CADM1_MOUSE
ID CADM1_MOUSE Reviewed; 456 AA.
AC Q8R5M8; Q6F3J3; Q7TNL1; Q80VG4; Q8K3T6; Q8R4L1; Q9QYL5; Q9QYL6; Q9Z2H8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
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|MGI:MGI:1889272};
GN Synonyms=Igsf4 {ECO:0000303|PubMed:12826663}, Necl2, Ra175,
GN Syncam {ECO:0000303|PubMed:12202822}, SynCam1 {ECO:0000305}, Tslc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAL86736.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ {ECO:0000312|EMBL:AAL86736.1};
RX PubMed=12242005; DOI=10.1016/s0378-1119(02)00835-1;
RA Fukami T., Satoh H., Fujita E., Maruyama T., Fukuhara H., Kuramochi M.,
RA Takamoto S., Momoi T., Murakami Y.;
RT "Identification of the Tslc1 gene, a mouse orthologue of the human tumor
RT suppressor TSLC1 gene.";
RL Gene 295:7-12(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAN01614.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAN01614.1};
RX PubMed=12202822; DOI=10.1126/science.1072356;
RA Biederer T., Sara Y., Mozhayeva M., Atasoy D., Liu X., Kavalali E.T.,
RA Sudhof T.C.;
RT "SynCAM, a synaptic adhesion molecule that drives synapse assembly.";
RL Science 297:1525-1531(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAB83501.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6 AND 7), AND FUNCTION.
RC TISSUE=Embryonic carcinoma {ECO:0000312|EMBL:BAA87914.1};
RX PubMed=12799182; DOI=10.1016/s0014-4827(03)00095-8;
RA Fujita E., Soyama A., Momoi T.;
RT "RA175, which is the mouse ortholog of TSLC1, a tumor suppressor gene in
RT human lung cancer, is a cell adhesion molecule.";
RL Exp. Cell Res. 287:57-66(2003).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAQ02381.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH PALS2,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAQ02381.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAQ02381.1};
RX PubMed=12826663; DOI=10.1074/jbc.m305387200;
RA Shingai T., Ikeda W., Kakunaga S., Morimoto K., Takekuni K., Itoh S.,
RA Satoh K., Takeuchi M., Imai T., Monden M., Takai Y.;
RT "Implications of nectin-like molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in
RT cell-cell adhesion and transmembrane protein localization in epithelial
RT cells.";
RL J. Biol. Chem. 278:35421-35427(2003).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAC67243.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-456 (ISOFORM 2).
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 [6] {ECO:0000305, ECO:0000312|EMBL:BAC66173.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC66173.1};
RC TISSUE=Mast cell {ECO:0000312|EMBL:BAC66173.1};
RA Ito A., Koma Y., Nagano T.;
RT "A secretion form of SgIGSF/TSLC1.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305, ECO:0000312|EMBL:BAC66173.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
RA Fujita E., Aikawa K., Momoi T.;
RT "Neuron-specific isoforms of RA175/TSLC1/SynCAM.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RX PubMed=12606335; DOI=10.1095/biolreprod.102.012344;
RA Wakayama T., Koami H., Ariga H., Kobayashi D., Sai Y., Tsuji A.,
RA Yamamoto M., Iseki S.;
RT "Expression and functional characterization of the adhesion molecule
RT spermatogenic immunoglobulin superfamily in the mouse testis.";
RL Biol. Reprod. 68:1755-1763(2003).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=15158462; DOI=10.1016/j.bbrc.2004.04.172;
RA Ito A., Koma Y., Watabe K., Jippo T., Wakayama T., Iseki S., Kitamura Y.;
RT "Contribution of the SgIGSF adhesion molecule to survival of cultured mast
RT cells in vivo.";
RL Biochem. Biophys. Res. Commun. 319:200-206(2004).
RN [10] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH CADM1.
