GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

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-MAY-2022, entry version 160.
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 PALS2,
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]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19752223; DOI=10.4049/jimmunol.0901248;
Takeuchi A., Itoh Y., Takumi A., Ishihara C., Arase N., Yokosuka T.,
Koseki H., Yamasaki S., Takai Y., Miyoshi J., Ogasawara K., Saito T.;
"CRTAM confers late-stage activation of CD8+ T cells to regulate retention
within lymph node.";
J. Immunol. 183:4220-4228(2009).
[19]
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).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-104; ASN-116; ASN-168;
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).
[21]
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).
[22]
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).
[23]
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).
[24]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=24687959; DOI=10.1084/jem.20130904;
Cortez V.S., Cervantes-Barragan L., Song C., Gilfillan S., McDonald K.G.,
Tussiwand R., Edelson B.T., Murakami Y., Murphy K.M., Newberry R.D.,
Sibley L.D., Colonna M.;
"CRTAM controls residency of gut CD4+CD8+ T cells in the steady state and
maintenance of gut CD4+ Th17 during parasitic infection.";
J. Exp. Med. 211:623-633(2014).
-!- FUNCTION: Mediates homophilic cell-cell adhesion in a Ca(2+)-
independent manner (PubMed:12202822, PubMed:12799182, PubMed:12826663).
Also mediates heterophilic cell-cell adhesion with CADM3 and NECTIN3 in
a Ca(2+)-independent manner (PubMed:12826663). Interaction with CRTAM
promotes natural killer (NK) cell cytotoxicity and interferon-gamma
(IFN-gamma) secretion by CD8+ T-cells in vitro as well as NK cell-
mediated rejection of tumors expressing CADM1 in vivo
(PubMed:15811952). In mast cells, may mediate attachment to and promote
communication with nerves (By similarity). CADM1, together with MITF,
is essential for development and survival of mast cells in vivo
(PubMed:15158462, PubMed:16605125). By interacting with CRTAM and thus
promoting the adhesion between CD8+ T-cells and CD8+ dendritic cells,
regulates the retention of activated CD8+ T-cell within the draining
lymph node (PubMed:19752223). Required for the intestinal retention of
intraepithelial CD4+ CD8+ T-cells and, to a lesser extent,
intraepithelial and lamina propria CD8+ T-cells and CD4+ T-cells
(PubMed:24687959). Interaction with CRTAM promotes the adhesion to gut-
associated CD103+ dendritic cells, which may facilitate the expression
of gut-homing and adhesion molecules on T-cells and the conversion of
CD4+ T-cells into CD4+ CD8+ T-cells (PubMed:24687959). Acts as a
synaptic cell adhesion molecule and plays a role in the formation of
dendritic spines and in synapse assembly (PubMed:12202822,
PubMed:23209303). May be involved in neuronal migration, axon growth,
pathfinding, and fasciculation on the axons of differentiating neurons
(PubMed:15707673). 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
(PubMed:12606335, PubMed:16612000). {ECO:0000250|UniProtKB:Q9BY67,
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:19752223,
ECO:0000269|PubMed:23209303, ECO:0000269|PubMed:24687959}.
-!- SUBUNIT: Homodimer (via Ig-like V-type domain) (By similarity).
Interacts with FARP1 (PubMed:23209303). Interacts (via Ig-like V-type
domain) with CRTAM (via Ig-like V-type domain); the interaction
competes with CRTAM homodimerization and CADM1 homodimerization
(PubMed:15811952, PubMed:15781451). Interacts (via C-terminus) with
EPB41L3/DAL1 (By similarity). The interaction with EPB41L3/DAL1 may act
to anchor CADM1 to the actin cytoskeleton (By similarity). Interacts
(via C-terminus) with MPP2 (via PDZ domain) (By similarity). Interacts
(via C-terminus) with MPP3 (via PDZ domain) (By similarity). Interacts
(via C-terminus) with PALS2 (via PDZ domain) (PubMed:12826663).
{ECO:0000250|UniProtKB:Q6AYP5, ECO:0000250|UniProtKB:Q9BY67,
ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:15781451,
ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:23209303}.
-!- INTERACTION:
Q8R5M8-2; P16144: ITGB4; Xeno; NbExp=3; IntAct=EBI-5651941, EBI-948678;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12826663,
ECO:0000269|PubMed:19752223, ECO:0000269|PubMed:20739279,
ECO:0000269|PubMed:24687959}; Single-pass type I membrane protein
{ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:20739279}. Cell
junction, synapse, synaptic cell membrane {ECO:0000269|PubMed:20739279,
ECO:0000269|PubMed:23209303}; Single-pass type I membrane protein
{ECO:0000305}. 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 dominantly in epithelial cells but not
expressed in fibroblast cells (at protein level) (PubMed:12826663).
