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   24-JAN-2024, entry version 151.
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); this interaction connects CADM1
CC       with DLG1 (By similarity). Interacts (via C-terminus) with PALS2 (via
CC       PDZ domain) (By similarity). {ECO:0000250|UniProtKB:Q8R5M8,
CC       ECO:0000250|UniProtKB:Q9BY67, 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   GlyCosmos; Q6AYP5; 6 sites, No reported glycans.
DR   GlyGen; Q6AYP5; 6 sites.
DR   iPTMnet; Q6AYP5; -.
DR   PhosphoSitePlus; Q6AYP5; -.
DR   jPOST; Q6AYP5; -.
DR   PaxDb; 10116-ENSRNOP00000041169; -.
DR   ABCD; Q6AYP5; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000110628.1; ENSRNOP00000081058.1; ENSRNOG00000018778.8. [Q6AYP5-1]
DR   Ensembl; ENSRNOT00055032434; ENSRNOP00055026255; ENSRNOG00055019005. [Q6AYP5-1]
DR   Ensembl; ENSRNOT00060024834; ENSRNOP00060019782; ENSRNOG00060014493. [Q6AYP5-1]
DR   Ensembl; ENSRNOT00065041150; ENSRNOP00065033600; ENSRNOG00065023910. [Q6AYP5-1]
DR   GeneID; 363058; -.
DR   KEGG; rno:363058; -.
DR   UCSC; RGD:1310999; rat. [Q6AYP5-1]
DR   AGR; RGD:1310999; -.
DR   CTD; 23705; -.
DR   RGD; 1310999; Cadm1.
DR   eggNOG; ENOG502R1KU; Eukaryota.
DR   GeneTree; ENSGT00940000156093; -.
DR   InParanoid; Q6AYP5; -.
DR   OMA; TYDRMYT; -.
DR   OrthoDB; 3039994at2759; -.
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; IDA:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
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: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:0120154; P:negative regulation of ERBB4 signaling pathway; IMP:RGD.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP: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   CDD; cd00096; Ig; 1.
DR   CDD; cd05883; IgI_2_Necl-2; 1.
DR   CDD; cd05881; IgV_1_Necl-2; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR45889:SF2; CELL ADHESION MOLECULE 1; 1.
DR   PANTHER; PTHR45889; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF13927; Ig_3; 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; Immunoglobulin; 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
//