GPR4_BOVIN
ID GPR4_BOVIN Reviewed; 362 AA.
AC Q1JQB3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=G-protein coupled receptor 4;
GN Name=GPR4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) 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; BC116089; AAI16090.1; -; mRNA.
DR RefSeq; NP_001069051.1; NM_001075583.1.
DR RefSeq; XP_005219298.1; XM_005219241.1.
DR AlphaFoldDB; Q1JQB3; -.
DR SMR; Q1JQB3; -.
DR STRING; 9913.ENSBTAP00000024480; -.
DR PaxDb; Q1JQB3; -.
DR Ensembl; ENSBTAT00000024480; ENSBTAP00000024480; ENSBTAG00000018398.
DR GeneID; 512876; -.
DR KEGG; bta:512876; -.
DR CTD; 2828; -.
DR VEuPathDB; HostDB:ENSBTAG00000018398; -.
DR VGNC; VGNC:29587; GPR4.
DR eggNOG; ENOG502QS9G; Eukaryota.
DR GeneTree; ENSGT01050000244810; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q1JQB3; -.
DR OMA; RTWEGCH; -.
DR OrthoDB; 716326at2759; -.
DR TreeFam; TF331803; -.
DR Reactome; R-BTA-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-BTA-416476; G alpha (q) signalling events.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000018398; Expressed in laryngeal cartilage and 98 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0060055; P:angiogenesis involved in wound healing; IEA:Ensembl.
DR GO; GO:0072144; P:glomerular mesangial cell development; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; 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:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..362
FT /note="G-protein coupled receptor 4"
FT /id="PRO_0000379518"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..92
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..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..271
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..289
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 362 AA; 41076 MW; A927566FC0B39C4F CRC64;
MGNRTLEGCH VDSRMDHLFP PSLYIFVIGV GLPTNCLALW AAYRQVRQRN ELGVYLMNLS
IADLLYICTL PLWVDYFLHH DNWIHGPGSC KLFGFIFYTN IYISIAFLCC ISVDRYLAVA
HPLRFARLRR VKTAVAVSSV VWATELGANS APLFHDELFR DRYNHTFCFE KFPMEGWVAW
MNLYRVFVGF LFPWALMLLS YRGILRAVRG SVSTERQEKV KIKRLALSLI AIVLVCFAPY
HVLLLSRSAV YLRRPRDCGF EERVFSAYHS SLAFTSLNCV ADPILYCLVN EGARSDVAKA
LHHLLRFLAS DKPQEMANAS LTLETPLTSK RNSMAKAMAA GWVAAPLAQG DQVQLKMLPP
AQ