Expressed in the T-cell area of lymph nodes, specifically in CD8+ and
CD4- CD8- dendritic cells (at protein level) (PubMed:19752223).
Expressed in CD8+ dendritic cells in the spleen (at protein level)
(PubMed:19752223). Expressed in CD103+ dendritic cells in the small
intestine lamina propria and mesenteric lymph nodes (at protein level)
(PubMed:24687959). Expressed in brain, lung, kidney, testis, heart,
spleen and liver, but not expressed in skeletal muscle
(PubMed:12242005, PubMed:12606335, PubMed:12202822).
{ECO:0000269|PubMed:12202822, ECO:0000269|PubMed:12242005,
ECO:0000269|PubMed:12606335, ECO:0000269|PubMed:12826663,
ECO:0000269|PubMed:19752223, ECO:0000269|PubMed:24687959}.
-!- 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 (PubMed:16382161, PubMed:16611999, PubMed:16612000).
Heterozygous males and females and homozygous null females are fertile
and have no overt developmental defects (PubMed:16382161,
PubMed:16611999, PubMed:16612000). In the small intestine mucosa and
under steady-state conditions, severe reduction in the number of
intraepithelial CD4+ CD8+ T-cells and, partial reduction in the number
of lamina propria and intraepithelial CD8+ and CD4+ T-cells
(PubMed:24687959). {ECO:0000269|PubMed:16382161,
ECO:0000269|PubMed:16611999, ECO:0000269|PubMed:16612000,
ECO:0000269|PubMed:24687959}.
-!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC67243.1; Type=Frameshift; Evidence={ECO:0000305};
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
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]
AlphaFoldDB; Q8R5M8; -.
SMR; Q8R5M8; -.
BioGRID; 207729; 16.
IntAct; Q8R5M8; 3.
MINT; Q8R5M8; -.
STRING; 10090.ENSMUSP00000083073; -.
GlyConnect; 2199; 4 N-Linked glycans (1 site).
GlyGen; Q8R5M8; 6 sites, 4 N-linked glycans (1 site).
iPTMnet; Q8R5M8; -.
PhosphoSitePlus; Q8R5M8; -.
jPOST; Q8R5M8; -.
MaxQB; Q8R5M8; -.
PaxDb; Q8R5M8; -.
PeptideAtlas; Q8R5M8; -.
PRIDE; Q8R5M8; -.
ProteomicsDB; 281746; -. [Q8R5M8-1]
ProteomicsDB; 281747; -. [Q8R5M8-2]
ProteomicsDB; 281748; -. [Q8R5M8-3]
ProteomicsDB; 281749; -. [Q8R5M8-4]
ProteomicsDB; 281750; -. [Q8R5M8-5]
ProteomicsDB; 281751; -. [Q8R5M8-6]
ProteomicsDB; 281752; -. [Q8R5M8-7]
ABCD; Q8R5M8; 1 sequenced antibody.
Antibodypedia; 32257; 661 antibodies from 40 providers.
DNASU; 54725; -.
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.
VEuPathDB; HostDB:ENSMUSG00000032076; -.
eggNOG; ENOG502R1KU; Eukaryota.
GeneTree; ENSGT00940000156093; -.
HOGENOM; CLU_047574_2_1_1; -.
InParanoid; Q8R5M8; -.
OMA; TYDRMYT; -.
PhylomeDB; Q8R5M8; -.
TreeFam; TF334317; -.
Reactome; R-MMU-418990; Adherens junctions interactions.
Reactome; R-MMU-420597; Nectin/Necl trans heterodimerization.
BioGRID-ORCS; 54725; 2 hits in 74 CRISPR screens.
ChiTaRS; Cadm1; mouse.
PRO; PR:Q8R5M8; -.
Proteomes; UP000000589; Chromosome 9.
RNAct; Q8R5M8; protein.
Bgee; ENSMUSG00000032076; Expressed in retina and 326 other tissues.
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:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:MGI.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISO:MGI.
GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0005102; F:signaling 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:0001889; P:liver development; ISO:MGI.
GO; GO:0097021; P:lymphocyte migration into lymphoid organs; IMP:UniProtKB.
GO; GO:0098880; P:maintenance of postsynaptic specialization structure; IDA:SynGO.
GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:0099054; P:presynapse assembly; IDA:SynGO.
GO; GO:0098942; P:retrograde trans-synaptic signaling by trans-synaptic protein complex; IDA:SynGO.
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:0099560; P:synaptic membrane adhesion; IDA:SynGO.
