. 73:6953-6963(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16760382; DOI=10.1099/vir.0.81919-0; RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.; RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview."; RL J. Gen. Virol. 87:1781-1804(2006). RN [3] RP FUNCTION, AND INTERACTION WITH HOST TRAF2; MAP3K14; IKBKB AND RIPK1. RX PubMed=10523854; DOI=10.1038/sj.onc.1202976; RA Chaudhary P.M., Jasmin A., Eby M.T., Hood L.; RT "Modulation of the NF-kappa B pathway by virally encoded death effector RT domains-containing proteins."; RL Oncogene 18:5738-5746(1999). RN [4] RP FUNCTION, AND INTERACTION WITH HOST TRAF2 AND IKBKG. RX PubMed=16311516; DOI=10.1038/sj.embor.7400580; RA Guasparri I., Wu H., Cesarman E.; RT "The KSHV oncoprotein vFLIP contains a TRAF-interacting motif and requires RT TRAF2 and TRAF3 for signalling."; RL EMBO Rep. 7:114-119(2006). RN [5] RP FUNCTION, AND INTERACTION WITH HOST CADM1. RX PubMed=29698475; DOI=10.1371/journal.ppat.1006968; RA Hunte R., Alonso P., Thomas R., Bazile C.A., Ramos J.C., van der Weyden L., RA Dominguez-Bendala J., Khan W.N., Shembade N.; RT "CADM1 is essential for KSHV-encoded vGPCR-and vFLIP-mediated chronic NF- RT kappaB activation."; RL PLoS Pathog. 14:E1006968-E1006968(2018). CC -!- FUNCTION: Plays a role in the modulation of host signaling pathways by CC acting as an activator of both the classic and the alternative NF- CC kappa-B pathways. Thereby, initiates an important range of cellular CC processes to promote cell survival, proliferation and protection from CC apoptosis. {ECO:0000269|PubMed:10523854, ECO:0000269|PubMed:16311516, CC ECO:0000269|PubMed:29698475}. CC -!- SUBUNIT: Interacts with host RIPK1, TRAF2, MAP3K14, IKBKB, and IKBKG. CC Interacts with host CADM1; this interaction is essential for chronic CC NF-kappa-B activation. {ECO:0000269|PubMed:10523854, CC ECO:0000269|PubMed:16311516, ECO:0000269|PubMed:29698475}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF148805; AAD46498.1; -; Genomic_DNA. DR RefSeq; YP_001129429.1; NC_009333.1. DR PDB; 5LDE; X-ray; 3.38 A; A/B=1-188. DR PDBsum; 5LDE; -. DR SMR; F5HEZ4; -. DR BioGRID; 1776997; 11. DR GeneID; 4961494; -. DR KEGG; vg:4961494; -. DR Proteomes; UP000000942; Genome. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0039652; P:induction by virus of host NF-kappaB cascade; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR GO; GO:0019050; P:suppression by virus of host apoptotic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.533.10; -; 2. DR InterPro; IPR011029; DEATH-like_dom_sf. DR InterPro; IPR001875; DED_dom. DR InterPro; IPR002398; Pept_C14. DR PANTHER; PTHR10454; CASPASE; 1. DR Pfam; PF01335; DED; 1. DR SMART; SM00031; DED; 2. DR SUPFAM; SSF47986; DEATH domain; 1. DR PROSITE; PS50168; DED; 2. PE 1: Evidence at protein level; KW 3D-structure; Activation of host NF-kappa-B by virus; Apoptosis; KW Host-virus interaction; KW Inhibition of host apoptosis by viral FLIP-like protein; KW Modulation of host cell apoptosis by virus; Reference proteome; Repeat. FT CHAIN 1..188 FT /note="Viral FLICE protein" FT /id="PRO_0000423909" FT DOMAIN 2..74 FT /note="DED 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00065" FT DOMAIN 93..169 FT /note="DED 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00065" FT HELIX 4..12 FT /evidence="ECO:0007829|PDB:5LDE" FT HELIX 16..25 FT /evidence="ECO:0007829|PDB:5LDE" FT HELIX 35..47 FT /evidence="ECO:0007829|PDB:5LDE" FT HELIX 53..63 FT /evidence="ECO:0007829|PDB:5LDE" FT HELIX 66..71 FT /evidence="ECO:0007829|PDB:5LDE" FT HELIX 77..83 FT /evidence="ECO:0007829|PDB:5LDE" FT TURN 84..86 FT /evidence="ECO:0007829|PDB:5LDE" FT HELIX 93..104 FT /evidence="ECO:0007829|PDB:5LDE" FT HELIX 107..117 FT /evidence="ECO:0007829|PDB:5LDE" FT HELIX 118..120 FT /evidence="ECO:0007829|PDB:5LDE" FT HELIX 130..139 FT /evidence="ECO:0007829|PDB:5LDE" FT HELIX 149..156 FT /evidence="ECO:0007829|PDB:5LDE" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:5LDE" FT HELIX 161..170 FT /evidence="ECO:0007829|PDB:5LDE" SQ SEQUENCE 188 AA; 21474 MW; 37CFE147EAE45371 CRC64; MATYEVLCEV ARKLGTDDRE VVLFLLNVFI PQPTLAQLIG ALRALKEEGR LTFPLLAECL FRAGRRDLLR DLLHLDPRFL ERHLAGTMSY FSPYQLTVLH VDGELCARDI RSLIFLSKDT IGSRSTPQTF LHWVYCMENL DLLGPTDVDA LMSMLRSLSR VDLQRQVQTL MGLHLSGPSH SQHYRHTP // ID F5H372_HUMAN Unreviewed; 67 AA. AC F5H372; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-DEC-2022, entry version 50. DE SubName: Full=Cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSP00000445375.1}; GN Name=CADM1 {ECO:0000313|Ensembl:ENSP00000445375.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000445375.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000445375.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000445375.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP000462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003179; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005020; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877463; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF511123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; F5H372; -. DR Ensembl; ENST00000540951.1; ENSP00000445375.1; ENSG00000182985.18. DR UCSC; uc058hpj.1; human. DR HGNC; HGNC:5951; CADM1. DR VEuPathDB; HostDB:ENSG00000182985; -. DR GeneTree; ENSGT00940000156093; -. DR HOGENOM; CLU_2811643_0_0_1; -. DR ChiTaRS; CADM1; human. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000182985; Expressed in paraflocculus and 216 other tissues. DR ExpressionAtlas; F5H372; baseline and differential. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..44 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 45..67 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003327228" SQ SEQUENCE 67 AA; 6582 MW; 0455D71C4F4D1D01 CRC64; MASVVLPSGS QCAAAAAAAA PPGLRLRLLL LLFSAAALIP TGLTSSPRLE CGGTISAHCS LGLPVLR // ID H1ZZW3_HUMAN Unreviewed; 43 AA. AC H1ZZW3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 14-DEC-2022, entry version 18. DE SubName: Full=Truncated CADM1 protein {ECO:0000313|EMBL:CCD32614.2}; GN Name=CADM1 {ECO:0000313|EMBL:CCD32614.2}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:CCD32614.2}; RN [1] {ECO:0000313|EMBL:CCD32614.2} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Mast cell line HMC-1 {ECO:0000313|EMBL:CCD32614.2}; RA Moiseeva E.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCD32614.2} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Mast cell line HMC-1 {ECO:0000313|EMBL:CCD32614.2}; RA Moiseeva E.P., Leyland M.L., Bradding P.; RT "CADM1 isoforms differentially regulate human mast cell survival and RT homotypic adhesion."; RL Cell. Mol. Life Sci. 69:2751-2764(2012). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HE586500; CCD32614.2; -; mRNA. DR AlphaFoldDB; H1ZZW3; -. DR ChiTaRS; CADM1; human. PE 2: Evidence at transcript level; SQ SEQUENCE 43 AA; 4160 MW; 0F03CC481105CF0A CRC64; MASVVLPSGS QCAAAAAAAA PPGLRLRLLL LLFSAAALIP TGK // ID F5H0H5_HUMAN Unreviewed; 79 AA. AC F5H0H5; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-DEC-2022, entry version 68. DE SubName: Full=Cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSP00000439847.1}; DE Flags: Fragment; GN Name=CADM1 {ECO:0000313|Ensembl:ENSP00000439847.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000439847.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000439847.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000439847.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP000462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003179; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005020; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877463; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF511123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; F5H0H5; -. DR SMR; F5H0H5; -. DR PeptideAtlas; F5H0H5; -. DR ProteomicsDB; 25342; -. DR Antibodypedia; 32257; 660 antibodies from 39 providers. DR Ensembl; ENST00000543540.5; ENSP00000439847.1; ENSG00000182985.18. DR UCSC; uc058hpg.1; human. DR HGNC; HGNC:5951; CADM1. DR VEuPathDB; HostDB:ENSG00000182985; -. DR GeneTree; ENSGT00940000156093; -. DR OMA; TYDRMYT; -. DR ChiTaRS; CADM1; human. