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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_MOUSE             Reviewed;         456 AA.
Q8R5M8; Q6F3J3; Q7TNL1; Q80VG4; Q8K3T6; Q8R4L1; Q9QYL5; Q9QYL6;
Q9Z2H8;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 2.
25-OCT-2017, entry version 134.
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|MGI:MGI:1889272};
Synonyms=Igsf4 {ECO:0000303|PubMed:12826663}, Necl2, Ra175,
Syncam {ECO:0000303|PubMed:12202822}, SynCam1 {ECO:0000305}, Tslc1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAL86736.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
STRAIN=129/SvJ {ECO:0000312|EMBL:AAL86736.1};
PubMed=12242005; DOI=10.1016/S0378-1119(02)00835-1;
Fukami T., Satoh H., Fujita E., Maruyama T., Fukuhara H.,
Kuramochi M., Takamoto S., Momoi T., Murakami Y.;
"Identification of the Tslc1 gene, a mouse orthologue of the human
tumor suppressor TSLC1 gene.";
Gene 295:7-12(2002).
[2] {ECO:0000305, ECO:0000312|EMBL:AAN01614.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAN01614.1};
PubMed=12202822; DOI=10.1126/science.1072356;
Biederer T., Sara Y., Mozhayeva M., Atasoy D., Liu X., Kavalali E.T.,
Sudhof T.C.;
"SynCAM, a synaptic adhesion molecule that drives synapse assembly.";
Science 297:1525-1531(2002).
[3] {ECO:0000305, ECO:0000312|EMBL:BAB83501.2}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6 AND 7), AND FUNCTION.
TISSUE=Embryonic carcinoma {ECO:0000312|EMBL:BAA87914.1};
PubMed=12799182; DOI=10.1016/S0014-4827(03)00095-8;
Fujita E., Soyama A., Momoi T.;
"RA175, which is the mouse ortholog of TSLC1, a tumor suppressor gene
in human lung cancer, is a cell adhesion molecule.";
Exp. Cell Res. 287:57-66(2003).
[4] {ECO:0000305, ECO:0000312|EMBL:AAQ02381.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH
MPP6, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAQ02381.1};
TISSUE=Brain {ECO:0000312|EMBL:AAQ02381.1};
PubMed=12826663; DOI=10.1074/jbc.M305387200;
Shingai T., Ikeda W., Kakunaga S., Morimoto K., Takekuni K., Itoh S.,
Satoh K., Takeuchi M., Imai T., Monden M., Takai Y.;
"Implications of nectin-like molecule-
2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and
transmembrane protein localization in epithelial cells.";
J. Biol. Chem. 278:35421-35427(2003).
[5] {ECO:0000305, ECO:0000312|EMBL:AAC67243.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 49-456 (ISOFORM 2).
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).
[6] {ECO:0000305, ECO:0000312|EMBL:BAC66173.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC66173.1};
TISSUE=Mast cell {ECO:0000312|EMBL:BAC66173.1};
Ito A., Koma Y., Nagano T.;
"A secretion form of SgIGSF/TSLC1.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000305, ECO:0000312|EMBL:BAC66173.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
Fujita E., Aikawa K., Momoi T.;
"Neuron-specific isoforms of RA175/TSLC1/SynCAM.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
PubMed=12606335; DOI=10.1095/biolreprod.102.012344;
Wakayama T., Koami H., Ariga H., Kobayashi D., Sai Y., Tsuji A.,
Yamamoto M., Iseki S.;
"Expression and functional characterization of the adhesion molecule
spermatogenic immunoglobulin superfamily in the mouse testis.";
Biol. Reprod. 68:1755-1763(2003).
[9] {ECO:0000305}
FUNCTION.
PubMed=15158462; DOI=10.1016/j.bbrc.2004.04.172;
Ito A., Koma Y., Watabe K., Jippo T., Wakayama T., Iseki S.,
Kitamura Y.;
"Contribution of the SgIGSF adhesion molecule to survival of cultured
mast cells in vivo.";
Biochem. Biophys. Res. Commun. 319:200-206(2004).
