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Cell adhesion molecule 1 (Immunoglobulin superfamily member 4) (IgSF4) (Nectin-like protein 2) (NECL-2) (Spermatogenic immunoglobulin superfamily) (SgIgSF) (Synaptic cell adhesion molecule) (SynCAM) (Tumor suppressor in lung cancer 1) (TSLC-1)

 CADM1_HUMAN             Reviewed;         442 AA.
Q9BY67; A4FVB5; F5H0J4; H0YGA7; H1ZZV9; H1ZZW1; H1ZZW2; Q86WB8;
Q8N2F4; X5D2C8;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 2.
25-OCT-2017, entry version 146.
RecName: Full=Cell adhesion molecule 1;
AltName: Full=Immunoglobulin superfamily member 4;
Short=IgSF4;
AltName: Full=Nectin-like protein 2;
Short=NECL-2;
AltName: Full=Spermatogenic immunoglobulin superfamily;
Short=SgIgSF;
AltName: Full=Synaptic cell adhesion molecule;
Short=SynCAM;
AltName: Full=Tumor suppressor in lung cancer 1;
Short=TSLC-1;
Flags: Precursor;
Name=CADM1 {ECO:0000312|HGNC:HGNC:5951};
Synonyms=IGSF4 {ECO:0000250|UniProtKB:Q8R5M8}, IGSF4A,
NECL2 {ECO:0000303|PubMed:15811952},
SYNCAM {ECO:0000250|UniProtKB:Q8R5M8},
TSLC1 {ECO:0000303|PubMed:15811952};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAF69029.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=15893517; DOI=10.1016/j.bbamem.2005.01.013;
Zhou Y., Du G., Hu X., Yu S., Liu Y., Xu Y., Huang X., Liu J., Yin B.,
Fan M., Peng X., Qiang B., Yuan J.;
"Nectin-like molecule 1 is a protein 4.1N associated protein and
recruits protein 4.1N from cytoplasm to the plasma membrane.";
Biochim. Biophys. Acta 1669:142-154(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), FUNCTION,
SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
TISSUE=Mast cell;
PubMed=22438059; DOI=10.1007/s00018-012-0948-y;
Moiseeva E.P., Leyland M.L., Bradding P.;
"CADM1 isoforms differentially regulate human mast cell survival and
homotypic adhesion.";
Cell. Mol. Life Sci. 69:2751-2764(2012).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
TISSUE=Fetal brain;
PubMed=24722188; DOI=10.1038/ncomms4650;
Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L.,
Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S.,
Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.,
Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S.,
Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M.,
Iakoucheva L.M.;
"Protein interaction network of alternatively spliced isoforms from
brain links genetic risk factors for autism.";
Nat. Commun. 5:3650-3650(2014).
[4] {ECO:0000305, ECO:0000312|EMBL:BAC66178.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Lung {ECO:0000312|EMBL:BAC66178.1};
Ito A., Koma Y., Nagano T.;
"Cloning of a secretory isoform of SgIGSF/TSLC-1.";
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305, ECO:0000312|EMBL:BAC11657.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Embryo {ECO:0000312|EMBL:BAC11657.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11279526; DOI=10.1038/86934;
Kuramochi M., Fukuhara H., Nobukuni T., Kanbe T., Maruyama T.,
Ghosh H.P., Pletcher M., Isomura M., Onizuka M., Kitamura T.,
Sekiya T., Reeves R.H., Murakami Y.;
"TSLC1 is a tumor-suppressor gene in human non-small-cell lung
cancer.";
Nat. Genet. 27:427-430(2001).
[9] {ECO:0000305}
FUNCTION, AND INTERACTION WITH EPB41L3.
PubMed=12234973;
Yageta M., Kuramochi M., Masuda M., Fukami T., Fukuhara H.,
Maruyama T., Shibuya M., Murakami Y.;
"Direct association of TSLC1 and DAL-1, two distinct tumor suppressor
proteins in lung cancer.";
Cancer Res. 62:5129-5133(2002).
[10] {ECO:0000305}
FUNCTION, SUBUNIT, AND GLYCOSYLATION.
