CADM1_HUMAN
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 03-AUG-2022, entry version 174.
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}. 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};
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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 PRIDE; 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; 597 antibodies from 40 providers.
DR CPTC; Q9BY67; 1 antibody.
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 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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 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 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
