CLM8_RAT
ID CLM8_RAT Reviewed; 310 AA.
AC A2TGX5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=CMRF35-like molecule 8;
DE Short=CLM-8;
DE AltName: Full=CD300 antigen-like family member A;
DE AltName: CD_antigen=CD300a;
DE Flags: Precursor;
GN Name=Cd300a;
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=Wistar;
RA Martinez-Barriocanal A., Peluffo H., Sayos J.;
RT "Cloning of the rat ortholog of the inhibitory receptor CD300a.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inhibitory receptor which may contribute to the down-
CC regulation of cytolytic activity in natural killer (NK) cells, and to
CC the down-regulation of mast cell degranulation. Negatively regulates
CC the Toll-like receptor (TLR) signaling mediated by MYD88 but not TRIF
CC through activation of PTPN6. {ECO:0000250|UniProtKB:Q9UGN4}.
CC -!- SUBUNIT: Upon tyrosine-phosphorylation, interacts with PTN6/SHP-1 and
CC PTPN11/SHP-2 and INPP5D. {ECO:0000250|UniProtKB:Q6SJQ0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6SJQ0};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6SJQ0}.
CC -!- PTM: Phosphorylated on tyrosine. {ECO:0000250|UniProtKB:Q6SJQ0}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6SJQ0}.
CC -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
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DR EMBL; EF199812; ABM90425.1; -; mRNA.
DR AlphaFoldDB; A2TGX5; -.
DR SMR; A2TGX5; -.
DR GlyGen; A2TGX5; 3 sites.
DR PeptideAtlas; A2TGX5; -.
DR RGD; 1583719; Cd300a.
DR InParanoid; A2TGX5; -.
DR PhylomeDB; A2TGX5; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:A2TGX5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0019902; F:phosphatase binding; ISO:RGD.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; ISO:RGD.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:RGD.
DR GO; GO:0038023; F:signaling receptor activity; ISO:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:1902569; P:negative regulation of activation of Janus kinase activity; ISO:RGD.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; ISO:RGD.
DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; ISO:RGD.
DR GO; GO:1902567; P:negative regulation of eosinophil activation; ISO:RGD.
DR GO; GO:2000417; P:negative regulation of eosinophil migration; ISO:RGD.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; ISO:RGD.
DR GO; GO:0043305; P:negative regulation of mast cell degranulation; ISO:RGD.
DR GO; GO:0034125; P:negative regulation of MyD88-dependent toll-like receptor signaling pathway; ISO:RGD.
DR GO; GO:1902564; P:negative regulation of neutrophil activation; ISO:RGD.
DR GO; GO:0051134; P:negative regulation of NK T cell activation; ISO:RGD.
DR GO; GO:0060101; P:negative regulation of phagocytosis, engulfment; ISO:RGD.
DR GO; GO:0014063; P:negative regulation of serotonin secretion; ISO:RGD.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:RGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
DR GO; GO:0050856; P:regulation of T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0002552; P:serotonin secretion by mast cell; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 1.
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; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..310
FT /note="CMRF35-like molecule 8"
FT /id="PRO_0000320133"
FT TOPO_DOM 27..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..128
FT /note="Ig-like V-type"
FT REGION 136..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6SJQ0"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 310 AA; 34495 MW; 8761E70FF6BD8360 CRC64;
MTQLASAVWP PTLLLLLLFW VPGCVPLRGP SSVTGTVGES LNVTCQYEER FKMNKKYWCR
GSLVLLCKDI VRTGGSEEAR NGRVSIRDDR DNLTFTVTLQ NLTLEDAGTY MCAVDIPLID
HSFKVELSVV PGNIPVSSPG TTRETTVVPT SFSTKGPTQG SIPEGHHEHY EPQGLSLPVL
LSVLALLLLL LVGTSLLAWR MFQKRSVKAD KHPEMSQNLR QAEEQSESQY VNLQLHTLPL
REEPVPPSQV EVEYSTLALP QEELHYTSVV FDSQRQNSHA NGDPPCQSPD QKTEYSEIRK
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