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Cell adhesion molecule 1 (Synaptic cell adhesion molecule) (SynCAM) (Tumor suppressor in lung cancer 1 homolog) (TSLC-1)

 CADM1_RAT               Reviewed;         476 AA.
Q6AYP5; F7EYW4; Q0WXX6;
15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 1.
10-OCT-2018, entry version 127.
RecName: Full=Cell adhesion molecule 1 {ECO:0000305};
AltName: Full=Synaptic cell adhesion molecule {ECO:0000305};
Short=SynCAM {ECO:0000305};
AltName: Full=Tumor suppressor in lung cancer 1 homolog {ECO:0000303|PubMed:16814249};
Short=TSLC-1 {ECO:0000303|PubMed:16814249};
Flags: Precursor;
Name=Cadm1 {ECO:0000312|RGD:1310999};
Synonyms=SynCam1 {ECO:0000303|PubMed:27756895};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Liver;
PubMed=16814249; DOI=10.1016/j.bbrc.2006.06.101;
Shimizu K., Itsuzaki Y., Onishi M., Fujii H., Honoki K., Tsujiuchi T.;
"Reduced expression of the Tslc1 gene and its aberrant DNA methylation
in rat lung tumors.";
Biochem. Biophys. Res. Commun. 347:358-362(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[5]
INTERACTION WITH MPP2, AND SUBCELLULAR LOCATION.
PubMed=27756895; DOI=10.1038/srep35283;
Rademacher N., Schmerl B., Lardong J.A., Wahl M.C., Shoichet S.A.;
"MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1 cell
adhesion molecules to core components of the postsynaptic density.";
Sci. Rep. 6:35283-35283(2016).
-!- 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:0000250|UniProtKB:Q8R5M8}.
-!- 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:Q8R5M8,
ECO:0000269|PubMed:27756895}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q8R5M8}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q8R5M8}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q8R5M8}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000269|PubMed:27756895}.
Note=Localized to the basolateral plasma membrane of epithelial
cells in gall bladder. {ECO:0000250|UniProtKB:Q8R5M8}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6AYP5-1; Sequence=Displayed;
Name=2;
IsoId=Q6AYP5-2; Sequence=VSP_058825;
-!- 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:0000250|UniProtKB:Q8R5M8}.
-!- PTM: Glycosylation at Asn-70 and Asn-104 promotes adhesive binding
and synapse induction. {ECO:0000250|UniProtKB:Q8R5M8}.
-!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB257091; BAE97778.1; -; mRNA.
EMBL; AABR07070099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC078966; AAH78966.1; -; mRNA.
RefSeq; NP_001012201.1; NM_001012201.1. [Q6AYP5-1]
UniGene; Rn.19928; -.
ProteinModelPortal; Q6AYP5; -.
SMR; Q6AYP5; -.
STRING; 10116.ENSRNOP00000041169; -.
iPTMnet; Q6AYP5; -.
PhosphoSitePlus; Q6AYP5; -.
GeneID; 363058; -.
KEGG; rno:363058; -.
UCSC; RGD:1310999; rat. [Q6AYP5-1]
CTD; 23705; -.
RGD; 1310999; Cadm1.
eggNOG; ENOG410IH4H; Eukaryota.
eggNOG; ENOG41116SB; LUCA.
HOGENOM; HOG000036057; -.
HOVERGEN; HBG057086; -.
InParanoid; Q6AYP5; -.
KO; K06781; -.
OrthoDB; EOG091G0BHE; -.
PhylomeDB; Q6AYP5; -.
TreeFam; TF334317; -.
PRO; PR:Q6AYP5; -.
Proteomes; UP000002494; Unplaced.
Bgee; ENSRNOG00000018778; Expressed in 10 organ(s), highest expression level in lung.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0008037; P:cell recognition; ISS:UniProtKB.
GO; GO:0051606; P:detection of stimulus; ISS: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:0001889; P:liver development; IMP:RGD.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISS:UniProtKB.
GO; GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; ISS:UniProtKB.
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; Cell junction; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
Repeat; Signal; Synapse; Transmembrane; Transmembrane helix.
SIGNAL 1 47 {ECO:0000255}.
CHAIN 48 476 Cell adhesion molecule 1. {ECO:0000255}.
/FTId=PRO_5004270763.
TOPO_DOM 48 408 Extracellular.
{ECO:0000250|UniProtKB:Q8R5M8}.
TRANSMEM 409 429 Helical. {ECO:0000255}.
DOMAIN 48 142 Ig-like V-type. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 147 241 Ig-like C2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 246 332 Ig-like C2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
MOD_RES 456 456 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8R5M8}.
MOD_RES 468 468 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q8R5M8}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q8R5M8}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q8R5M8}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q8R5M8}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q8R5M8}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:Q8R5M8}.
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 335 476 DPPTTIPPPTTTTTTTTTTTTTTTILTIITDTTATTEPAVH
GLTQLPNSAEELDSEDLSDSRAGEEGAIGAVDHAVIGGVVA
VVVFAMLCLLIILGRYFARHKGTYFTHEAKGADDAADADTA
IINAEGGQNNSEEKKEYFI -> GT (in isoform 2).
/FTId=VSP_058825.
CONFLICT 4 4 P -> T (in Ref. 1; BAE97778).
{ECO:0000305}.
CONFLICT 150 150 L -> M (in Ref. 1; BAE97778).
{ECO:0000305}.
SEQUENCE 476 AA; 51854 MW; 486A43D37082C8FE CRC64;
MASPVLPSGS QCAAAAAVAA AAAPPGLRLR LLLLLLSAAA LIPTGDGQNL FTKDVTVIEG
EVATISCQVN KSDDSVIQLL NPNRQTIYFR DFRPLKDSRF QLLNFSSSEL KVSLTNVSIS
DEGRYFCQLY TDPPQESYTT ITVLVPPRNL MIDIQKDTAV EGEEIEVNCT AMASKPATTI
RWFKGNKELK GKSEVEEWSD MYTVTSQLML KVHKEDDGVP VICQVEHPAV TGNLQTQRYL
EVQYKPQVQI QMTYPLQGLT REGDAFELTC EATGKPQPVM VTWVRVDDEM PQHAVLSGPN
LFINNLNKTD NGTYRCEASN TVGKAHSDYM LYVYDPPTTI PPPTTTTTTT TTTTTTTTIL
TIITDTTATT EPAVHGLTQL PNSAEELDSE DLSDSRAGEE GAIGAVDHAV IGGVVAVVVF
AMLCLLIILG RYFARHKGTY FTHEAKGADD AADADTAIIN AEGGQNNSEE KKEYFI


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