[10] {ECO:0000305}
FUNCTION, AND INTERACTION WITH CADM1.
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).
[11] {ECO:0000305}
FUNCTION.
PubMed=15707673; DOI=10.1016/j.devbrainres.2004.10.015;
Fujita E., Urase K., Soyama A., Kouroku Y., Momoi T.;
"Distribution of RA175/TSLC1/SynCAM, a member of the immunoglobulin
superfamily, in the developing nervous system.";
Brain Res. Dev. Brain Res. 154:199-209(2005).
[12] {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).
[13] {ECO:0000305}
FUNCTION.
PubMed=16605125;
Kitamura Y.;
"MITF and SgIGSF: an essential transcription factor and its target
adhesion molecule for development and survival of mast cells.";
Novartis Found. Symp. 271:4-11(2005).
[14] {ECO:0000305}
DISRUPTION PHENOTYPE.
PubMed=16382161; DOI=10.1128/MCB.26.2.718-726.2006;
Fujita E., Kouroku Y., Ozeki S., Tanabe Y., Toyama Y., Maekawa M.,
Kojima N., Senoo H., Toshimori K., Momoi T.;
"Oligo-astheno-teratozoospermia in mice lacking
RA175/TSLC1/SynCAM/IGSF4A, a cell adhesion molecule in the
immunoglobulin superfamily.";
Mol. Cell. Biol. 26:718-726(2006).
[15] {ECO:0000305}
DISRUPTION PHENOTYPE.
PubMed=16611999; DOI=10.1128/MCB.26.9.3595-3609.2006;
van der Weyden L., Arends M.J., Chausiaux O.E., Ellis P.J.,
Lange U.C., Surani M.A., Affara N., Murakami Y., Adams D.J.,
Bradley A.;
"Loss of TSLC1 causes male infertility due to a defect at the
spermatid stage of spermatogenesis.";
Mol. Cell. Biol. 26:3595-3609(2006).
[16] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16612000; DOI=10.1128/MCB.26.9.3610-3624.2006;
Yamada D., Yoshida M., Williams Y.N., Fukami T., Kikuchi S.,
Masuda M., Maruyama T., Ohta T., Nakae D., Maekawa A., Kitamura T.,
Murakami Y.;
"Disruption of spermatogenic cell adhesion and male infertility in
mice lacking TSLC1/IGSF4, an immunoglobulin superfamily cell adhesion
molecule.";
Mol. Cell. Biol. 26:3610-3624(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104 AND ASN-116.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-104; ASN-116;
ASN-168; ASN-304; ASN-307 AND ASN-311.
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-436, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[21]
GLYCOSYLATION AT ASN-70 AND ASN-104, AND SUBCELLULAR LOCATION.
PubMed=20739279; DOI=10.1074/jbc.M110.120865;
Fogel A.I., Li Y., Giza J., Wang Q., Lam T.T., Modis Y., Biederer T.;
"N-glycosylation at the SynCAM (synaptic cell adhesion molecule)
immunoglobulin interface modulates synaptic adhesion.";
J. Biol. Chem. 285:34864-34874(2010).
[22]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FARP1.
PubMed=23209303; DOI=10.1083/jcb.201205041;
Cheadle L., Biederer T.;
"The novel synaptogenic protein Farp1 links postsynaptic cytoskeletal
dynamics and transsynaptic organization.";
J. Cell Biol. 199:985-1001(2012).
-!- 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. 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:0000269|PubMed:12202822,
ECO:0000269|PubMed:12606335, ECO:0000269|PubMed:12799182,
ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:15158462,
ECO:0000269|PubMed:15707673, ECO:0000269|PubMed:15811952,
ECO:0000269|PubMed:16605125, ECO:0000269|PubMed:16612000,
ECO:0000269|PubMed:23209303}.
-!- SUBUNIT: Homodimer. 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. Interacts
with FARP1. {ECO:0000250|UniProtKB:Q6AYP5,
ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:15781451,
ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:23209303}.
