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GPR17_MOUSE
ID   GPR17_MOUSE             Reviewed;         339 AA.
AC   Q6NS65; Q80UD2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Uracil nucleotide/cysteinyl leukotriene receptor;
DE            Short=UDP/CysLT receptor;
DE   AltName: Full=G-protein coupled receptor 17;
GN   Name=Gpr17 {ECO:0000312|MGI:MGI:3584514};
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] {ECO:0000312|EMBL:AAH70439.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH70439.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH70439.1};
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   [2] {ECO:0000312|EMBL:AAO85055.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 132-308.
RX   PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
CC   -!- FUNCTION: Dual specificity receptor for uracil nucleotides and
CC       cysteinyl leukotrienes (CysLTs). Signals through G(i) and inhibition of
CC       adenylyl cyclase. May mediate brain damage by nucleotides and CysLTs
CC       following ischemia (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q6NS65; Q99JA4: Cysltr1; NbExp=2; IntAct=EBI-15791369, EBI-15791392;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; BC070439; AAH70439.1; -; mRNA.
DR   EMBL; AY255543; AAO85055.1; -; mRNA.
DR   CCDS; CCDS29114.1; -.
DR   RefSeq; NP_001020552.1; NM_001025381.2.
DR   AlphaFoldDB; Q6NS65; -.
DR   SMR; Q6NS65; -.
DR   BioGRID; 300034; 1.
DR   DIP; DIP-48915N; -.
DR   IntAct; Q6NS65; 1.
DR   STRING; 10090.ENSMUSP00000063670; -.
DR   BindingDB; Q6NS65; -.
DR   ChEMBL; CHEMBL4295864; -.
DR   DrugCentral; Q6NS65; -.
DR   GuidetoPHARMACOLOGY; 88; -.
DR   GlyGen; Q6NS65; 2 sites.
DR   iPTMnet; Q6NS65; -.
DR   PhosphoSitePlus; Q6NS65; -.
DR   SwissPalm; Q6NS65; -.
DR   PaxDb; Q6NS65; -.
DR   PeptideAtlas; Q6NS65; -.
DR   PRIDE; Q6NS65; -.
DR   ProteomicsDB; 271269; -.
DR   Antibodypedia; 18483; 447 antibodies from 36 providers.
DR   DNASU; 574402; -.
DR   Ensembl; ENSMUST00000064016; ENSMUSP00000063670; ENSMUSG00000052229.
DR   GeneID; 574402; -.
DR   KEGG; mmu:574402; -.
DR   UCSC; uc008eiw.2; mouse.
DR   CTD; 2840; -.
DR   MGI; MGI:3584514; Gpr17.
DR   VEuPathDB; HostDB:ENSMUSG00000052229; -.
DR   eggNOG; ENOG502QW6S; Eukaryota.
DR   GeneTree; ENSGT01050000244810; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q6NS65; -.
DR   OMA; TCLNGAM; -.
DR   OrthoDB; 1166460at2759; -.
DR   PhylomeDB; Q6NS65; -.
DR   TreeFam; TF330775; -.
DR   Reactome; R-MMU-391906; Leukotriene receptors.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   Reactome; R-MMU-417957; P2Y receptors.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 574402; 4 hits in 72 CRISPR screens.
DR   PRO; PR:Q6NS65; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q6NS65; protein.
DR   Bgee; ENSMUSG00000052229; Expressed in lumbar subsegment of spinal cord and 90 other tissues.
DR   Genevisible; Q6NS65; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0033612; F:receptor serine/threonine kinase binding; ISO:MGI.
DR   GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IMP:MGI.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..339
FT                   /note="Uracil nucleotide/cysteinyl leukotriene receptor"
FT                   /id="PRO_0000278171"
FT   TOPO_DOM        1..36
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..195
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        217..232
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        254..280
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        302..339
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        104..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   339 AA;  37839 MW;  087248DC3294D0D6 CRC64;
     MNGLEAALPS LTDNSSLAYS EQCGQETPLE NMLFACFYLL DFILAFVGNA LALWLFIWDH
     KSGTPANVFL MHLAVADLSC VLVLPTRLVY HFSGNHWPFG EIPCRLTGFL FYLNMYASIY
     FLTCISADRF LAIVHPVKSL KLRRPLYAHL ACAFLWIVVA VAMAPLLVSP QTVQTNHTVV
     CLQLYREKAS HHALASLAVA FTFPFITTVT CYLLIIRSLR QGPRIEKHLK NKAVRMIAMV
     LAIFLICFVP YHIHRSVYVL HYRGGGTSCA AQRALALGNR ITSCLTSLNG ALDPVMYFFV
     AEKFRHALCN LLCSKRLTGP PPSFEGKTNE SSLSARSEL
 
 
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