CADM2_MOUSE
ID CADM2_MOUSE Reviewed; 435 AA.
AC Q8BLQ9; B1B1A5; B1B1A6; B2RTL0; Q8BXJ7; Q8BYP1; Q8BZP4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain cortex, Diencephalon, Hypothalamus, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 21-124, GLYCOSYLATION AT ASN-31
RP AND ASN-51, AND DISULFIDE BOND.
RX PubMed=20739279; DOI=10.1074/jbc.m110.120865;
RA Fogel A.I., Li Y., Giza J., Wang Q., Lam T.T., Modis Y., Biederer T.;
RT "N-glycosylation at the SynCAM (synaptic cell adhesion molecule)
RT immunoglobulin interface modulates synaptic adhesion.";
RL J. Biol. Chem. 285:34864-34874(2010).
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=3;
CC Name=1;
CC IsoId=Q8BLQ9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BLQ9-2; Sequence=VSP_026336, VSP_026337;
CC Name=3;
CC IsoId=Q8BLQ9-3; Sequence=VSP_026337;
CC -!- PTM: Glycosylation at Asn-51 reduces adhesive binding.
CC {ECO:0000269|PubMed:20739279}.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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DR EMBL; AK038842; BAC30148.1; -; mRNA.
DR EMBL; AK046800; BAC32876.1; -; mRNA.
DR EMBL; AK033973; BAC28533.1; -; mRNA.
DR EMBL; AK043760; BAC31646.1; -; mRNA.
DR EMBL; AC154674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT010571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139401; AAI39402.1; -; mRNA.
DR EMBL; BC139402; AAI39403.1; -; mRNA.
DR CCDS; CCDS28270.1; -. [Q8BLQ9-2]
DR CCDS; CCDS49885.1; -. [Q8BLQ9-3]
DR CCDS; CCDS84251.1; -. [Q8BLQ9-1]
DR RefSeq; NP_001139449.1; NM_001145977.1. [Q8BLQ9-3]
DR RefSeq; NP_001334176.1; NM_001347247.1. [Q8BLQ9-1]
DR RefSeq; NP_848836.2; NM_178721.4. [Q8BLQ9-2]
DR PDB; 3M45; X-ray; 2.21 A; A/B/C/D=21-124.
DR PDBsum; 3M45; -.
DR AlphaFoldDB; Q8BLQ9; -.
DR SMR; Q8BLQ9; -.
DR IntAct; Q8BLQ9; 1.
DR GlyConnect; 2421; 9 N-Linked glycans (3 sites). [Q8BLQ9-2]
DR GlyGen; Q8BLQ9; 3 sites.
DR iPTMnet; Q8BLQ9; -.
DR PhosphoSitePlus; Q8BLQ9; -.
DR MaxQB; Q8BLQ9; -.
DR PeptideAtlas; Q8BLQ9; -.
DR PRIDE; Q8BLQ9; -.
DR ProteomicsDB; 273893; -. [Q8BLQ9-1]
DR ProteomicsDB; 273894; -. [Q8BLQ9-2]
DR ProteomicsDB; 273895; -. [Q8BLQ9-3]
DR Antibodypedia; 2209; 213 antibodies from 26 providers.
DR DNASU; 239857; -.
DR Ensembl; ENSMUST00000114292; ENSMUSP00000109931; ENSMUSG00000064115. [Q8BLQ9-2]
DR Ensembl; ENSMUST00000120594; ENSMUSP00000113500; ENSMUSG00000064115. [Q8BLQ9-1]
DR Ensembl; ENSMUST00000120898; ENSMUSP00000113178; ENSMUSG00000064115. [Q8BLQ9-3]
DR GeneID; 239857; -.
DR KEGG; mmu:239857; -.
DR UCSC; uc007zqn.2; mouse. [Q8BLQ9-2]
DR UCSC; uc007zqo.2; mouse. [Q8BLQ9-3]
DR CTD; 253559; -.
DR MGI; MGI:2442722; Cadm2.
DR VEuPathDB; HostDB:ENSMUSG00000064115; -.
DR GeneTree; ENSGT00940000155947; -.
DR HOGENOM; CLU_047574_2_1_1; -.
DR InParanoid; Q8BLQ9; -.
DR OMA; RCRVDHE; -.
DR PhylomeDB; Q8BLQ9; -.
DR TreeFam; TF326804; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR BioGRID-ORCS; 239857; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cadm2; mouse.
DR PRO; PR:Q8BLQ9; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BLQ9; protein.
DR Bgee; ENSMUSG00000064115; Expressed in primary motor cortex and 161 other tissues.
DR ExpressionAtlas; Q8BLQ9; baseline and differential.
DR Genevisible; Q8BLQ9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cell projection; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..435
FT /note="Cell adhesion molecule 2"
FT /id="PRO_0000291971"
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 337..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000269|PubMed:20739279"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20739279"
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 ECO:0000269|PubMed:20739279"
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 20
FT /note="Q -> QAAASKSKVK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026336"
FT VAR_SEQ 315..354
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026337"
FT CONFLICT 297
FT /note="E -> K (in Ref. 1; BAC30148)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="E -> K (in Ref. 1; BAC28533)"
FT /evidence="ECO:0000305"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:3M45"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:3M45"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3M45"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:3M45"
FT STRAND 77..91
FT /evidence="ECO:0007829|PDB:3M45"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3M45"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:3M45"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3M45"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:3M45"
SQ SEQUENCE 435 AA; 47559 MW; B5F4AB448B2EA5E1 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
GQALTLTCES KGKPLPEPVL WTKDGAELPD PDRMVVSGRE LNILFLNKTD NGTYRCEATN
TIGQSSAEYV LIVHDVPNTL LPTTIIPSLT TAPVTTSVTI TTSPSTSASS SSRRDPNSLA
GQNGPDHALI GGIVAVVVFV TLCSIFLLGR YLARHKGTYL TNEAKGAEDA PDADTAIINA
EGSQVNAEEK KEYFI