-!- INTERACTION:
P16144:ITGB4 (xeno); NbExp=3; IntAct=EBI-5651941, EBI-948678;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12826663,
ECO:0000269|PubMed:20739279}; Single-pass type I membrane protein
{ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:20739279}. Cell
junction, synapse {ECO:0000269|PubMed:20739279,
ECO:0000269|PubMed:23209303}. Note=Localized to the basolateral
plasma membrane of epithelial cells in gall bladder.
{ECO:0000269|PubMed:12826663}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1 {ECO:0000269|PubMed:12799182};
IsoId=Q8R5M8-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:12202822, ECO:0000269|PubMed:12242005,
ECO:0000269|PubMed:15893517, ECO:0000269|Ref.7};
IsoId=Q8R5M8-2; Sequence=VSP_052470;
Name=3 {ECO:0000269|Ref.7};
IsoId=Q8R5M8-3; Sequence=VSP_052466;
Name=4 {ECO:0000269|PubMed:12826663, ECO:0000269|Ref.7};
IsoId=Q8R5M8-4; Sequence=VSP_052465;
Name=5 {ECO:0000269|Ref.6, ECO:0000269|Ref.7};
IsoId=Q8R5M8-5; Sequence=VSP_052464, VSP_052468;
Name=6 {ECO:0000269|PubMed:12799182};
IsoId=Q8R5M8-6; Sequence=VSP_052463, VSP_052469;
Name=7 {ECO:0000269|PubMed:12799182};
IsoId=Q8R5M8-7; Sequence=VSP_052463, VSP_052467;
-!- TISSUE SPECIFICITY: Expressed in brain, lung, kidney, testis,
heart, spleen and liver, but not expressed in skeletal muscle. In
brain, enriched in the synaptic plasma membrane. Expressed
dominantly in epithelial cells but not expressed in fibroblast
cells (at protein level). {ECO:0000269|PubMed:12202822,
ECO:0000269|PubMed:12242005, ECO:0000269|PubMed:12606335,
ECO:0000269|PubMed:12826663}.
-!- DEVELOPMENTAL STAGE: Expressed in spermatogenic cells during early
spermatogenesis. Expression increases in intermediate
spermatogonia through to zygotene spermatocytes but becomes
diminished in the steps from early pachytene spermatocytes through
to round spermatids. After meiosis, expression reappears in
spermatids and is present in elongating spermatids until
spermiation. Not detected in Sertoli cells.
{ECO:0000269|PubMed:12606335}.
-!- DOMAIN: The cytoplasmic domain appears to play a critical role in
proapoptosis and tumor suppressor activity in NSCLC.
{ECO:0000250|UniProtKB:Q9BY67}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12606335,
ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770,
ECO:0000269|PubMed:20739279}.
-!- PTM: Glycosylation at Asn-70 and Asn-104 promotes adhesive binding
and synapse induction. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Male mice are infertile, due to a defect at
the spermatid stage of spermatogenesis, and show
oligoasthenoteratozoospermia with almost no mature motile
spermatozoa in the epididymis. Heterozygous males and females and
homozygous null females are fertile and have no overt
developmental defects. {ECO:0000269|PubMed:16382161,
ECO:0000269|PubMed:16611999, ECO:0000269|PubMed:16612000}.
-!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC67243.1; Type=Frameshift; Positions=65; Evidence={ECO:0000305};
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EMBL; AF434663; AAL86736.1; -; mRNA.
EMBL; AF539424; AAN01614.1; -; mRNA.
EMBL; AB021964; BAA87914.1; -; mRNA.
EMBL; AB021965; BAA87915.1; -; mRNA.
EMBL; AB064265; BAB83501.2; -; mRNA.
EMBL; AY351388; AAQ02381.1; -; mRNA.
EMBL; AF061260; AAC67243.1; ALT_FRAME; mRNA.
EMBL; AB092414; BAC66173.1; -; mRNA.
EMBL; AB183399; BAD30018.1; -; mRNA.
EMBL; AB183400; BAD30019.1; -; mRNA.
EMBL; AB183401; BAD30020.1; -; mRNA.
EMBL; AB183402; BAD30021.1; -; mRNA.