GO; GO:0009826; P:unidimensional cell growth; IMP:MGI.
Gene3D; 2.60.40.10; -; 3.
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; 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
/evidence="ECO:0000255"
CHAIN 48..456
/note="Cell adhesion molecule 1"
/evidence="ECO:0000255"
/id="PRO_0000291969"
TOPO_DOM 48..388
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 389..409
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 410..456
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 48..142
/note="Ig-like V-type"
/evidence="ECO:0000255"
DOMAIN 147..241
/note="Ig-like C2-type 1"
/evidence="ECO:0000255"
DOMAIN 246..332
/note="Ig-like C2-type 2"
/evidence="ECO:0000255"
MOD_RES 436
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 448
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:19144319"
CARBOHYD 70
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:20739279"
CARBOHYD 104
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:20739279"
CARBOHYD 116
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770"
CARBOHYD 168
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973"
CARBOHYD 307
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973"
CARBOHYD 311
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973"
DISULFID 67..127
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 169..223
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 270..316
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
VAR_SEQ 1..150
/note="Missing (in isoform 6 and isoform 7)"
/evidence="ECO:0000303|PubMed:12799182, ECO:0000303|Ref.6,
ECO:0000303|Ref.7"
/id="VSP_052463"
VAR_SEQ 335..336
/note="DP -> GT (in isoform 5)"
/evidence="ECO:0000303|PubMed:15893517, ECO:0000303|Ref.6,
ECO:0000303|Ref.7"
/id="VSP_052464"
VAR_SEQ 336..374
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:12826663, ECO:0000303|Ref.7"
/id="VSP_052465"
VAR_SEQ 336..363
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:12799182, ECO:0000303|Ref.7"
/id="VSP_052466"
VAR_SEQ 336..352
/note="Missing (in isoform 7)"
/evidence="ECO:0000303|PubMed:12799182, ECO:0000303|Ref.7"
/id="VSP_052467"
VAR_SEQ 337..456
/note="Missing (in isoform 5)"
/evidence="ECO:0000303|PubMed:15893517, ECO:0000303|Ref.6,
ECO:0000303|Ref.7"
/id="VSP_052468"
VAR_SEQ 355..365
/note="Missing (in isoform 6)"
/evidence="ECO:0000303|PubMed:12799182, ECO:0000303|Ref.6"
/id="VSP_052469"
VAR_SEQ 364..374
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:12202822,
ECO:0000303|PubMed:12242005, ECO:0000303|PubMed:15893517,
ECO:0000303|Ref.7"
/id="VSP_052470"
CONFLICT 8
/note="S -> C (in Ref. 2; AAN01614 and 7; BAD30018)"
/evidence="ECO:0000305"
CONFLICT 266
/note="F -> L (in Ref. 3; BAA87914/BAA87915)"
/evidence="ECO:0000305"
CONFLICT 315
/note="R -> P (in Ref. 3; BAA87914/BAA87915)"
/evidence="ECO:0000305"
CONFLICT 330
/note="M -> I (in Ref. 3; BAA87914/BAA87915)"
/evidence="ECO:0000305"
CONFLICT 356
/note="T -> S (in Ref. 2; AAN01614 and 7; BAD30018)"
/evidence="ECO:0000305"
CONFLICT 429
/note="D -> N (in Ref. 3; BAB83501)"
/evidence="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


Related products :

Catalog number Product name Quantity
EIAAB05121 Cadm1,Cell adhesion molecule 1,IgSF4,Igsf4,Immunoglobulin superfamily member 4,Mouse,Mus musculus,Necl2,NECL-2,Nectin-like protein 2,Ra175,SgIgSF,Spermatogenic immunoglobulin superfamily,Synaptic cell
EIAAB05120 CADM1,Cell adhesion molecule 1,Homo sapiens,Human,IgSF4,IGSF4,IGSF4A,Immunoglobulin superfamily member 4,NECL2,NECL-2,Nectin-like protein 2,SgIgSF,Spermatogenic immunoglobulin superfamily,Synaptic cel
EIAAB05126 Brain immunoglobulin receptor,CADM3,Cell adhesion molecule 3,Homo sapiens,Human,IgSF4B,IGSF4B,Immunoglobulin superfamily member 4B,NECL1,NECL-1,Nectin-like protein 1,Synaptic cell adhesion molecule 3,