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 [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=15707673; DOI=10.1016/j.devbrainres.2004.10.015;
RA Fujita E., Urase K., Soyama A., Kouroku Y., Momoi T.;
RT "Distribution of RA175/TSLC1/SynCAM, a member of the immunoglobulin
RT superfamily, in the developing nervous system.";
RL Brain Res. Dev. Brain Res. 154:199-209(2005).
RN [12] {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 [13] {ECO:0000305}
RP FUNCTION.
RX PubMed=16605125;
RA Kitamura Y.;
RT "MITF and SgIGSF: an essential transcription factor and its target adhesion
RT molecule for development and survival of mast cells.";
RL Novartis Found. Symp. 271:4-11(2005).
RN [14] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=16382161; DOI=10.1128/mcb.26.2.718-726.2006;
RA Fujita E., Kouroku Y., Ozeki S., Tanabe Y., Toyama Y., Maekawa M.,
RA Kojima N., Senoo H., Toshimori K., Momoi T.;
RT "Oligo-astheno-teratozoospermia in mice lacking RA175/TSLC1/SynCAM/IGSF4A,
RT a cell adhesion molecule in the immunoglobulin superfamily.";
RL Mol. Cell. Biol. 26:718-726(2006).
RN [15] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=16611999; DOI=10.1128/mcb.26.9.3595-3609.2006;
RA van der Weyden L., Arends M.J., Chausiaux O.E., Ellis P.J., Lange U.C.,
RA Surani M.A., Affara N., Murakami Y., Adams D.J., Bradley A.;
RT "Loss of TSLC1 causes male infertility due to a defect at the spermatid
RT stage of spermatogenesis.";
RL Mol. Cell. Biol. 26:3595-3609(2006).
RN [16] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16612000; DOI=10.1128/mcb.26.9.3610-3624.2006;
RA Yamada D., Yoshida M., Williams Y.N., Fukami T., Kikuchi S., Masuda M.,
RA Maruyama T., Ohta T., Nakae D., Maekawa A., Kitamura T., Murakami Y.;
RT "Disruption of spermatogenic cell adhesion and male infertility in mice
RT lacking TSLC1/IGSF4, an immunoglobulin superfamily cell adhesion
RT molecule.";
RL Mol. Cell. Biol. 26:3610-3624(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19752223; DOI=10.4049/jimmunol.0901248;
RA Takeuchi A., Itoh Y., Takumi A., Ishihara C., Arase N., Yokosuka T.,
RA Koseki H., Yamasaki S., Takai Y., Miyoshi J., Ogasawara K., Saito T.;
RT "CRTAM confers late-stage activation of CD8+ T cells to regulate retention
RT within lymph node.";
RL J. Immunol. 183:4220-4228(2009).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104 AND ASN-116.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [20]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-104; ASN-116; ASN-168;
RP ASN-307 AND ASN-311.
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-436, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [22]
RP GLYCOSYLATION AT ASN-70 AND ASN-104, AND SUBCELLULAR LOCATION.
RX PubMed=20739279; DOI=10.1074/jbc.m110.120865;
RA Fogel A.I., Li Y., Giza J., Wang Q., Lam T.T., Modis Y., Biederer T.;
RT "N-glycosylation at the SynCAM (synaptic cell adhesion molecule)
RT immunoglobulin interface modulates synaptic adhesion.";
RL J. Biol. Chem. 285:34864-34874(2010).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FARP1.
RX PubMed=23209303; DOI=10.1083/jcb.201205041;
RA Cheadle L., Biederer T.;
RT "The novel synaptogenic protein Farp1 links postsynaptic cytoskeletal
RT dynamics and transsynaptic organization.";
RL J. Cell Biol. 199:985-1001(2012).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24687959; DOI=10.1084/jem.20130904;
RA Cortez V.S., Cervantes-Barragan L., Song C., Gilfillan S., McDonald K.G.,
RA Tussiwand R., Edelson B.T., Murakami Y., Murphy K.M., Newberry R.D.,
RA Sibley L.D., Colonna M.;
RT "CRTAM controls residency of gut CD4+CD8+ T cells in the steady state and
RT maintenance of gut CD4+ Th17 during parasitic infection.";
RL J. Exp. Med. 211:623-633(2014).
