CADM2_RAT
ID CADM2_RAT Reviewed; 435 AA.
AC Q1WIM2;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Cell adhesion molecule 2;
DE AltName: Full=Immunoglobulin superfamily member 4D;
DE Short=IgSF4D;
DE AltName: Full=Nectin-like protein 3;
DE Short=NECL-3;
DE AltName: Full=Synaptic cell adhesion molecule 2;
DE Short=SynCAM 2;
DE Flags: Precursor;
GN Name=Cadm2; Synonyms=Igsf4d, Necl3;
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 STRAIN=Sprague-Dawley;
RA Maurel P., Einheber S., Rubin M.B., Galinska J., Thaker P., Salzer J.L.;
RT "The nectin-like proteins: candidate cell adhesion molecules to mediate
RT axo-glial interactions.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 PROTEIN SEQUENCE OF 195-204 AND 231-273, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, 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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Adhesion molecule that engages in homo- and heterophilic
CC interactions with the other nectin-like family members, leading to cell
CC aggregation. Important for synapse organization, providing regulated
CC trans-synaptic adhesion. Preferentially binds to oligodendrocytes (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein. Synapse {ECO:0000250}. Cell projection, axon
CC {ECO:0000250}. Note=Found in the axoplasm of myelinated axons.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1WIM2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1WIM2-2; Sequence=VSP_026338;
CC -!- PTM: Glycosylation at Asn-51 reduces adhesive binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ272744; ABB85363.1; -; mRNA.
DR EMBL; AABR03079773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03081486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03078395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03080530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03080991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03078776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001040567.1; NM_001047102.1.
DR AlphaFoldDB; Q1WIM2; -.
DR SMR; Q1WIM2; -.
DR BioGRID; 262128; 1.
DR STRING; 10116.ENSRNOP00000040899; -.
DR GlyGen; Q1WIM2; 4 sites, 15 N-linked glycans (2 sites).
DR iPTMnet; Q1WIM2; -.
DR PhosphoSitePlus; Q1WIM2; -.
DR PaxDb; Q1WIM2; -.
DR PRIDE; Q1WIM2; -.
DR GeneID; 360687; -.
DR KEGG; rno:360687; -.
DR UCSC; RGD:1305678; rat. [Q1WIM2-1]
DR CTD; 253559; -.
DR RGD; 1305678; Cadm2.
DR eggNOG; ENOG502QV9X; Eukaryota.
DR InParanoid; Q1WIM2; -.
DR OrthoDB; 716894at2759; -.
DR PhylomeDB; Q1WIM2; -.
DR TreeFam; TF326804; -.
DR Reactome; R-RNO-418990; Adherens junctions interactions.
DR PRO; PR:Q1WIM2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
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; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..435
FT /note="Cell adhesion molecule 2"
FT /id="PRO_0000291972"
FT TOPO_DOM 25..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..119
FT /note="Ig-like V-type"
FT DOMAIN 127..219
FT /note="Ig-like C2-type 1"
FT DOMAIN 227..312
FT /note="Ig-like C2-type 2"
FT REGION 341..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 146..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 248..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 315..354
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_026338"
FT CONFLICT 20
FT /note="L -> Q (in Ref. 1; ABB85363)"
FT /evidence="ECO:0000305"
SQ 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
