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 29-SEP-2021, entry version 171. 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, GN NECL2 {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}. Cell junction, synapse CC {ECO:0000250|UniProtKB:Q8R5M8}. Note=Localized to the basolateral CC plasma membrane of epithelial cells in gall bladder. CC {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 SMR; Q9BY67; -. DR BioGRID; 117218; 18. DR CORUM; Q9BY67; -. DR DIP; DIP-57599N; -. DR IntAct; Q9BY67; 14. 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 PaxDb; Q9BY67; -. DR PeptideAtlas; Q9BY67; -. DR PRIDE; Q9BY67; -. DR ProteomicsDB; 25359; -. DR ProteomicsDB; 38329; -. DR ProteomicsDB; 79594; -. [Q9BY67-1] DR ProteomicsDB; 79595; -. [Q9BY67-2] DR ABCD; Q9BY67; 12 sequenced antibodies. DR Antibodypedia; 32257; 653 antibodies. DR DNASU; 23705; -. DR Ensembl; ENST00000331581; ENSP00000329797; ENSG00000182985. [Q9BY67-3] DR Ensembl; ENST00000452722; ENSP00000395359; ENSG00000182985. [Q9BY67-1] DR Ensembl; ENST00000537058; ENSP00000439817; ENSG00000182985. [Q9BY67-4] DR Ensembl; ENST00000542447; ENSP00000439176; ENSG00000182985. [Q9BY67-5] DR GeneID; 23705; -. DR KEGG; hsa:23705; -. DR UCSC; uc001ppk.4; human. [Q9BY67-1] DR CTD; 23705; -. DR DisGeNET; 23705; -. DR GeneCards; CADM1; -. DR HGNC; HGNC:5951; CADM1. DR HPA; ENSG00000182985; Low tissue specificity. 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; MLFVYDP; -. 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 BioGRID-ORCS; 23705; 4 hits in 1011 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 cerebellum and 258 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell. 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: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: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; SSF48726; 3. DR PROSITE; PS50835; IG_LIKE; 3. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Cell adhesion; KW Cell junction; Cell membrane; Developmental protein; Differentiation; KW Disulfide bond; Glycoprotein; Host-virus interaction; Immunity; KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome; KW Repeat; Signal; Spermatogenesis; Synapse; Transmembrane; KW Transmembrane helix; 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 52..55 FT /evidence="ECO:0007829|PDB:4H5S" FT STRAND 60..68 FT /evidence="ECO:0007829|PDB:4H5S" FT STRAND 74..77 FT /evidence="ECO:0007829|PDB:4H5S" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:4H5S" FT STRAND 97..103 FT /evidence="ECO:0007829|PDB:4H5S" FT STRAND 106..113 FT /evidence="ECO:0007829|PDB:4H5S" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:4H5S" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:4H5S" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:4H5S" FT STRAND 132..141 FT /evidence="ECO:0007829|PDB:4H5S" 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 //