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GPR4_PIG
ID   GPR4_PIG                Reviewed;         363 AA.
AC   P50132; A0A287AXR9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=G-protein coupled receptor 4;
GN   Name=GPR4;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8595909; DOI=10.1006/geno.1995.0013;
RA   Mahadevan M.S., Baird S., Bailly J.E., Shutler G.G., Sabourin L.A.,
RA   Tsilfidis C., Neville C.E., Narang M., Korneluk R.G.;
RT   "Isolation of a novel G protein-coupled receptor (GPR4) localized to
RT   chromosome 19q13.3.";
RL   Genomics 30:84-88(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc;
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Proton-sensing G-protein coupled receptor couples to multiple
CC       intracellular signaling pathways, including GNAS/cAMP,
CC       GNAQ/phospholipase C (PLC), and GNA13/Rho pathways. Acidosis-induced
CC       GPR4 activation increases paracellular gap formation and permeability
CC       of vascular endothelial cells through the GNA12/GNA13/Rho GTPase
CC       signaling pathway. In the brain may mediate central respiratory
CC       sensitivity to CO(2)/H(+). {ECO:0000250|UniProtKB:Q8BUD0}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P46093};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U22108; AAA98458.1; -; Genomic_DNA.
DR   EMBL; AEMK02000041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B57641; B57641.
DR   RefSeq; NP_001116590.1; NM_001123118.1.
DR   AlphaFoldDB; P50132; -.
DR   SMR; P50132; -.
DR   STRING; 9823.ENSSSCP00000027843; -.
DR   PRIDE; P50132; -.
DR   Ensembl; ENSSSCT00000048531; ENSSSCP00000048942; ENSSSCG00000037184.
DR   Ensembl; ENSSSCT00015013399; ENSSSCP00015005178; ENSSSCG00015010239.
DR   Ensembl; ENSSSCT00025068871; ENSSSCP00025029654; ENSSSCG00025050472.
DR   Ensembl; ENSSSCT00030079836; ENSSSCP00030036556; ENSSSCG00030057267.
DR   Ensembl; ENSSSCT00035088253; ENSSSCP00035036871; ENSSSCG00035065529.
DR   Ensembl; ENSSSCT00040094910; ENSSSCP00040041994; ENSSSCG00040069335.
DR   Ensembl; ENSSSCT00045017735; ENSSSCP00045012208; ENSSSCG00045010480.
DR   Ensembl; ENSSSCT00055018646; ENSSSCP00055014687; ENSSSCG00055009564.
DR   Ensembl; ENSSSCT00060026499; ENSSSCP00060011277; ENSSSCG00060019629.
DR   Ensembl; ENSSSCT00065004228; ENSSSCP00065001719; ENSSSCG00065003170.
DR   GeneID; 100144489; -.
DR   KEGG; ssc:100144489; -.
DR   CTD; 2828; -.
DR   VGNC; VGNC:88631; GPR4.
DR   eggNOG; ENOG502QS9G; Eukaryota.
DR   GeneTree; ENSGT01050000244810; -.
DR   InParanoid; P50132; -.
DR   OMA; RTWEGCH; -.
DR   OrthoDB; 716326at2759; -.
DR   Proteomes; UP000008227; Chromosome 6.
DR   Proteomes; UP000314985; Unplaced.
DR   Bgee; ENSSSCG00000037184; Expressed in oocyte and 24 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR   GO; GO:0043114; P:regulation of vascular permeability; ISS:UniProtKB.
DR   GO; GO:0010447; P:response to acidic pH; ISS:UniProtKB.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR002276; GPR4_orph.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01147; GPR4RECEPTOR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..363
FT                   /note="G-protein coupled receptor 4"
FT                   /id="PRO_0000069513"
FT   TOPO_DOM        1..17
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..42
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..54
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..76
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..91
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..113
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..132
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..154
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        155..179
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..201
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..224
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..263
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..284
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        285..363
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          344..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        90..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        38
FT                   /note="A -> R (in Ref. 1; AAA98458)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        341..350
FT                   /note="GWVASPPSQG -> AGWHLRPPR (in Ref. 1; AAA98458)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   363 AA;  40974 MW;  04610250913FF42D CRC64;
     MGNGTWEGCH VDSRVDHLFP PSLYIFVIGV GLPTNCLALW AAYRQVRQRN ELGVYLMNLS
     IADLLYICTL PLWVDYFLHH DNWIHGPGSC KLFGFIFYTN IYISIAFLCC ISVDRYLAVA
     HPLRFARLRR VKTAVAVSSV VWATELGANS VPLFHDELFR DRYNHTFCFE KFPMEGWVAW
     MNLYRVFVGF LFPWALMLLS YRGILRAVRG SVSTERQEKA KIKRLALSLI AIVLVCFAPY
     HVLLLSRSAV YLGHPWDCGF EERVFSAYHS SLAFTSLNCV ADPILYCLVN EGARSDVAKA
     LHNLLRFLTS DKPQEMASAS LTLDTPLTSK RNSMARAVAA GWVASPPSQG DQVQLKMLPP
     PAP
 
 
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