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000182985; Expressed in paraflocculus and 216 other tissues. DR ExpressionAtlas; F5H0H5; baseline and differential. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR Pfam; PF08205; C2-set_2; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|PeptideAtlas:F5H0H5, KW ECO:0007829|ProteomicsDB:F5H0H5}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT DOMAIN 1..79 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT NON_TER 79 FT /evidence="ECO:0000313|Ensembl:ENSP00000439847.1" SQ SEQUENCE 79 AA; 8868 MW; BC591DE09FBC1B20 CRC64; MIDIQKDTAV EGEEIEVNCT AMASKPATTI RWFKGNTELK GKSEVEEWSD MYTVTSQLML KVHKEDDGVP VICQVEHPA // ID F5H8J9_HUMAN Unreviewed; 110 AA. AC F5H8J9; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 8. DT 14-DEC-2022, entry version 75. DE SubName: Full=Cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSP00000442001.1}; DE Flags: Fragment; GN Name=CADM1 {ECO:0000313|Ensembl:ENSP00000442001.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000442001.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000442001.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000442001.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP000462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003179; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005020; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877463; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF511123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; F5H8J9; -. DR SMR; F5H8J9; -. DR PeptideAtlas; F5H8J9; -. DR ProteomicsDB; 27806; -. DR Antibodypedia; 32257; 660 antibodies from 39 providers. DR Ensembl; ENST00000542450.5; ENSP00000442001.1; ENSG00000182985.18. DR UCSC; uc058hpf.1; human. DR HGNC; HGNC:5951; CADM1. DR VEuPathDB; HostDB:ENSG00000182985; -. DR GeneTree; ENSGT00940000156093; -. DR HOGENOM; CLU_173690_0_0_1; -. DR OMA; TYDRMYT; -. DR ChiTaRS; CADM1; human. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000182985; Expressed in paraflocculus and 216 other tissues. DR ExpressionAtlas; F5H8J9; baseline and differential. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR Pfam; PF08205; C2-set_2; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|MaxQB:F5H8J9, KW ECO:0007829|PeptideAtlas:F5H8J9}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT DOMAIN 1..91 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT NON_TER 110 FT /evidence="ECO:0000313|Ensembl:ENSP00000442001.1" SQ SEQUENCE 110 AA; 12498 MW; DBCEB73A4D76E654 CRC64; MIDIQKDTAV EGEEIEVNCT AMASKPATTI RWFKGNTELK GKSEVEEWSD MYTVTSQLML KVHKEDDGVP VICQVEHPAV TGNLQTQRYL EVQYKPQVHI QMTYPLQGLT // ID F5H125_HUMAN Unreviewed; 182 AA. AC F5H125; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 14-DEC-2022, entry version 65. DE SubName: Full=Cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSP00000439696.1}; DE Flags: Fragment; GN Name=CADM1 {ECO:0000313|Ensembl:ENSP00000439696.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000439696.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000439696.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000439696.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP000462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003179; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005020; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877463; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF511123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; F5H125; -. DR SMR; F5H125; -. DR MaxQB; F5H125; -. DR PeptideAtlas; F5H125; -. DR ProteomicsDB; 25520; -. DR Antibodypedia; 32257; 660 antibodies from 39 providers. DR Ensembl; ENST00000545094.5; ENSP00000439696.1; ENSG00000182985.18. DR UCSC; uc058hph.1; human. DR HGNC; HGNC:5951; CADM1. DR VEuPathDB; HostDB:ENSG00000182985; -. DR GeneTree; ENSGT00940000156093; -. DR HOGENOM; CLU_047574_1_1_1; -. DR ChiTaRS; CADM1; human. