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Cell adhesion molecule 2 (Immunoglobulin superfamily member 4D) (IgSF4D) (Nectin-like protein 3) (NECL-3) (Synaptic cell adhesion molecule 2) (SynCAM 2)

 CADM2_RAT               Reviewed;         435 AA.
Q1WIM2;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 2.
25-MAY-2022, entry version 99.
RecName: Full=Cell adhesion molecule 2;
AltName: Full=Immunoglobulin superfamily member 4D;
Short=IgSF4D;
AltName: Full=Nectin-like protein 3;
Short=NECL-3;
AltName: Full=Synaptic cell adhesion molecule 2;
Short=SynCAM 2;
Flags: Precursor;
Name=Cadm2; Synonyms=Igsf4d, Necl3;
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).
STRAIN=Sprague-Dawley;
Maurel P., Einheber S., Rubin M.B., Galinska J., Thaker P., Salzer J.L.;
"The nectin-like proteins: candidate cell adhesion molecules to mediate
axo-glial interactions.";
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[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]
PROTEIN SEQUENCE OF 195-204 AND 231-273, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, 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]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24090084; DOI=10.1021/pr400783j;
Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
Graham M.E., Packer N.H., Cordwell S.J.;
"Site-specific glycan-peptide analysis for determination of N-glycoproteome
heterogeneity.";
J. Proteome Res. 12:5791-5800(2013).
-!- FUNCTION: Adhesion molecule that engages in homo- and heterophilic
interactions with the other nectin-like family members, leading to cell
aggregation. Important for synapse organization, providing regulated
trans-synaptic adhesion. Preferentially binds to oligodendrocytes (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
membrane protein. Cell junction, synapse {ECO:0000250}. Cell
projection, axon {ECO:0000250}. Note=Found in the axoplasm of
myelinated axons. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q1WIM2-1; Sequence=Displayed;
Name=2;
IsoId=Q1WIM2-2; Sequence=VSP_026338;
-!- PTM: Glycosylation at Asn-51 reduces adhesive binding. {ECO:0000250}.
-!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
---------------------------------------------------------------------------
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EMBL; DQ272744; ABB85363.1; -; mRNA.
EMBL; AABR03079773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03081486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03078395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03080530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03080991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03078776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001040567.1; NM_001047102.1.
AlphaFoldDB; Q1WIM2; -.
SMR; Q1WIM2; -.
BioGRID; 262128; 1.
STRING; 10116.ENSRNOP00000040899; -.
GlyGen; Q1WIM2; 4 sites, 15 N-linked glycans (2 sites).
iPTMnet; Q1WIM2; -.
PhosphoSitePlus; Q1WIM2; -.
PaxDb; Q1WIM2; -.
GeneID; 360687; -.
KEGG; rno:360687; -.
UCSC; RGD:1305678; rat. [Q1WIM2-1]
CTD; 253559; -.
RGD; 1305678; Cadm2.
eggNOG; ENOG502QV9X; Eukaryota.
InParanoid; Q1WIM2; -.
OrthoDB; 716894at2759; -.
PhylomeDB; Q1WIM2; -.
TreeFam; TF326804; -.
Reactome; R-RNO-418990; Adherens junctions interactions.
PRO; PR:Q1WIM2; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD.
GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; 2.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
Cell projection; Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
Repeat; Signal; Synapse; Transmembrane; Transmembrane helix.
SIGNAL 1..24
/evidence="ECO:0000255"
CHAIN 25..435
/note="Cell adhesion molecule 2"
/id="PRO_0000291972"
TOPO_DOM 25..367
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 368..388
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 389..435
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 27..119
/note="Ig-like V-type"
DOMAIN 127..219
/note="Ig-like C2-type 1"
DOMAIN 227..312
/note="Ig-like C2-type 2"
REGION 341..360
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 341..359
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 423
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
CARBOHYD 31
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 51
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0007744|PubMed:24090084"
CARBOHYD 291
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 44..104
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 146..203
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 248..296
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
VAR_SEQ 315..354
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|Ref.1"
/id="VSP_026338"
CONFLICT 20
/note="L -> Q (in Ref. 1; ABB85363)"
/evidence="ECO:0000305"
SEQUENCE 435 AA; 47528 MW; 43EF8BA865C8CE45 CRC64;
MIWKRSAVLR FYSVCGLLLL GSQGQFPLTQ NVTVVEGGTA ILTCRVDQND NTSLQWSNPA
QQTLYFDDKK ALRDNRIELV RASWHELSIS VSDVSLSDEG QYTCSLFTMP VKTSKAYLTV
LGVPEKPQIS GFSSPVMEGD LMQLTCKTSG SKPAADIRWF KNDKEIKDVK YLKEEDANRK
TFTVSSTLDF RVDRSDDGVA VICRVDHESL NATPQVAMQV LEIHYTPSVK IIPSTPFPQE
GQALTLTCES KGKPLPEPVL WTKDGAELPD PDRMVVSGRE LNILFLNKTD NGTYRCEATN
TIGQSSAEYV LIVHDVPNTL LPTTIIPSLT TAPVTTTVAI TTSPSTSASS SSRRDPNSLA
GQNGPDHALI GGIVAVVVFV TLCSIFLLGR YLARHKGTYL TNEAKGAEDA PDADTAIINA
EGSQVNAEEK KEYFI


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