CADM2_HUMAN
ID CADM2_HUMAN Reviewed; 435 AA.
AC Q8N3J6; G3XHN7; G3XHN8; Q3KQY9; Q658Q7; Q8IZP8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 156.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6), AND ALTERNATIVE SPLICING.
RX PubMed=21864505; DOI=10.1016/j.bbrc.2011.08.013;
RA Hiruma A., Ikeda I., Terui T., Ozawa M., Hashimoto T., Yasumoto S.,
RA Nakayama J., Kubota Y., Iijima M., Sueki H., Matsumoto Y., Kato M.,
RA Akasaka E., Ikoma N., Mabuchi T., Tamiya S., Matsuyama T., Ozawa A.,
RA Inoko H., Oka A.;
RT "A novel splicing variant of CADM2 as a protective transcript of
RT psoriasis.";
RL Biochem. Biophys. Res. Commun. 412:626-632(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Gingrich J.R., D'Angelo A., Chang G.M., Greenberg N.M.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 105-435 (ISOFORM 2).
RC TISSUE=Amygdala, and Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17967169; DOI=10.1186/1471-2202-8-90;
RA Pellissier F., Gerber A., Bauer C., Ballivet M., Ossipow V.;
RT "The adhesion molecule Necl-3/SynCAM-2 localizes to myelinated axons, binds
RT to oligodendrocytes and promotes cell adhesion.";
RL BMC Neurosci. 8:90-90(2007).
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.
CC {ECO:0000269|PubMed:17967169}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17967169};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:17967169}.
CC Synapse {ECO:0000269|PubMed:17967169}. Cell projection, axon
CC {ECO:0000269|PubMed:17967169}. Note=Found in the axoplasm of myelinated
CC axons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8N3J6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N3J6-2; Sequence=VSP_026334, VSP_026335;
CC Name=3;
CC IsoId=Q8N3J6-3; Sequence=VSP_026333;
CC Name=5; Synonyms=7;
CC IsoId=Q8N3J6-4; Sequence=VSP_055355, VSP_055356;
CC Name=6; Synonyms=8;
CC IsoId=Q8N3J6-5; Sequence=VSP_055355;
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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DR EMBL; AB646740; BAK93303.1; -; mRNA.
DR EMBL; AB646741; BAK93304.1; -; mRNA.
DR EMBL; AB646742; BAK93305.1; -; mRNA.
DR EMBL; AB646743; BAK93306.1; -; mRNA.
DR EMBL; AF538973; AAN16368.1; -; mRNA.
DR EMBL; AL833049; CAH56314.1; -; mRNA.
DR EMBL; AL834270; CAD38945.1; -; mRNA.
DR EMBL; BC105999; AAI06000.1; -; mRNA.
DR CCDS; CCDS33792.1; -. [Q8N3J6-3]
DR CCDS; CCDS54613.1; -. [Q8N3J6-2]
DR CCDS; CCDS54614.1; -. [Q8N3J6-1]
DR RefSeq; NP_001161146.1; NM_001167674.1. [Q8N3J6-1]
DR RefSeq; NP_001161147.1; NM_001167675.1. [Q8N3J6-2]
DR RefSeq; NP_001243431.1; NM_001256502.1. [Q8N3J6-5]
DR RefSeq; NP_001243432.1; NM_001256503.1. [Q8N3J6-5]
DR RefSeq; NP_001243433.1; NM_001256504.1. [Q8N3J6-4]
DR RefSeq; NP_001243434.1; NM_001256505.1. [Q8N3J6-4]
DR RefSeq; NP_694854.2; NM_153184.3. [Q8N3J6-3]
DR RefSeq; XP_006713144.1; XM_006713081.3.
DR AlphaFoldDB; Q8N3J6; -.
DR SMR; Q8N3J6; -.
DR BioGRID; 128973; 4.
DR IntAct; Q8N3J6; 1.
DR STRING; 9606.ENSP00000384193; -.
DR GlyGen; Q8N3J6; 3 sites.
DR iPTMnet; Q8N3J6; -.
DR PhosphoSitePlus; Q8N3J6; -.
DR BioMuta; CADM2; -.
DR DMDM; 74759850; -.
DR EPD; Q8N3J6; -.
DR jPOST; Q8N3J6; -.
DR MassIVE; Q8N3J6; -.
DR PaxDb; Q8N3J6; -.
DR PeptideAtlas; Q8N3J6; -.
DR PRIDE; Q8N3J6; -.