PubMed=12050160; DOI=10.1074/jbc.M203620200;
Masuda M., Yageta M., Fukuhara H., Kuramochi M., Maruyama T.,
Nomoto A., Murakami Y.;
"The tumor suppressor protein TSLC1 is involved in cell-cell
adhesion.";
J. Biol. Chem. 277:31014-31019(2002).
[11] {ECO:0000305}
DOMAIN.
PubMed=14633730;
Mao X., Seidlitz E., Ghosh K., Murakami Y., Ghosh H.P.;
"The cytoplasmic domain is critical to the tumor suppressor activity
of TSLC1 in non-small cell lung cancer.";
Cancer Res. 63:7979-7985(2003).
[12] {ECO:0000305}
DISEASE.
PubMed=12925956; DOI=10.1002/ijc.11348;
Fukami T., Fukuhara H., Kuramochi M., Maruyama T., Isogai K.,
Sakamoto M., Takamoto S., Murakami Y.;
"Promoter methylation of the TSLC1 gene in advanced lung tumors and
various cancer cell lines.";
Int. J. Cancer 107:53-59(2003).
[13] {ECO:0000305}
FUNCTION.
PubMed=12920246; DOI=10.1097/01.LAB.0000081391.28136.80;
Ito A., Okada M., Uchino K., Wakayama T., Koma Y., Iseki S.,
Tsubota N., Okita Y., Kitamura Y.;
"Expression of the TSLC1 adhesion molecule in pulmonary epithelium and
its down-regulation in pulmonary adenocarcinoma other than
bronchioloalveolar carcinoma.";
Lab. Invest. 83:1175-1183(2003).
[14] {ECO:0000305}
INTERACTION WITH MPP3.
PubMed=13679854; DOI=10.1038/sj.onc.1206744;
Fukuhara H., Masuda M., Yageta M., Fukami T., Kuramochi M.,
Maruyama T., Kitamura T., Murakami Y.;
"Association of a lung tumor suppressor TSLC1 with MPP3, a human
homologue of Drosophila tumor suppressor Dlg.";
Oncogene 22:6160-6165(2003).
[15] {ECO:0000305}
DOMAIN.
PubMed=15184878; DOI=10.1038/sj.onc.1207756;
Mao X., Seidlitz E., Truant R., Hitt M., Ghosh H.P.;
"Re-expression of TSLC1 in a non-small-cell lung cancer cell line
induces apoptosis and inhibits tumor growth.";
Oncogene 23:5632-5642(2004).
[16] {ECO:0000305}
FUNCTION, AND INTERACTION WITH CRTAM.
PubMed=15811952; DOI=10.1182/blood-2005-02-0817;
Boles K.S., Barchet W., Diacovo T., Cella M., Colonna M.;
"The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell
responses through the cell-surface receptor CRTAM.";
Blood 106:779-786(2005).
[17] {ECO:0000305}
INTERACTION WITH CRTAM.
PubMed=15781451; DOI=10.1074/jbc.M502095200;
Galibert L., Diemer G.S., Liu Z., Johnson R.S., Smith J.L., Walzer T.,
Comeau M.R., Rauch C.T., Wolfson M.F., Sorensen R.A.,
Van der Vuurst de Vries A.-R., Branstetter D.G., Koelling R.M.,
Scholler J., Fanslow W.C., Baum P.R., Derry J.M., Yan W.;
"Nectin-like protein 2 defines a subset of T-cell zone dendritic cells
and is a ligand for class-I-restricted T-cell-associated molecule.";
J. Biol. Chem. 280:21955-21964(2005).
[18] {ECO:0000305}
FUNCTION.
PubMed=15905536; DOI=10.4049/jimmunol.174.11.6934;
Furuno T., Ito A., Koma Y., Watabe K., Yokozaki H., Bienenstock J.,
Nakanishi M., Kitamura Y.;
"The spermatogenic Ig superfamily/synaptic cell adhesion molecule
mast-cell adhesion molecule promotes interaction with nerves.";
J. Immunol. 174:6934-6942(2005).
[19] {ECO:0000305}
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-113.