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000182985; Expressed in paraflocculus and 216 other tissues. DR ExpressionAtlas; F5H125; baseline and differential. DR Gene3D; 2.60.40.10; -; 2. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR Pfam; PF08205; C2-set_2; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 2. PE 1: Evidence at protein level; KW Membrane {ECO:0000256|ARBA:ARBA00022989}; KW Proteomics identification {ECO:0007829|EPD:F5H125, KW ECO:0007829|MaxQB:F5H125}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. FT DOMAIN 1..106 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 111..182 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT NON_TER 182 FT /evidence="ECO:0000313|Ensembl:ENSP00000439696.1" SQ SEQUENCE 182 AA; 20514 MW; 6D88866443D2B434 CRC64; MKASGHTSGD GQNLFTKDVT VIEGEVATIS CQVNKSDDSV IQLLNPNRQT IYFRDFRPLK DSRFQLLNFS SSELKVSLTN VSISDEGRYF CQLYTDPPQE SYTTITVLVP PRNLMIDIQK DTAVEGEEIE VNCTAMASKP ATTIRWFKGN TELKGKSEVE EWSDMYTVTS QLMLKVHKED DG // ID A0A087X0T8_HUMAN Unreviewed; 346 AA. AC A0A087X0T8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 14-DEC-2022, entry version 48. DE SubName: Full=Cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSP00000483648.1}; GN Name=CADM1 {ECO:0000313|Ensembl:ENSP00000483648.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000483648.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000483648.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000483648.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP000462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003179; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005020; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877463; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF511123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; A0A087X0T8; -. DR SMR; A0A087X0T8; -. DR PeptideAtlas; A0A087X0T8; -. DR Antibodypedia; 32257; 660 antibodies from 39 providers. DR Ensembl; ENST00000612235.4; ENSP00000483648.1; ENSG00000182985.18. DR UCSC; uc058hot.1; human. DR HGNC; HGNC:5951; CADM1. DR VEuPathDB; HostDB:ENSG00000182985; -. DR GeneTree; ENSGT00940000156093; -. DR ChiTaRS; CADM1; human. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000182985; Expressed in paraflocculus and 216 other tissues. DR ExpressionAtlas; A0A087X0T8; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 3. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR Pfam; PF08205; C2-set_2; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 3. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR PROSITE; PS50835; IG_LIKE; 3. PE 1: Evidence at protein level; KW Membrane {ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0007829|EPD:A0A087X0T8, KW ECO:0007829|MaxQB:A0A087X0T8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 306..331 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..98 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 103..197 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 202..276 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" SQ SEQUENCE 346 AA; 38780 MW; 5F8AC7DC7F4CDFB6 CRC64; GDGQNLFTKD VTVIEGEVAT ISCQVNKSDD SVIQLLNPNR QTIYFRDFRP LKDSRFQLLN FSSSELKVSL TNVSISDEGR YFCQLYTDPP QESYTTITVL VPPRNLMIDI QKDTAVEGEE IEVNCTAMAS KPATTIRWFK GNTELKGKSE VEEWSDMYTV TSQLMLKVHK EDDGVPVICQ VEHPAVTGNL QTQRYLEVQY KPQVHIQMTY PLQGLTREGD ALELTCEAIG KPQPVMVTWV RVDDEMPQHA VLSGPNLFIN NLNKTDNGTY RCEASNIVGK AHSDYMLYVY DSRAGEEGSI RAVDHAVIGG VVAVVVFAML CLLIILGRYF ARHKGLFSLT SSPRIK // ID H0YG94_HUMAN Unreviewed; 188 AA. AC H0YG94; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 8. DT 14-DEC-2022, entry version 67. DE SubName: Full=Cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSP00000442227.1}; DE Flags: Fragment; GN Name=CADM1 {ECO:0000313|Ensembl:ENSP00000442227.