CCDS; CCDS23147.1; -. [Q8R5M8-4]
CCDS; CCDS23148.1; -. [Q8R5M8-2]
CCDS; CCDS23149.1; -. [Q8R5M8-1]
CCDS; CCDS23150.1; -. [Q8R5M8-3]
RefSeq; NP_001020771.1; NM_001025600.1. [Q8R5M8-4]
RefSeq; NP_061240.3; NM_018770.3. [Q8R5M8-2]
RefSeq; NP_997558.2; NM_207675.2. [Q8R5M8-1]
RefSeq; NP_997559.1; NM_207676.2. [Q8R5M8-3]
UniGene; Mm.234832; -.
ProteinModelPortal; Q8R5M8; -.
IntAct; Q8R5M8; 3.
MINT; MINT-4131381; -.
STRING; 10090.ENSMUSP00000083073; -.
iPTMnet; Q8R5M8; -.
PhosphoSitePlus; Q8R5M8; -.
PaxDb; Q8R5M8; -.
PeptideAtlas; Q8R5M8; -.
PRIDE; Q8R5M8; -.
Ensembl; ENSMUST00000034581; ENSMUSP00000034581; ENSMUSG00000032076. [Q8R5M8-4]
Ensembl; ENSMUST00000085909; ENSMUSP00000083073; ENSMUSG00000032076. [Q8R5M8-1]
Ensembl; ENSMUST00000114547; ENSMUSP00000110194; ENSMUSG00000032076. [Q8R5M8-2]
Ensembl; ENSMUST00000114548; ENSMUSP00000110195; ENSMUSG00000032076. [Q8R5M8-3]
GeneID; 54725; -.
KEGG; mmu:54725; -.
UCSC; uc009phn.1; mouse. [Q8R5M8-5]
UCSC; uc009pho.1; mouse. [Q8R5M8-1]
UCSC; uc009phq.1; mouse. [Q8R5M8-3]
UCSC; uc009phr.1; mouse. [Q8R5M8-4]
UCSC; uc009phs.1; mouse. [Q8R5M8-2]
CTD; 23705; -.
MGI; MGI:1889272; Cadm1.
eggNOG; ENOG410IH4H; Eukaryota.
eggNOG; ENOG41116SB; LUCA.
GeneTree; ENSGT00900000140811; -.
HOVERGEN; HBG057086; -.
InParanoid; Q8R5M8; -.
KO; K06781; -.
PhylomeDB; Q8R5M8; -.
TreeFam; TF334317; -.
Reactome; R-MMU-418990; Adherens junctions interactions.
Reactome; R-MMU-420597; Nectin/Necl trans heterodimerization.
ChiTaRS; Cadm1; mouse.
PRO; PR:Q8R5M8; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032076; -.
CleanEx; MM_CADM1; -.
ExpressionAtlas; Q8R5M8; baseline and differential.
Genevisible; Q8R5M8; MM.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0070852; C:cell body fiber; IDA:MGI.
GO; GO:0005913; C:cell-cell adherens junction; IBA:GO_Central.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
GO; GO:0043196; C:varicosity; IDA:MGI.
GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0004872; F:receptor activity; IBA:GO_Central.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0060348; P:bone development; IMP:MGI.
GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IDA:MGI.
GO; GO:0007155; P:cell adhesion; IDA:MGI.
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; IDA:UniProtKB.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0050715; P:positive regulation of cytokine secretion; ISO:MGI.
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.
GO; GO:0007416; P:synapse assembly; IDA:MGI.
GO; GO:0009826; P:unidimensional cell growth; IMP:MGI.
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;
Alternative splicing; Apoptosis; Cell adhesion; Cell junction;
Cell membrane; Complete proteome; Developmental protein;
Differentiation; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
Repeat; Signal; Spermatogenesis; Synapse; Transmembrane;
Transmembrane helix; Tumor suppressor.
SIGNAL 1 47 {ECO:0000255}.
CHAIN 48 456 Cell adhesion molecule 1. {ECO:0000255}.
/FTId=PRO_0000291969.
TOPO_DOM 48 388 Extracellular. {ECO:0000255}.
TRANSMEM 389 409 Helical. {ECO:0000255}.