TISSUE=Plasma {ECO:0000269|PubMed:16335952};
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-113.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101; ASN-113; ASN-301 AND
ASN-302.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 400-411 IN COMPLEX WITH
EPB41L3, MUTAGENESIS OF TYR-406 AND THR-408, AND INTERACTION WITH
EPB41L3.
PubMed=21131357; DOI=10.1074/jbc.M110.174011;
Busam R.D., Thorsell A.G., Flores A., Hammarstrom M., Persson C.,
Obrink B., Hallberg B.M.;
"Structural basis of tumor suppressor in lung cancer 1 (TSLC1) binding
to differentially expressed in adenocarcinoma of the lung (DAL-
1/4.1B).";
J. Biol. Chem. 286:4511-4516(2011).
-!- FUNCTION: Mediates homophilic cell-cell adhesion in a Ca(2+)-
independent manner. Also mediates heterophilic cell-cell adhesion
with CADM3 and NECTIN3 in a Ca(2+)-independent manner. Acts as a
tumor suppressor in non-small-cell lung cancer (NSCLC) cells.
Interaction with CRTAM promotes natural killer (NK) cell
cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+
cells in vitro as well as NK cell-mediated rejection of tumors
expressing CADM3 in vivo. May contribute to the less invasive
phenotypes of lepidic growth tumor cells. In mast cells, may
mediate attachment to and promote communication with nerves.
CADM1, together with MITF, is essential for development and
survival of mast cells in vivo. Acts as a synaptic cell adhesion
molecule and plays a role in the formation of dendritic spines and
in synapse assembly (By similarity). May be involved in neuronal
migration, axon growth, pathfinding, and fasciculation on the
axons of differentiating neurons. May play diverse roles in the
spermatogenesis including in the adhesion of spermatocytes and
spermatids to Sertoli cells and for their normal differentiation
into mature spermatozoa. {ECO:0000250,
ECO:0000269|PubMed:11279526, ECO:0000269|PubMed:12050160,
ECO:0000269|PubMed:12234973, ECO:0000269|PubMed:12920246,
ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:15905536,
ECO:0000269|PubMed:22438059}.
-!- SUBUNIT: Homodimer. Interacts with FARP1 (By similarity).
Interacts with CRTAM. Interacts (via C-terminus) with
EPB41L3/DAL1. The interaction with EPB41L3/DAL1 may act to anchor
CADM1 to the actin cytoskeleton. Interacts via its C-terminus with
the PDZ domain of MPP2, MPP3 and MPP6.
{ECO:0000250|UniProtKB:Q6AYP5, ECO:0000250|UniProtKB:Q8R5M8,
ECO:0000269|PubMed:12050160, ECO:0000269|PubMed:12234973,
ECO:0000269|PubMed:13679854, ECO:0000269|PubMed:15781451,
ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:21131357}.
-!- INTERACTION:
O95727-1:CRTAM; NbExp=4; IntAct=EBI-5652260, EBI-16044697;
P60900:PSMA6; NbExp=3; IntAct=EBI-5652260, EBI-357793;
O35696:St8sia2 (xeno); NbExp=2; IntAct=EBI-5652260, EBI-15854779;
Q64690:ST8SIA4 (xeno); NbExp=2; IntAct=EBI-5652260, EBI-15854853;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11279526,
ECO:0000269|PubMed:22438059}; Single-pass type I membrane protein
{ECO:0000269|PubMed:11279526}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q8R5M8}. Note=Localized to the basolateral
plasma membrane of epithelial cells in gall bladder.
{ECO:0000250|UniProtKB:Q8R5M8}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1 {ECO:0000269|PubMed:15893517};
IsoId=Q9BY67-1; Sequence=Displayed;
Name=2 {ECO:0000269|Ref.4};
IsoId=Q9BY67-2; Sequence=VSP_052461, VSP_052462;
Name=3;
IsoId=Q9BY67-3; Sequence=VSP_047406;
Name=4;
IsoId=Q9BY67-4; Sequence=VSP_047407;
Name=5; Synonyms=E;
IsoId=Q9BY67-5; Sequence=VSP_047405;
-!- DOMAIN: The cytoplasmic domain appears to play a critical role in
proapoptosis and tumor suppressor activity in NSCLC.