EIAAB05125 Cadm3,Cell adhesion molecule 3,IgSF4B,Igsf4b,Immunoglobulin superfamily member 4B,Mouse,Mus musculus,Necl1,NECL-1,Nectin-like protein 1,Synaptic cell adhesion molecule 3,Syncam3,TSLC1-like protein 1,T
EIAAB05123 Cadm2,Cell adhesion molecule 2,IgSF4D,Igsf4d,Immunoglobulin superfamily member 4D,Necl3,NECL-3,Nectin-like protein 3,Rat,Rattus norvegicus
EIAAB05124 Cadm2,Cell adhesion molecule 2,IgSF4D,Igsf4d,Immunoglobulin superfamily member 4D,Mouse,Mus musculus,Necl3,NECL-3,Nectin-like protein 3
EIAAB05127 Cadm3,Cell adhesion molecule 3,IgSF4B,Igsf4b,Immunoglobulin superfamily member 4B,Necl1,NECL-1,Nectin-like protein 1,Rat,Rattus norvegicus
EIAAB05128 Cadm4,Cell adhesion molecule 4,IgSF4C,Igsf4c,Immunoglobulin superfamily member 4C,Necl4,NECL-4,Nectin-like protein 4,Rat,Rattus norvegicus
EIAAB05122 CADM2,Cell adhesion molecule 2,Homo sapiens,Human,IgSF4D,IGSF4D,Immunoglobulin superfamily member 4D,NECL3,NECL-3,Nectin-like protein 3
EIAAB05129 Cadm4,Cell adhesion molecule 4,IgSF4C,Igsf4c,Immunoglobulin superfamily member 4C,Mouse,Mus musculus,Necl4,NECL-4,Nectin-like protein 4,TSLC1-like protein 2,Tsll2
EIAAB05130 CADM4,Cell adhesion molecule 4,Homo sapiens,Human,IgSF4C,IGSF4C,Immunoglobulin superfamily member 4C,NECL4,NECL-4,Nectin-like protein 4,TSLC1-like protein 2,TSLL2
31-360 Cell adhesion molecules (CAMs) are members of the immunoglobulin superfamily. NRCAM is a neuronal cell adhesion molecule with multiple immunoglobulin-like C2-type domains and fibronectin type-III doma 0.05 mg
31-361 Cell adhesion molecules (CAMs) are members of the immunoglobulin superfamily. NRCAM is a neuronal cell adhesion molecule with multiple immunoglobulin-like C2-type domains and fibronectin type-III doma 0.1 mg
32-131 CD31, also known as platelet endothelial cell adhesion molecule 1 (PECAM1), is a type I integral membrane glycoprotein and a member of the immunoglobulin superfamily of cell surface receptors.It is co 0.1 mL
25-998 IGSF11 functions as a cell adhesion molecule through homophilic interaction. IGSF11 stimulates cell growth.IGSF11 is an immunoglobulin (Ig) superfamily member that is preferentially expressed in brain 0.05 mg
EIAAB10579 Colorectal cancer suppressor,DCC,Homo sapiens,Human,IGDCC1,Immunoglobulin superfamily DCC subclass member 1,Netrin receptor DCC,Tumor suppressor protein DCC
EIAAB27851 Ankyrin-binding cell adhesion molecule NrCAM,Neuronal cell adhesion molecule,Neuronal surface protein Bravo,Ng-CAM-related,NgCAM-related cell adhesion molecule,Nrcam,Nr-CAM,Rat,Rattus norvegicus,rBrav
EIAAB11953 Down syndrome cell adhesion molecule 2,Down syndrome cell adhesion molecule-like protein 1,DSCAM2,DSCAML1,Homo sapiens,Human,KIAA1132
EIAAB07193 Call,Cell adhesion molecule with homology to L1CAM,Chl1,Chl1-like protein,Close homolog of L1,Mouse,Mus musculus,Neural cell adhesion molecule L1-like protein
E0086r ELISA kit CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,Lnhr,L-selectin,Ly-22,Ly-22,Lymph node homing receptor,Lymphocyte 96T
EIAAB27849 hBravo,Homo sapiens,Human,KIAA0343,Neuronal cell adhesion molecule,Neuronal surface protein Bravo,Ng-CAM-related,NgCAM-related cell adhesion molecule,NRCAM,Nr-CAM
E0086b ELISA Bos taurus,Bovine,CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,L-selectin,Lymph node homing receptor,SELL 96T
E0086m ELISA CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,Lnhr,L-selectin,Ly22,Ly-22,Ly-22,Lymph node homing receptor,Lymphocyte 96T
E0086r ELISA CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,Lnhr,L-selectin,Ly-22,Ly-22,Lymph node homing receptor,Lymphocyte anti 96T
E0086b ELISA kit Bos taurus,Bovine,CD62 antigen-like family member L,LAM-1,LECAM1,Leukocyte adhesion molecule 1,Leukocyte-endothelial cell adhesion molecule 1,L-selectin,Lymph node homing receptor,SELL 96T