CADM1_RAT
ID CADM1_RAT Reviewed; 476 AA.
AC Q6AYP5; F7EYW4; Q0WXX6;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cell adhesion molecule 1 {ECO:0000305};
DE AltName: Full=Synaptic cell adhesion molecule {ECO:0000305};
DE Short=SynCAM {ECO:0000305};
DE AltName: Full=Tumor suppressor in lung cancer 1 homolog {ECO:0000303|PubMed:16814249};
DE Short=TSLC-1 {ECO:0000303|PubMed:16814249};
DE Flags: Precursor;
GN Name=Cadm1 {ECO:0000312|RGD:1310999};
GN Synonyms=SynCam1 {ECO:0000303|PubMed:27756895};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=16814249; DOI=10.1016/j.bbrc.2006.06.101;
RA Shimizu K., Itsuzaki Y., Onishi M., Fujii H., Honoki K., Tsujiuchi T.;
RT "Reduced expression of the Tslc1 gene and its aberrant DNA methylation in
RT rat lung tumors.";
RL Biochem. Biophys. Res. Commun. 347:358-362(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP INTERACTION WITH MPP2, AND SUBCELLULAR LOCATION.
RX PubMed=27756895; DOI=10.1038/srep35283;
RA Rademacher N., Schmerl B., Lardong J.A., Wahl M.C., Shoichet S.A.;
RT "MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1 cell
RT adhesion molecules to core components of the postsynaptic density.";
RL Sci. Rep. 6:35283-35283(2016).
CC -!- FUNCTION: Mediates homophilic cell-cell adhesion in a Ca(2+)-
CC independent manner. Also mediates heterophilic cell-cell adhesion with
CC CADM3 and NECTIN3 in a Ca(2+)-independent manner. Interaction with
CC CRTAM promotes natural killer (NK) cell cytotoxicity and interferon-
CC gamma (IFN-gamma) secretion by CD8+ T-cells in vitro as well as NK
CC cell-mediated rejection of tumors expressing CADM1 in vivo (By
CC similarity). 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. By
CC interacting with CRTAM and thus promoting the adhesion between CD8+ T-
CC cells and CD8+ dendritic cells, regulates the retention of activated
CC CD8+ T-cell within the draining lymph node. Required for the intestinal
CC retention of intraepithelial CD4+ CD8+ T-cells and, to a lesser extent,
CC intraepithelial and lamina propria CD8+ T-cells and CD4+ T-cells.
CC Interaction with CRTAM promotes the adhesion to gut-associated CD103+
CC dendritic cells, which may facilitate the expression of gut-homing and
CC adhesion molecules on T-cells and the conversion of CD4+ T-cells into
CC CD4+ CD8+ T-cells. Acts as a synaptic cell adhesion molecule and plays
CC a role in the formation of dendritic spines and in synapse assembly.
CC May be involved in neuronal migration, axon growth, pathfinding, and
CC fasciculation on the axons of differentiating neurons. May play diverse
CC roles in the spermatogenesis including in the adhesion of spermatocytes
CC and spermatids to Sertoli cells and for their normal differentiation
CC into mature spermatozoa (By similarity). {ECO:0000250|UniProtKB:Q8R5M8,
CC ECO:0000250|UniProtKB:Q9BY67}.
CC -!- SUBUNIT: Homodimer (via Ig-like V-type domain) (By similarity).
CC Interacts with FARP1 (By similarity). 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 (By
CC similarity). Interacts (via C-terminus) with EPB41L3/DAL1 (By
CC similarity). The interaction with EPB41L3/DAL1 may act to anchor CADM1
CC to the actin cytoskeleton (By similarity). Interacts (via C-terminus)
CC with MPP2 (via PDZ domain) (PubMed:27756895). Interacts (via C-
CC terminus) with MPP3 (via PDZ domain) (By similarity). Interacts (via C-
CC terminus) with PALS2 (via PDZ domain) (By similarity).
CC {ECO:0000250|UniProtKB:Q8R5M8, ECO:0000250|UniProtKB:Q9BY67,
CC ECO:0000269|PubMed:27756895}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8R5M8};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8R5M8}.
CC Synapse {ECO:0000250|UniProtKB:Q8R5M8}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:27756895}. Note=Localized to the basolateral plasma
CC membrane of epithelial cells in gall bladder.