{ECO:0000269|PubMed:14633730, ECO:0000269|PubMed:15184878}.
-!- PTM: Glycosylation at Asn-67 and Asn-101 promotes adhesive binding
and synapse induction. {ECO:0000250}.
-!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI25103.1; Type=Frameshift; Positions=1; Evidence={ECO:0000305};
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EMBL; AF132811; AAF69029.1; -; mRNA.
EMBL; HE586496; CCD32610.1; -; mRNA.
EMBL; HE586497; CCD32611.1; -; mRNA.
EMBL; HE586498; CCD32612.1; -; mRNA.
EMBL; HE586499; CCD32613.1; -; mRNA.
EMBL; KJ534791; AHW56431.1; -; mRNA.
EMBL; KJ534794; AHW56434.1; -; mRNA.
EMBL; AB094146; BAC66178.1; -; mRNA.
EMBL; AK075502; BAC11657.1; -; mRNA.
EMBL; AP000462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP005020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC125102; AAI25103.1; ALT_FRAME; mRNA.
CCDS; CCDS53711.1; -. [Q9BY67-5]
CCDS; CCDS73398.1; -. [Q9BY67-4]
CCDS; CCDS73399.1; -. [Q9BY67-3]
CCDS; CCDS8373.1; -. [Q9BY67-1]
RefSeq; NP_001091987.1; NM_001098517.1. [Q9BY67-5]
RefSeq; NP_001287972.1; NM_001301043.1. [Q9BY67-3]
RefSeq; NP_001287973.1; NM_001301044.1. [Q9BY67-4]
RefSeq; NP_001287974.1; NM_001301045.1.
RefSeq; NP_055148.3; NM_014333.3. [Q9BY67-1]
UniGene; Hs.370510; -.
PDB; 3BIN; X-ray; 2.30 A; B=400-411.
PDB; 4H5S; X-ray; 1.70 A; B=45-144.
PDBsum; 3BIN; -.
PDBsum; 4H5S; -.
ProteinModelPortal; Q9BY67; -.
SMR; Q9BY67; -.
BioGrid; 117218; 10.
CORUM; Q9BY67; -.
DIP; DIP-57599N; -.
IntAct; Q9BY67; 10.
MINT; MINT-1184987; -.
STRING; 9606.ENSP00000395359; -.
iPTMnet; Q9BY67; -.
PhosphoSitePlus; Q9BY67; -.
BioMuta; CADM1; -.
DMDM; 150438862; -.
EPD; Q9BY67; -.
PaxDb; Q9BY67; -.
PeptideAtlas; Q9BY67; -.
PRIDE; Q9BY67; -.
Ensembl; ENST00000331581; ENSP00000329797; ENSG00000182985. [Q9BY67-3]
Ensembl; ENST00000452722; ENSP00000395359; ENSG00000182985. [Q9BY67-1]
Ensembl; ENST00000537058; ENSP00000439817; ENSG00000182985. [Q9BY67-4]
Ensembl; ENST00000542447; ENSP00000439176; ENSG00000182985. [Q9BY67-5]
GeneID; 23705; -.
KEGG; hsa:23705; -.
UCSC; uc001ppk.4; human. [Q9BY67-1]
CTD; 23705; -.
DisGeNET; 23705; -.
EuPathDB; HostDB:ENSG00000182985.16; -.
GeneCards; CADM1; -.
HGNC; HGNC:5951; CADM1.
HPA; CAB037266; -.
MIM; 605686; gene.
neXtProt; NX_Q9BY67; -.
OpenTargets; ENSG00000182985; -.
PharmGKB; PA29764; -.
eggNOG; ENOG410IH4H; Eukaryota.
eggNOG; ENOG41116SB; LUCA.
GeneTree; ENSGT00900000140811; -.
HOGENOM; HOG000036057; -.
HOVERGEN; HBG057086; -.
InParanoid; Q9BY67; -.
KO; K06781; -.
OMA; EIYTTIT; -.
PhylomeDB; Q9BY67; -.
TreeFam; TF334317; -.
Reactome; R-HSA-418990; Adherens junctions interactions.
Reactome; R-HSA-420597; Nectin/Necl trans heterodimerization.
