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 26-FEB-2020, entry version 163. 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). CC -!- FUNCTION: Mediates homophilic cell-cell adhesion in a Ca(2+)- CC independent manner. Also mediates heterophilic cell-cell adhesion with CC CADM3 and NECTIN3 in a Ca(2+)-independent manner. Acts as a tumor CC suppressor in non-small-cell lung cancer (NSCLC) cells. Interaction CC with CRTAM promotes natural killer (NK) cell cytotoxicity and CC interferon-gamma (IFN-gamma) secretion by CD8+ cells in vitro as well CC as NK cell-mediated rejection of tumors expressing CADM3 in vivo. May CC contribute to the less invasive phenotypes of lepidic growth tumor CC cells. In mast cells, may mediate attachment to and promote CC communication with nerves. CADM1, together with MITF, is essential for CC development and survival of mast cells in vivo. Acts as a synaptic cell CC adhesion molecule and plays a role in the formation of dendritic spines CC and in synapse assembly (By similarity). May be involved in neuronal CC migration, axon growth, pathfinding, and fasciculation on the axons of CC differentiating neurons. May play diverse roles in the spermatogenesis CC including in the adhesion of spermatocytes and spermatids to Sertoli CC cells and for their normal differentiation into mature spermatozoa. CC {ECO:0000250, ECO:0000269|PubMed:11279526, ECO:0000269|PubMed:12050160, CC ECO:0000269|PubMed:12234973, ECO:0000269|PubMed:12920246, CC ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:15905536, CC ECO:0000269|PubMed:22438059}. CC -!- SUBUNIT: Homodimer. Interacts with FARP1 (By similarity). Interacts CC with CRTAM. Interacts (via C-terminus) with EPB41L3/DAL1. The CC interaction with EPB41L3/DAL1 may act to anchor CADM1 to the actin CC cytoskeleton. Interacts via its C-terminus with the PDZ domain of MPP2, CC MPP3 and MPP6. {ECO:0000250|UniProtKB:Q6AYP5, CC ECO:0000250|UniProtKB:Q8R5M8, ECO:0000269|PubMed:12050160, CC ECO:0000269|PubMed:12234973, ECO:0000269|PubMed:13679854, CC ECO:0000269|PubMed:15781451, ECO:0000269|PubMed:15811952, CC ECO:0000269|PubMed:21131357}. 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 O95727-1:CRTAM; NbExp=4; IntAct=EBI-5652260, EBI-16044697; CC P60900:PSMA6; NbExp=3; IntAct=EBI-5652260, EBI-357793; CC O35696:St8sia2 (xeno); NbExp=2; IntAct=EBI-5652260, EBI-15854779; CC 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; 16. DR CORUM; Q9BY67; -. DR DIP; DIP-57599N; -. DR IntAct; Q9BY67; 13. DR MINT; Q9BY67; -. DR STRING; 9606.ENSP00000329797; -. DR GlyConnect; 1101; -. 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 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; CAB037266; -. DR MIM; 605686; gene. DR neXtProt; NX_Q9BY67; -. DR OpenTargets; ENSG00000182985; -. DR PharmGKB; PA29764; -. DR eggNOG; ENOG410IH4H; Eukaryota. DR eggNOG; ENOG41116SB; LUCA. DR GeneTree; ENSGT00940000156093; -. DR InParanoid; Q9BY67; -. DR KO; K06781; -. DR OMA; ETEMTCT; -. DR OrthoDB; 716894at2759; -. DR PhylomeDB; Q9BY67; -. DR TreeFam; TF334317; -. DR Reactome; R-HSA-418990; Adherens junctions interactions. DR Reactome; R-HSA-420597; Nectin/Necl trans heterodimerization. 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 246 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:0034332; P:adherens junction organization; TAS:Reactome. 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:0007275; P:multicellular organism development; IEA:UniProtKB-KW. DR GO; GO:0050715; P:positive regulation of cytokine secretion; 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 GO; GO:0016032; P:viral process; 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; 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; Polymorphism; KW Reference proteome; Repeat; Signal; Spermatogenesis; Synapse; KW Transmembrane; 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 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:0000244|PDB:4H5S" FT STRAND 60..68 FT /evidence="ECO:0000244|PDB:4H5S" FT STRAND 74..77 FT /evidence="ECO:0000244|PDB:4H5S" FT STRAND 83..86 FT /evidence="ECO:0000244|PDB:4H5S" FT STRAND 97..103 FT /evidence="ECO:0000244|PDB:4H5S" FT STRAND 106..113 FT /evidence="ECO:0000244|PDB:4H5S" FT HELIX 116..118 FT /evidence="ECO:0000244|PDB:4H5S" FT STRAND 120..126 FT /evidence="ECO:0000244|PDB:4H5S" FT STRAND 128..130 FT /evidence="ECO:0000244|PDB:4H5S" FT STRAND 132..141 FT /evidence="ECO:0000244|PDB:4H5S" FT STRAND 405..407 FT /evidence="ECO:0000244|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 //