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000442227.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000442227.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000442227.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP000462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003179; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005020; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877463; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF511123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; H0YG94; -. DR ProteomicsDB; 38319; -. DR Antibodypedia; 32257; 660 antibodies from 39 providers. DR Ensembl; ENST00000543249.1; ENSP00000442227.1; ENSG00000182985.18. DR UCSC; uc058hpi.1; human. DR HGNC; HGNC:5951; CADM1. DR VEuPathDB; HostDB:ENSG00000182985; -. DR GeneTree; ENSGT00940000156093; -. DR ChiTaRS; CADM1; human. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000182985; Expressed in paraflocculus and 216 other tissues. DR ExpressionAtlas; H0YG94; baseline and differential. DR Gene3D; 2.60.40.10; -; 2. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR Pfam; PF08205; C2-set_2; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 2. PE 1: Evidence at protein level; KW Membrane {ECO:0000256|ARBA:ARBA00022989}; KW Proteomics identification {ECO:0007829|EPD:H0YG94, KW ECO:0007829|MaxQB:H0YG94}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. FT DOMAIN 22..123 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 128..188 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT REGION 1..28 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 11..28 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000442227.1" FT NON_TER 188 FT /evidence="ECO:0000313|Ensembl:ENSP00000442227.1" SQ SEQUENCE 188 AA; 21134 MW; 1E81311DA02546CE CRC64; XSGDLPSYSP LPHSPRSQRS IPSVQGDGQN LFTKDVTVIE GEVATISCQV NKSDDSVIQL LNPNRQTIYF RDFRPLKDSR FQLLNFSSSE LKVSLTNVSI SDEGRYFCQL YTDPPQESYT TITVLVPPRN LMIDIQKDTA VEGEEIEVNC TAMASKPATT IRWFKGNTEL KGKSEVEEWS DMYTVTSQ // ID A0A0A0MTJ8_HUMAN Unreviewed; 413 AA. AC A0A0A0MTJ8; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 14-DEC-2022, entry version 46. DE SubName: Full=Cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSP00000442387.1}; DE Flags: Fragment; GN Name=CADM1 {ECO:0000313|Ensembl:ENSP00000442387.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000442387.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000442387.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000442387.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- SIMILARITY: Belongs to the nectin family. CC {ECO:0000256|ARBA:ARBA00007810}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP000462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003179; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005020; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877463; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF511123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Antibodypedia; 32257; 660 antibodies from 39 providers. DR Ensembl; ENST00000545380.5; ENSP00000442387.1; ENSG00000182985.18. DR UCSC; uc058how.1; human. DR HGNC; HGNC:5951; CADM1. DR VEuPathDB; HostDB:ENSG00000182985; -. DR GeneTree; ENSGT00940000156093; -. DR ChiTaRS; CADM1; human. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000182985; Expressed in paraflocculus and 216 other tissues. DR ExpressionAtlas; A0A0A0MTJ8; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 3. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR003585; Neurexin-like. DR Pfam; PF08205; C2-set_2; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00294; 4.1m; 1. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 3. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR PROSITE; PS50835; IG_LIKE; 3. PE 1: Evidence at protein level; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0007829|EPD:A0A0A0MTJ8, KW ECO:0007829|MaxQB:A0A0A0MTJ8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1..43 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 44..413 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5001974512" FT TRANSMEM 346..366 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 39..138 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 143..237 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 242..316 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000442387.1" SQ SEQUENCE 413 AA; 45533 MW; A809F2698DAE3C8B CRC64; XSVVLPSGSQ CAAAAAAAAP PGLRLRLLLL LFSAAALIPT GDGQNLFTKD VTVIEGEVAT ISCQVNKSDD SVIQLLNPNR QTIYFRDFRP LKDSRFQLLN FSSSELKVSL TNVSISDEGR YFCQLYTDPP QESYTTITVL VPPRNLMIDI QKDTAVEGEE IEVNCTAMAS KPATTIRWFK GNTELKGKSE VEEWSDMYTV TSQLMLKVHK EDDGVPVICQ VEHPAVTGNL QTQRYLEVQY KPQVHIQMTY PLQGLTREGD ALELTCEAIG KPQPVMVTWV RVDDEMPQHA VLSGPNLFIN NLNKTDNGTY RCEASNIVGK AHSDYMLYVY DSRAGEEGSI RAVDHAVIGG VVAVVVFAML CLLIILGRYF ARHKGTYFTH EAKGADDAAD ADTAIINAEG GQNNSEEKKE YFI // ID X5DQS5_HUMAN Unreviewed; 443 AA. AC X5DQS5; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 14-DEC-2022, entry version 60. DE SubName: Full=Cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSP00000440322.1}; DE SubName: Full=Cell adhesion molecule 1 isoform C {ECO:0000313|EMBL:AHW56437.1}; DE Flags: Fragment; GN Name=CADM1 {ECO:0000313|EMBL:AHW56437.1, GN ECO:0000313|Ensembl:ENSP00000440322.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AHW56437.1}; RN [1] {ECO:0000313|Ensembl:ENSP00000440322.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|EMBL:AHW56437.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Fetal whole brain {ECO:0000313|EMBL:AHW56437.1}; RX PubMed=24722188; RA Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., RA Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., RA Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A., RA Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., RA Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.; RT "Protein interaction network of alternatively spliced isoforms from brain RT links genetic risk factors for autism."; RL Nat. Commun. 5:3650-3650(2014). RN [4] {ECO:0000313|Ensembl:ENSP00000440322.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- SIMILARITY: Belongs to the nectin family. CC {ECO:0000256|ARBA:ARBA00007810}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP000462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003179; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005020; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877463; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF511123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KJ534797; AHW56437.1; -; mRNA. DR RefSeq; NP_001287974.1; NM_001301045.1. DR SMR; X5DQS5; -. DR Antibodypedia; 32257; 660 antibodies from 39 providers. DR DNASU; 23705; -. DR Ensembl; ENST00000536727.5; ENSP00000440322.1; ENSG00000182985.18. DR GeneID; 23705; -. DR UCSC; uc001ppj.5; human. DR CTD; 23705; -. DR HGNC; HGNC:5951; CADM1. DR VEuPathDB; HostDB:ENSG00000182985; -. DR GeneTree; ENSGT00940000156093; -. DR OrthoDB; 716894at2759; -. DR BioGRID-ORCS; 23705; 8 hits in 1071 CRISPR screens. DR ChiTaRS; CADM1; human. DR GenomeRNAi; 23705; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000182985; Expressed in paraflocculus and 216 other tissues. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 3. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR003585; Neurexin-like. DR Pfam; PF08205; C2-set_2; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00294; 4.1m; 1. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 3. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR PROSITE; PS50835; IG_LIKE; 3. PE 1: Evidence at protein level; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0007829|EPD:X5DQS5, KW ECO:0007829|MaxQB:X5DQS5}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1..44 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 45..443 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014110275" FT TRANSMEM 376..396 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 40..139 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 144..238 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 243..317 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT NON_TER 443 FT /evidence="ECO:0000313|EMBL:AHW56437.1" SQ SEQUENCE 443 AA; 48648 MW; 046B43AA156F6F64 CRC64; MASVVLPSGS QCAAAAAAAA PPGLRLRLLL LLFSAAALIP TGDGQNLFTK DVTVIEGEVA TISCQVNKSD DSVIQLLNPN RQTIYFRDFR PLKDSRFQLL NFSSSELKVS LTNVSISDEG RYFCQLYTDP PQESYTTITV LVPPRNLMID IQKDTAVEGE EIEVNCTAMA SKPATTIRWF KGNTELKGKS EVEEWSDMYT VTSQLMLKVH KEDDGVPVIC QVEHPAVTGN LQTQRYLEVQ YKPQVHIQMT YPLQGLTREG DALELTCEAI GKPQPVMVTW VRVDDEMPQH AVLSGPNLFI NNLNKTDNGT YRCEASNIVG KAHSDYMLYV YDTTATTEPA VHGLTQLPNS AEELDSEDLS DSRAGEEGSI RAVDHAVIGG VVAVVVFAML CLLIILGRYF ARHKGTYFTH EAKGADDAAD ADTAIINAEG GQNNSEEKKE YFI // ID A0A087X1W8_HUMAN Unreviewed; 412 AA. AC A0A087X1W8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 14-DEC-2022, entry version 46. DE SubName: Full=Cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSP00000484516.1}; GN Name=CADM1 {ECO:0000313|Ensembl:ENSP00000484516.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000484516.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000484516.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [2] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000484516.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- SIMILARITY: Belongs to the nectin family. CC {ECO:0000256|ARBA:ARBA00007810}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP000462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000465; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP003179; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP005020; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877463; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF455527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF511123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; A0A087X1W8; -. DR SMR; A0A087X1W8; -. DR IntAct; A0A087X1W8; 1. DR Antibodypedia; 32257; 660 antibodies from 39 providers. DR Ensembl; ENST00000616271.4; ENSP00000484516.1; ENSG00000182985.18. DR UCSC; uc058hpa.1; human. DR HGNC; HGNC:5951; CADM1. DR VEuPathDB; HostDB:ENSG00000182985; -. DR GeneTree; ENSGT00940000156093; -. DR ChiTaRS; CADM1; human. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000182985; Expressed in paraflocculus and 216 other tissues. DR ExpressionAtlas; A0A087X1W8; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 3. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR003585; Neurexin-like. DR Pfam; PF08205; C2-set_2; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00294; 4.1m; 1. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 3. DR SUPFAM; SSF48726; Immunoglobulin; 3. DR PROSITE; PS50835; IG_LIKE; 3. PE 1: Evidence at protein level; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0007829|EPD:A0A087X1W8, KW ECO:0007829|MaxQB:A0A087X1W8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 345..365 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..98 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 103..197 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 202..276 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" SQ SEQUENCE 412 AA; 45676 MW; 2A9F2495E9613CA5 CRC64; GDGQNLFTKD VTVIEGEVAT ISCQVNKSDD SVIQLLNPNR QTIYFRDFRP LKDSRFQLLN FSSSELKVSL TNVSISDEGR YFCQLYTDPP QESYTTITVL VPPRNLMIDI QKDTAVEGEE IEVNCTAMAS KPATTIRWFK GNTELKGKSE VEEWSDMYTV TSQLMLKVHK EDDGVPVICQ VEHPAVTGNL QTQRYLEVQY KPQVHIQMTY PLQGLTREGD ALELTCEAIG KPQPVMVTWV RVDDEMPQHA VLSGPNLFIN NLNKTDNGTY RCEASNIVGK AHSDYMLYVY DPPTTIPPPT TTTTTTTTTT TTILTIITDT TATTEPAVHD SRAGEEGSIR AVDHAVIGGV VAVVVFAMLC LLIILGRYFA RHKGTYFTHE AKGADDAADA DTAIINAEGG QNNSEEKKEY FI // ID H1ZZW4_HUMAN Unreviewed; 68 AA. AC H1ZZW4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 14-DEC-2022, entry version 25. DE SubName: Full=CADM1 protein {ECO:0000313|EMBL:CCD32615.1}; DE Flags: Fragment; GN Name=CADM1 {ECO:0000313|EMBL:CCD32615.