ChiTaRS; CADM1; human.
EvolutionaryTrace; Q9BY67; -.
GeneWiki; Cell_adhesion_molecule_1; -.
GenomeRNAi; 23705; -.
PRO; PR:Q9BY67; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000182985; -.
CleanEx; HS_CADM1; -.
ExpressionAtlas; Q9BY67; baseline and differential.
Genevisible; Q9BY67; HS.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0005913; C:cell-cell adherens junction; IBA:GO_Central.
GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0004872; F:receptor activity; IBA:GO_Central.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0034332; P:adherens junction organization; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0008037; P:cell recognition; IDA:UniProtKB.
GO; GO:0051606; P:detection of stimulus; IDA:UniProtKB.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0050715; P:positive regulation of cytokine secretion; IDA:UniProtKB.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
GO; GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; IDA:UniProtKB.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR003585; Neurexin-like.
Pfam; PF08205; C2-set_2; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00294; 4.1m; 1.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Cell adhesion;
Cell junction; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
Immunity; Immunoglobulin domain; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Signal; Spermatogenesis;
Synapse; Transmembrane; Transmembrane helix; Tumor suppressor.
SIGNAL 1 44 {ECO:0000255}.
CHAIN 45 442 Cell adhesion molecule 1. {ECO:0000255}.
/FTId=PRO_0000291968.
TOPO_DOM 45 374 Extracellular. {ECO:0000255}.
TRANSMEM 375 395 Helical. {ECO:0000255}.
TOPO_DOM 396 442 Cytoplasmic. {ECO:0000255}.
DOMAIN 45 139 Ig-like V-type. {ECO:0000255}.
DOMAIN 144 238 Ig-like C2-type 1. {ECO:0000255}.
DOMAIN 243 329 Ig-like C2-type 2. {ECO:0000255}.
MOD_RES 422 422 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8R5M8}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R5M8}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 302 302 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 304 304 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 64 124 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 166 220 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 267 313 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 332 333 DP -> GT (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_052461.
VAR_SEQ 333 360 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:24722188}.
/FTId=VSP_047405.
VAR_SEQ 334 442 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_052462.
VAR_SEQ 359 359 T -> TDTTATTEPAVHGLTQLPNSAEELDSEDLS (in
isoform 3).
{ECO:0000303|PubMed:22438059}.
/FTId=VSP_047406.
VAR_SEQ 359 359 T -> TDTTATTEPAVH (in isoform 4).
{ECO:0000303|PubMed:22438059}.
/FTId=VSP_047407.
VARIANT 285 285 D -> E (in dbSNP:rs45525440).
/FTId=VAR_061309.
MUTAGEN 406 406 Y->A: Nearly abolishes EPB41L3 binding.
{ECO:0000269|PubMed:21131357}.
MUTAGEN 408 408 T->A: Strongly reduced affinity for
EPB41L3. {ECO:0000269|PubMed:21131357}.
CONFLICT 13 13 A -> V (in Ref. 2; CCD32613).
{ECO:0000305}.
CONFLICT 153 153 K -> R (in Ref. 1; AAF69029).
{ECO:0000305}.
CONFLICT 333 359 PPTTIPPPTTTTTTTTTTTTTILTIIT -> TTATTEPAVH
GLTQLPNSAEELDSEDLS (in Ref. 5; BAC11657).
{ECO:0000305}.
STRAND 52 55 {ECO:0000244|PDB:4H5S}.
STRAND 60 68 {ECO:0000244|PDB:4H5S}.
STRAND 74 77 {ECO:0000244|PDB:4H5S}.
STRAND 83 86 {ECO:0000244|PDB:4H5S}.
STRAND 97 103 {ECO:0000244|PDB:4H5S}.
STRAND 106 113 {ECO:0000244|PDB:4H5S}.
HELIX 116 118 {ECO:0000244|PDB:4H5S}.
STRAND 120 126 {ECO:0000244|PDB:4H5S}.
STRAND 128 130 {ECO:0000244|PDB:4H5S}.
STRAND 132 141 {ECO:0000244|PDB:4H5S}.
STRAND 405 407 {ECO:0000244|PDB:3BIN}.
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


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