CC -!- FUNCTION: Mediates homophilic cell-cell adhesion in a Ca(2+)-
CC independent manner (PubMed:12202822, PubMed:12799182, PubMed:12826663).
CC Also mediates heterophilic cell-cell adhesion with CADM3 and NECTIN3 in
CC a Ca(2+)-independent manner (PubMed:12826663). Interaction with CRTAM
CC promotes natural killer (NK) cell cytotoxicity and interferon-gamma
CC (IFN-gamma) secretion by CD8+ T-cells in vitro as well as NK cell-
CC mediated rejection of tumors expressing CADM1 in vivo
CC (PubMed:15811952). In mast cells, may mediate attachment to and promote
CC communication with nerves (By similarity). CADM1, together with MITF,
CC is essential for development and survival of mast cells in vivo
CC (PubMed:15158462, PubMed:16605125). By interacting with CRTAM and thus
CC promoting the adhesion between CD8+ T-cells and CD8+ dendritic cells,
CC regulates the retention of activated CD8+ T-cell within the draining
CC lymph node (PubMed:19752223). Required for the intestinal retention of
CC intraepithelial CD4+ CD8+ T-cells and, to a lesser extent,
CC intraepithelial and lamina propria CD8+ T-cells and CD4+ T-cells
CC (PubMed:24687959). Interaction with CRTAM promotes the adhesion to gut-
CC associated CD103+ dendritic cells, which may facilitate the expression
CC of gut-homing and adhesion molecules on T-cells and the conversion of
CC CD4+ T-cells into CD4+ CD8+ T-cells (PubMed:24687959). Acts as a
CC synaptic cell adhesion molecule and plays a role in the formation of
CC dendritic spines and in synapse assembly (PubMed:12202822,
CC PubMed:23209303). May be involved in neuronal migration, axon growth,
CC pathfinding, and fasciculation on the axons of differentiating neurons
CC (PubMed:15707673). 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 (PubMed:12606335, PubMed:16612000). {ECO:0000250|UniProtKB:Q9BY67,
CC ECO:0000269|PubMed:12202822, ECO:0000269|PubMed:12606335,
CC ECO:0000269|PubMed:12799182, ECO:0000269|PubMed:12826663,
CC ECO:0000269|PubMed:15158462, ECO:0000269|PubMed:15707673,
CC ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:16605125,
CC ECO:0000269|PubMed:16612000, ECO:0000269|PubMed:19752223,
CC ECO:0000269|PubMed:23209303, ECO:0000269|PubMed:24687959}.
CC -!- SUBUNIT: Homodimer (via Ig-like V-type domain) (By similarity).
CC Interacts with FARP1 (PubMed:23209303). Interacts (via Ig-like V-type
CC domain) with CRTAM (via Ig-like V-type domain); the interaction
CC competes with CRTAM homodimerization and CADM1 homodimerization
CC (PubMed:15811952, PubMed:15781451). Interacts (via C-terminus) with
CC EPB41L3/DAL1 (By similarity). The interaction with EPB41L3/DAL1 may act
CC to anchor CADM1 to the actin cytoskeleton (By similarity). Interacts
CC (via C-terminus) with MPP2 (via PDZ domain) (By similarity). Interacts
CC (via C-terminus) with MPP3 (via PDZ domain) (By similarity). Interacts
CC (via C-terminus) with PALS2 (via PDZ domain) (PubMed:12826663).
CC {ECO:0000250|UniProtKB:Q6AYP5, ECO:0000250|UniProtKB:Q9BY67,
CC ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:15781451,
CC ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:23209303}.