TOPO_DOM 410 456 Cytoplasmic. {ECO:0000255}.
DOMAIN 48 142 Ig-like V-type. {ECO:0000255}.
DOMAIN 147 241 Ig-like C2-type 1. {ECO:0000255}.
DOMAIN 246 332 Ig-like C2-type 2. {ECO:0000255}.
MOD_RES 436 436 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 448 448 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:20739279}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770,
ECO:0000269|PubMed:20739279}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 304 304 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 67 127 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 169 223 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 270 316 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 150 Missing (in isoform 6 and isoform 7).
{ECO:0000303|PubMed:12799182,
ECO:0000303|Ref.6, ECO:0000303|Ref.7}.
/FTId=VSP_052463.
VAR_SEQ 335 336 DP -> GT (in isoform 5).
{ECO:0000303|PubMed:15893517,
ECO:0000303|Ref.6, ECO:0000303|Ref.7}.
/FTId=VSP_052464.
VAR_SEQ 336 374 Missing (in isoform 4).
{ECO:0000303|PubMed:12826663,
ECO:0000303|Ref.7}.
/FTId=VSP_052465.
VAR_SEQ 336 363 Missing (in isoform 3).
{ECO:0000303|PubMed:12799182,
ECO:0000303|Ref.7}.
/FTId=VSP_052466.
VAR_SEQ 336 352 Missing (in isoform 7).
{ECO:0000303|PubMed:12799182,
ECO:0000303|Ref.7}.
/FTId=VSP_052467.
VAR_SEQ 337 456 Missing (in isoform 5).
{ECO:0000303|PubMed:15893517,
ECO:0000303|Ref.6, ECO:0000303|Ref.7}.
/FTId=VSP_052468.
VAR_SEQ 355 365 Missing (in isoform 6).
{ECO:0000303|PubMed:12799182,
ECO:0000303|Ref.6}.
/FTId=VSP_052469.
VAR_SEQ 364 374 Missing (in isoform 2).
{ECO:0000303|PubMed:12202822,
ECO:0000303|PubMed:12242005,
ECO:0000303|PubMed:15893517,
ECO:0000303|Ref.7}.
/FTId=VSP_052470.
CONFLICT 8 8 S -> C (in Ref. 2; AAN01614 and 7;
BAD30018). {ECO:0000305}.
CONFLICT 266 266 F -> L (in Ref. 3; BAA87914/BAA87915).
{ECO:0000305}.
CONFLICT 315 315 R -> P (in Ref. 3; BAA87914/BAA87915).
{ECO:0000305}.
CONFLICT 330 330 M -> I (in Ref. 3; BAA87914/BAA87915).
{ECO:0000305}.
CONFLICT 356 356 T -> S (in Ref. 2; AAN01614 and 7;
BAD30018). {ECO:0000305}.
CONFLICT 429 429 D -> N (in Ref. 3; BAB83501).
{ECO:0000305}.
SEQUENCE 456 AA; 49788 MW; 3226E86C04161C7F CRC64;
MASAVLPSGS QCAAAAAVAA AAAPPGLRLR LLLLLLSAAA LIPTGDGQNL FTKDVTVIEG
EVATISCQVN KSDDSVIQLL NPNRQTIYFR DFRPLKDSRF QLLNFSSSEL KVSLTNVSIS
DEGRYFCQLY TDPPQESYTT ITVLVPPRNL MIDIQKDTAV EGEEIEVNCT AMASKPATTI
RWFKGNKELK GKSEVEEWSD MYTVTSQLML KVHKEDDGVP VICQVEHPAV TGNLQTQRYL
EVQYKPQVHI QMTYPLQGLT REGDAFELTC EAIGKPQPVM VTWVRVDDEM PQHAVLSGPN
LFINNLNKTD NGTYRCEASN IVGKAHSDYM LYVYDPPTTI PPPTTTTTTT TTTTTTILTI
ITDTTATTEP AVHDSRAGEE GTIGAVDHAV IGGVVAVVVF AMLCLLIILG RYFARHKGTY
FTHEAKGADD AADADTAIIN AEGGQNNSEE KKEYFI


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