CC {ECO:0000250|UniProtKB:Q8R5M8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6AYP5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6AYP5-2; Sequence=VSP_058825;
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:0000250|UniProtKB:Q8R5M8}.
CC -!- PTM: Glycosylation at Asn-70 and Asn-104 promotes adhesive binding and
CC synapse induction. {ECO:0000250|UniProtKB:Q8R5M8}.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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DR EMBL; AB257091; BAE97778.1; -; mRNA.
DR EMBL; AABR07070099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC078966; AAH78966.1; -; mRNA.
DR RefSeq; NP_001012201.1; NM_001012201.1. [Q6AYP5-1]
DR AlphaFoldDB; Q6AYP5; -.
DR SMR; Q6AYP5; -.
DR STRING; 10116.ENSRNOP00000041169; -.
DR GlyGen; Q6AYP5; 6 sites.
DR iPTMnet; Q6AYP5; -.
DR PhosphoSitePlus; Q6AYP5; -.
DR jPOST; Q6AYP5; -.
DR PRIDE; Q6AYP5; -.
DR ABCD; Q6AYP5; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000110628; ENSRNOP00000081058; ENSRNOG00000018778. [Q6AYP5-1]
DR GeneID; 363058; -.
DR KEGG; rno:363058; -.
DR UCSC; RGD:1310999; rat. [Q6AYP5-1]
DR CTD; 23705; -.
DR RGD; 1310999; Cadm1.
DR eggNOG; ENOG502R1KU; Eukaryota.
DR GeneTree; ENSGT00940000156093; -.
DR InParanoid; Q6AYP5; -.
DR OrthoDB; 716894at2759; -.
DR PhylomeDB; Q6AYP5; -.
DR TreeFam; TF334317; -.
DR Reactome; R-RNO-418990; Adherens junctions interactions.
DR Reactome; R-RNO-420597; Nectin/Necl trans heterodimerization.
DR PRO; PR:Q6AYP5; -.
DR Proteomes; UP000002494; Chromosome 8.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:HGNC.
DR GO; GO:0070852; C:cell body fiber; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISS:HGNC.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
DR GO; GO:0030165; F:PDZ domain binding; ISS:HGNC.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC.
DR GO; GO:0005102; F:signaling receptor binding; ISS:HGNC.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0008037; P:cell recognition; ISS:HGNC.
DR GO; GO:0051606; P:detection of stimulus; ISS:HGNC.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:HGNC.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:HGNC.
DR GO; GO:0001889; P:liver development; IMP:RGD.
DR GO; GO:0097021; P:lymphocyte migration into lymphoid organs; ISO:RGD.
DR GO; GO:0098880; P:maintenance of postsynaptic specialization structure; ISO:RGD.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISS:HGNC.
DR GO; GO:0099054; P:presynapse assembly; ISO:RGD.
DR GO; GO:0098942; P:retrograde trans-synaptic signaling by trans-synaptic protein complex; ISO:RGD.
DR GO; GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; ISS:HGNC.
DR GO; GO:0007416; P:synapse assembly; ISO:RGD.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:RGD.
DR GO; GO:0009826; P:unidimensional cell growth; ISO:RGD.
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; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..47
FT /evidence="ECO:0000255"
FT CHAIN 48..476
FT /note="Cell adhesion molecule 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004270763"
FT TOPO_DOM 48..408
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8R5M8"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 48..142
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 147..241
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 246..332
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MOD_RES 456
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5M8"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5M8"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5M8"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5M8"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5M8"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5M8"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5M8"
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 335..476
FT /note="DPPTTIPPPTTTTTTTTTTTTTTTILTIITDTTATTEPAVHGLTQLPNSAEE
FT LDSEDLSDSRAGEEGAIGAVDHAVIGGVVAVVVFAMLCLLIILGRYFARHKGTYFTHEA
FT KGADDAADADTAIINAEGGQNNSEEKKEYFI -> GT (in isoform 2)"
FT /id="VSP_058825"
FT CONFLICT 4
FT /note="P -> T (in Ref. 1; BAE97778)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="L -> M (in Ref. 1; BAE97778)"
FT /evidence="ECO:0000305"
SQ 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