CC -!- INTERACTION:
CC Q8R5M8-2; P16144: ITGB4; Xeno; NbExp=3; IntAct=EBI-5651941, EBI-948678;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12826663,
CC ECO:0000269|PubMed:19752223, ECO:0000269|PubMed:20739279,
CC ECO:0000269|PubMed:24687959}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:20739279}. Synaptic
CC cell membrane {ECO:0000269|PubMed:20739279,
CC ECO:0000269|PubMed:23209303}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=Localized to the basolateral plasma membrane of
CC epithelial cells in gall bladder. {ECO:0000269|PubMed:12826663}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1 {ECO:0000269|PubMed:12799182};
CC IsoId=Q8R5M8-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12202822, ECO:0000269|PubMed:12242005,
CC ECO:0000269|PubMed:15893517, ECO:0000269|Ref.7};
CC IsoId=Q8R5M8-2; Sequence=VSP_052470;
CC Name=3 {ECO:0000269|Ref.7};
CC IsoId=Q8R5M8-3; Sequence=VSP_052466;
CC Name=4 {ECO:0000269|PubMed:12826663, ECO:0000269|Ref.7};
CC IsoId=Q8R5M8-4; Sequence=VSP_052465;
CC Name=5 {ECO:0000269|Ref.6, ECO:0000269|Ref.7};
CC IsoId=Q8R5M8-5; Sequence=VSP_052464, VSP_052468;
CC Name=6 {ECO:0000269|PubMed:12799182};
CC IsoId=Q8R5M8-6; Sequence=VSP_052463, VSP_052469;
CC Name=7 {ECO:0000269|PubMed:12799182};
CC IsoId=Q8R5M8-7; Sequence=VSP_052463, VSP_052467;
CC -!- TISSUE SPECIFICITY: Expressed dominantly in epithelial cells but not
CC expressed in fibroblast cells (at protein level) (PubMed:12826663).
CC Expressed in the T-cell area of lymph nodes, specifically in CD8+ and
CC CD4- CD8- dendritic cells (at protein level) (PubMed:19752223).
CC Expressed in CD8+ dendritic cells in the spleen (at protein level)
CC (PubMed:19752223). Expressed in CD103+ dendritic cells in the small
CC intestine lamina propria and mesenteric lymph nodes (at protein level)
CC (PubMed:24687959). Expressed in brain, lung, kidney, testis, heart,
CC spleen and liver, but not expressed in skeletal muscle
CC (PubMed:12242005, PubMed:12606335, PubMed:12202822).
CC {ECO:0000269|PubMed:12202822, ECO:0000269|PubMed:12242005,
CC ECO:0000269|PubMed:12606335, ECO:0000269|PubMed:12826663,
CC ECO:0000269|PubMed:19752223, ECO:0000269|PubMed:24687959}.
CC -!- DEVELOPMENTAL STAGE: Expressed in spermatogenic cells during early
CC spermatogenesis. Expression increases in intermediate spermatogonia
CC through to zygotene spermatocytes but becomes diminished in the steps
CC from early pachytene spermatocytes through to round spermatids. After
CC meiosis, expression reappears in spermatids and is present in
CC elongating spermatids until spermiation. Not detected in Sertoli cells.
CC {ECO:0000269|PubMed:12606335}.
CC -!- DOMAIN: The cytoplasmic domain appears to play a critical role in
CC proapoptosis and tumor suppressor activity in NSCLC.
CC {ECO:0000250|UniProtKB:Q9BY67}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12606335,
CC ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770,
CC ECO:0000269|PubMed:20739279}.
CC -!- PTM: Glycosylation at Asn-70 and Asn-104 promotes adhesive binding and
CC synapse induction. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Male mice are infertile, due to a defect at the
CC spermatid stage of spermatogenesis, and show
CC oligoasthenoteratozoospermia with almost no mature motile spermatozoa
CC in the epididymis (PubMed:16382161, PubMed:16611999, PubMed:16612000).
CC Heterozygous males and females and homozygous null females are fertile
CC and have no overt developmental defects (PubMed:16382161,
CC PubMed:16611999, PubMed:16612000). In the small intestine mucosa and
CC under steady-state conditions, severe reduction in the number of
CC intraepithelial CD4+ CD8+ T-cells and, partial reduction in the number
CC of lamina propria and intraepithelial CD8+ and CD4+ T-cells
CC (PubMed:24687959). {ECO:0000269|PubMed:16382161,
CC ECO:0000269|PubMed:16611999, ECO:0000269|PubMed:16612000,
CC ECO:0000269|PubMed:24687959}.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC67243.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF434663; AAL86736.1; -; mRNA.
