CADM4_RAT
ID CADM4_RAT Reviewed; 388 AA.
AC Q1WIM1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cell adhesion molecule 4;
DE AltName: Full=Immunoglobulin superfamily member 4C;
DE Short=IgSF4C;
DE AltName: Full=Nectin-like protein 4;
DE Short=NECL-4;
DE Flags: Precursor;
GN Name=Cadm4; Synonyms=Igsf4c, Necl4;
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].
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 PROTEIN SEQUENCE OF 46-73; 77-85; 133-157; 177-187; 192-257 AND 353-383,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, 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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-67, 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: Involved in the cell-cell adhesion. Has calcium- and
CC magnesium-independent cell-cell adhesion activity. May have tumor-
CC suppressor activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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DR EMBL; DQ272745; ABB85364.1; -; mRNA.
DR RefSeq; NP_001040572.1; NM_001047107.1.
DR AlphaFoldDB; Q1WIM1; -.
DR SMR; Q1WIM1; -.
DR BioGRID; 265212; 1.
DR IntAct; Q1WIM1; 1.
DR MINT; Q1WIM1; -.
DR STRING; 10116.ENSRNOP00000026793; -.
DR GlyGen; Q1WIM1; 4 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q1WIM1; -.
DR PhosphoSitePlus; Q1WIM1; -.
DR SwissPalm; Q1WIM1; -.
DR PaxDb; Q1WIM1; -.
DR PRIDE; Q1WIM1; -.
DR ABCD; Q1WIM1; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000026793; ENSRNOP00000026793; ENSRNOG00000024243.
DR GeneID; 365216; -.
DR KEGG; rno:365216; -.
DR UCSC; RGD:1304722; rat.
DR CTD; 199731; -.
DR RGD; 1304722; Cadm4.
DR eggNOG; ENOG502RFJZ; Eukaryota.
DR GeneTree; ENSGT00940000161223; -.
DR InParanoid; Q1WIM1; -.
DR OrthoDB; 716894at2759; -.
DR PhylomeDB; Q1WIM1; -.
DR PRO; PR:Q1WIM1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0044291; C:cell-cell contact zone; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD.
DR GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; ISO:RGD.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; ISS:UniProtKB.
DR GO; GO:0061041; P:regulation of wound healing; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR028807; Cadm4.
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 PANTHER; PTHR45889:SF3; PTHR45889:SF3; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix; Tumor suppressor.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..388
FT /note="Cell adhesion molecule 4"
FT /id="PRO_0000291982"
FT TOPO_DOM 25..324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..119
FT /note="Ig-like V-type"
FT DOMAIN 124..219
FT /note="Ig-like C2-type 1"
FT DOMAIN 224..307
FT /note="Ig-like C2-type 2"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 145..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 245..291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 388 AA; 42781 MW; D4657BBF73531426 CRC64;
MGRARRFQWP LLLLWAAAAG PGTAQEVQTE NVTVAEGGVA EITCRLHQYD GSIVVIQNPA
RQTLFFNGTR ALKDERFQLE EFSPRRVRIR LSDARLEDEG GYFCQLYTED THHQIATLTV
LVAPENPVVE VREQAVEGGE VELSCLVPRS RPAAVLRWYR DRKELKGVSS GQENGKVWSV
ASTVRFRVDR KDDGGIVICE AQNQALPSGH SKQTQYVLDV QYSPTARIHA SQAVVREGDT
LVLTCAVTGN PRPNQIRWNR GNESLPERAE ALGETLTLPG LVSADNGTYT CEAANKHGHA
RALYVLVVYD PGAVVEAQTS VPYAIVGGIL ALLVFLIICV LVGMVWCSVR QKGSYLTHEA
SGLDEQGEAR EAFLNGSDGH KRKEEFFI