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:CCD32615.1}; RN [1] {ECO:0000313|EMBL:CCD32615.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Mast cell line HMC-1 {ECO:0000313|EMBL:CCD32615.1}; RA Moiseeva E.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCD32615.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Mast cell line HMC-1 {ECO:0000313|EMBL:CCD32615.1}; RX PubMed=23063768; DOI=10.1016/j.molimm.2012.08.024; RA Moiseeva E.P., Leyland M.L., Bradding P.; RT "CADM1 is expressed as multiple alternatively spliced functional and RT dysfunctional isoforms in human mast cells."; RL Mol. Immunol. 53:345-354(2013). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HE586501; CCD32615.1; -; mRNA. DR AlphaFoldDB; H1ZZW4; -. DR PeptideAtlas; H1ZZW4; -. DR ChiTaRS; CADM1; human. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR Pfam; PF07679; I-set; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. PE 2: Evidence at transcript level; FT DOMAIN 4..36 FT /note="I-set" FT /evidence="ECO:0000259|Pfam:PF07679" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:CCD32615.1" FT NON_TER 68 FT /evidence="ECO:0000313|EMBL:CCD32615.1" SQ SEQUENCE 68 AA; 7307 MW; 9814D28B581A6450 CRC64; GPNLFINNLN KTDNGTYRCE ASNIVGKAHS DYMLYVYDSR AGEEGSIRAV DHAVIGGVVA VVVFAMLC // ID H1ZZW5_HUMAN Unreviewed; 45 AA. AC H1ZZW5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 14-DEC-2022, entry version 20. DE SubName: Full=Truncated CADM1 protein {ECO:0000313|EMBL:CCD32616.2}; GN Name=CADM1 {ECO:0000313|EMBL:CCD32616.2}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:CCD32616.2}; RN [1] {ECO:0000313|EMBL:CCD32616.2} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lung mast cells D450 {ECO:0000313|EMBL:CCD32616.2}; RA Moiseeva E.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCD32616.2} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lung mast cells D450 {ECO:0000313|EMBL:CCD32616.2}; RX PubMed=23063768; DOI=10.1016/j.molimm.2012.08.024; RA Moiseeva E.P., Leyland M.L., Bradding P.; RT "CADM1 is expressed as multiple alternatively spliced functional and RT dysfunctional isoforms in human mast cells."; RL Mol. Immunol. 53:345-354(2013). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HE586502; CCD32616.2; -; mRNA. DR AlphaFoldDB; H1ZZW5; -. DR ChiTaRS; CADM1; human. PE 2: Evidence at transcript level; SQ SEQUENCE 45 AA; 4454 MW; D4575AE3CC481105 CRC64; MASVVLPSGS QCAAAAAAAA PPGLRLRLLL LLFSAAALIP TGQFF // ID H1ZZW6_HUMAN Unreviewed; 8 AA. AC H1ZZW6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 11-DEC-2019, entry version 10. DE SubName: Full=Truncated CADM1 protein {ECO:0000313|EMBL:CCD32617.2}; DE Flags: Fragment; GN Name=CADM1 {ECO:0000313|EMBL:CCD32617.2}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:CCD32617.2}; RN [1] {ECO:0000313|EMBL:CCD32617.2} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lung mast cells D450 {ECO:0000313|EMBL:CCD32617.2}; RA Moiseeva E.; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CCD32617.2} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lung mast cells D450 {ECO:0000313|EMBL:CCD32617.2}; RX PubMed=23063768; DOI=10.1016/j.molimm.2012.08.024; RA Moiseeva E.P., Leyland M.L., Bradding P.; RT "CADM1 is expressed as multiple alternatively spliced functional and RT dysfunctional isoforms in human mast cells."; RL Mol. Immunol. 53:345-354(2013). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HE586503; CCD32617.2; -; mRNA. DR ChiTaRS; CADM1; human. PE 2: Evidence at transcript level; FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:CCD32617.2" SQ SEQUENCE 8 AA; 922 MW; 05C9D6D861B76057 CRC64; LIPTGQFF //