DR EMBL; AF539424; AAN01614.1; -; mRNA.
DR EMBL; AB021964; BAA87914.1; -; mRNA.
DR EMBL; AB021965; BAA87915.1; -; mRNA.
DR EMBL; AB064265; BAB83501.2; -; mRNA.
DR EMBL; AY351388; AAQ02381.1; -; mRNA.
DR EMBL; AF061260; AAC67243.1; ALT_FRAME; mRNA.
DR EMBL; AB092414; BAC66173.1; -; mRNA.
DR EMBL; AB183399; BAD30018.1; -; mRNA.
DR EMBL; AB183400; BAD30019.1; -; mRNA.
DR EMBL; AB183401; BAD30020.1; -; mRNA.
DR EMBL; AB183402; BAD30021.1; -; mRNA.
DR CCDS; CCDS23147.1; -. [Q8R5M8-4]
DR CCDS; CCDS23148.1; -. [Q8R5M8-2]
DR CCDS; CCDS23149.1; -. [Q8R5M8-1]
DR CCDS; CCDS23150.1; -. [Q8R5M8-3]
DR RefSeq; NP_001020771.1; NM_001025600.1. [Q8R5M8-4]
DR RefSeq; NP_061240.3; NM_018770.3. [Q8R5M8-2]
DR RefSeq; NP_997558.2; NM_207675.2. [Q8R5M8-1]
DR RefSeq; NP_997559.1; NM_207676.2. [Q8R5M8-3]
DR AlphaFoldDB; Q8R5M8; -.
DR SMR; Q8R5M8; -.
DR BioGRID; 207729; 16.
DR IntAct; Q8R5M8; 3.
DR MINT; Q8R5M8; -.
DR STRING; 10090.ENSMUSP00000083073; -.
DR GlyConnect; 2199; 4 N-Linked glycans (1 site).
DR GlyGen; Q8R5M8; 6 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q8R5M8; -.
DR PhosphoSitePlus; Q8R5M8; -.
DR jPOST; Q8R5M8; -.
DR MaxQB; Q8R5M8; -.
DR PaxDb; Q8R5M8; -.
DR PeptideAtlas; Q8R5M8; -.
DR PRIDE; Q8R5M8; -.
DR ProteomicsDB; 281746; -. [Q8R5M8-1]
DR ProteomicsDB; 281747; -. [Q8R5M8-2]
DR ProteomicsDB; 281748; -. [Q8R5M8-3]
DR ProteomicsDB; 281749; -. [Q8R5M8-4]
DR ProteomicsDB; 281750; -. [Q8R5M8-5]
DR ProteomicsDB; 281751; -. [Q8R5M8-6]
DR ProteomicsDB; 281752; -. [Q8R5M8-7]
DR ABCD; Q8R5M8; 1 sequenced antibody.
DR Antibodypedia; 32257; 597 antibodies from 40 providers.
DR DNASU; 54725; -.
DR Ensembl; ENSMUST00000034581; ENSMUSP00000034581; ENSMUSG00000032076. [Q8R5M8-4]
DR Ensembl; ENSMUST00000085909; ENSMUSP00000083073; ENSMUSG00000032076. [Q8R5M8-1]
DR Ensembl; ENSMUST00000114547; ENSMUSP00000110194; ENSMUSG00000032076. [Q8R5M8-2]
DR Ensembl; ENSMUST00000114548; ENSMUSP00000110195; ENSMUSG00000032076. [Q8R5M8-3]
DR GeneID; 54725; -.
DR KEGG; mmu:54725; -.