DR ProteomicsDB; 71814; -. [Q8N3J6-1]
DR ProteomicsDB; 71815; -. [Q8N3J6-2]
DR ProteomicsDB; 71816; -. [Q8N3J6-3]
DR TopDownProteomics; Q8N3J6-3; -. [Q8N3J6-3]
DR Antibodypedia; 2209; 213 antibodies from 26 providers.
DR DNASU; 253559; -.
DR Ensembl; ENST00000383699.8; ENSP00000373200.3; ENSG00000175161.14. [Q8N3J6-2]
DR Ensembl; ENST00000405615.2; ENSP00000384193.2; ENSG00000175161.14. [Q8N3J6-3]
DR Ensembl; ENST00000407528.6; ENSP00000384575.2; ENSG00000175161.14. [Q8N3J6-1]
DR GeneID; 253559; -.
DR KEGG; hsa:253559; -.
DR MANE-Select; ENST00000383699.8; ENSP00000373200.3; NM_001167675.2; NP_001161147.1. [Q8N3J6-2]
DR UCSC; uc003dqj.4; human. [Q8N3J6-1]
DR CTD; 253559; -.
DR DisGeNET; 253559; -.
DR GeneCards; CADM2; -.
DR HGNC; HGNC:29849; CADM2.
DR HPA; ENSG00000175161; Group enriched (brain, retina).
DR MIM; 609938; gene.
DR neXtProt; NX_Q8N3J6; -.
DR OpenTargets; ENSG00000175161; -.
DR PharmGKB; PA162380882; -.
DR VEuPathDB; HostDB:ENSG00000175161; -.
DR eggNOG; ENOG502QV9X; Eukaryota.
DR GeneTree; ENSGT00940000155947; -.
DR HOGENOM; CLU_047574_2_1_1; -.
DR InParanoid; Q8N3J6; -.
DR OMA; RCRVDHE; -.
DR OrthoDB; 716894at2759; -.
DR PhylomeDB; Q8N3J6; -.
DR TreeFam; TF326804; -.
DR PathwayCommons; Q8N3J6; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR SignaLink; Q8N3J6; -.
DR SIGNOR; Q8N3J6; -.
DR BioGRID-ORCS; 253559; 18 hits in 1070 CRISPR screens.
DR ChiTaRS; CADM2; human.
DR GenomeRNAi; 253559; -.
DR Pharos; Q8N3J6; Tbio.
DR PRO; PR:Q8N3J6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8N3J6; protein.
DR Bgee; ENSG00000175161; Expressed in endothelial cell and 136 other tissues.
DR ExpressionAtlas; Q8N3J6; baseline and differential.
DR Genevisible; Q8N3J6; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032809; C:neuronal cell body membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..435
FT /note="Cell adhesion molecule 2"
FT /id="PRO_0000291970"
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 MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q1WIM2"
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:0000255"
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 1..108
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:21864505"
FT /id="VSP_055355"
FT VAR_SEQ 1..20
FT /note="MIWKRSAVLRFYSVCGLLLQ -> MFVLFLCNLSLVPAAASKNKVK (in
FT isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_026333"
FT VAR_SEQ 20
FT /note="Q -> QAAASKNKVK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_026334"
FT VAR_SEQ 315..354
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:21864505"
FT /id="VSP_055356"
FT VAR_SEQ 316..355
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_026335"
FT CONFLICT 174
FT /note="E -> K (in Ref. 2; AAN16368)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="A -> T (in Ref. 2; AAN16368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 47554 MW; 59DDD41B7F34D446 CRC64;
MIWKRSAVLR FYSVCGLLLQ GSQGQFPLTQ NVTVVEGGTA ILTCRVDQND NTSLQWSNPA
QQTLYFDDKK ALRDNRIELV RASWHELSIS VSDVSLSDEG QYTCSLFTMP VKTSKAYLTV
LGVPEKPQIS GFSSPVMEGD LMQLTCKTSG SKPAADIRWF KNDKEIKDVK YLKEEDANRK
TFTVSSTLDF RVDRSDDGVA VICRVDHESL NATPQVAMQV LEIHYTPSVK IIPSTPFPQE
GQPLILTCES KGKPLPEPVL WTKDGGELPD PDRMVVSGRE LNILFLNKTD NGTYRCEATN
TIGQSSAEYV LIVHDVPNTL LPTTIIPSLT TATVTTTVAI TTSPTTSATT SSIRDPNALA
GQNGPDHALI GGIVAVVVFV TLCSIFLLGR YLARHKGTYL TNEAKGAEDA PDADTAIINA
EGSQVNAEEK KEYFI
