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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