DR UCSC; uc009phn.1; mouse. [Q8R5M8-5]
DR UCSC; uc009pho.1; mouse. [Q8R5M8-1]
DR UCSC; uc009phq.1; mouse. [Q8R5M8-3]
DR UCSC; uc009phr.1; mouse. [Q8R5M8-4]
DR UCSC; uc009phs.1; mouse. [Q8R5M8-2]
DR CTD; 23705; -.
DR MGI; MGI:1889272; Cadm1.
DR VEuPathDB; HostDB:ENSMUSG00000032076; -.
DR eggNOG; ENOG502R1KU; Eukaryota.
DR GeneTree; ENSGT00940000156093; -.
DR HOGENOM; CLU_047574_2_1_1; -.
DR InParanoid; Q8R5M8; -.
DR OMA; TYDRMYT; -.
DR PhylomeDB; Q8R5M8; -.
DR TreeFam; TF334317; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-420597; Nectin/Necl trans heterodimerization.
DR BioGRID-ORCS; 54725; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cadm1; mouse.
DR PRO; PR:Q8R5M8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R5M8; protein.
DR Bgee; ENSMUSG00000032076; Expressed in epithelium of lens and 275 other tissues.
DR ExpressionAtlas; Q8R5M8; baseline and differential.
DR Genevisible; Q8R5M8; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
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; IDA:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
DR GO; GO:0001889; P:liver development; ISO:MGI.
DR GO; GO:0097021; P:lymphocyte migration into lymphoid organs; IMP:UniProtKB.
DR GO; GO:0098880; P:maintenance of postsynaptic specialization structure; IDA:SynGO.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
DR GO; GO:0099054; P:presynapse assembly; IDA:SynGO.
DR GO; GO:0098942; P:retrograde trans-synaptic signaling by trans-synaptic protein complex; IDA:SynGO.
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:0007416; P:synapse assembly; IDA:MGI.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:MGI.
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 Alternative splicing; Apoptosis; Cell adhesion; Cell membrane;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Immunity; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Spermatogenesis; Synapse;
KW Transmembrane; Transmembrane helix; Tumor suppressor.
FT SIGNAL 1..47
FT /evidence="ECO:0000255"
FT CHAIN 48..456
FT /note="Cell adhesion molecule 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000291969"
FT TOPO_DOM 48..388
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..142
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255"
FT DOMAIN 147..241
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 246..332
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:20739279"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:20739279"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT DISULFID 67..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 169..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 270..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..150
FT /note="Missing (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:12799182, ECO:0000303|Ref.6,
FT ECO:0000303|Ref.7"
FT /id="VSP_052463"
FT VAR_SEQ 335..336
FT /note="DP -> GT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15893517, ECO:0000303|Ref.6,
FT ECO:0000303|Ref.7"
FT /id="VSP_052464"
FT VAR_SEQ 336..374
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12826663, ECO:0000303|Ref.7"
FT /id="VSP_052465"
FT VAR_SEQ 336..363
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12799182, ECO:0000303|Ref.7"
FT /id="VSP_052466"
FT VAR_SEQ 336..352
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:12799182, ECO:0000303|Ref.7"
FT /id="VSP_052467"
FT VAR_SEQ 337..456
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15893517, ECO:0000303|Ref.6,
FT ECO:0000303|Ref.7"
FT /id="VSP_052468"
FT VAR_SEQ 355..365
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:12799182, ECO:0000303|Ref.6"
FT /id="VSP_052469"
FT VAR_SEQ 364..374
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12202822,
FT ECO:0000303|PubMed:12242005, ECO:0000303|PubMed:15893517,
FT ECO:0000303|Ref.7"
FT /id="VSP_052470"
FT CONFLICT 8
FT /note="S -> C (in Ref. 2; AAN01614 and 7; BAD30018)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="F -> L (in Ref. 3; BAA87914/BAA87915)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="R -> P (in Ref. 3; BAA87914/BAA87915)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="M -> I (in Ref. 3; BAA87914/BAA87915)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="T -> S (in Ref. 2; AAN01614 and 7; BAD30018)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="D -> N (in Ref. 3; BAB83501)"
FT /evidence="ECO:0000305"
SQ 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
