GPBAR_BOVIN
ID GPBAR_BOVIN Reviewed; 329 AA.
AC Q862A9; Q0II36;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=G-protein coupled bile acid receptor 1;
GN Name=GPBAR1; Synonyms=TGR5;
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 [MRNA].
RX PubMed=12524422; DOI=10.1074/jbc.m209706200;
RA Kawamata Y., Fujii R., Hosoya M., Harada M., Yoshida H., Miwa M.,
RA Fukusumi S., Habata Y., Itoh T., Shintani Y., Hinuma S., Fujisawa Y.,
RA Fujino M.;
RT "A G protein-coupled receptor responsive to bile acids.";
RL J. Biol. Chem. 278:9435-9440(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for bile acid. Bile acid-binding induces its
CC internalization, activation of extracellular signal-regulated kinase
CC and intracellular cAMP production. May be involved in the suppression
CC of macrophage functions by bile acids. Involved in bile acid promoted
CC GLP1R secretion (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB089306; BAC55234.1; -; mRNA.
DR EMBL; BC122824; AAI22825.1; -; mRNA.
DR RefSeq; NP_778219.1; NM_175049.3.
DR RefSeq; XP_005202862.1; XM_005202805.3.
DR RefSeq; XP_005202863.1; XM_005202806.3.
DR AlphaFoldDB; Q862A9; -.
DR SMR; Q862A9; -.
DR PaxDb; Q862A9; -.
DR Ensembl; ENSBTAT00000005120; ENSBTAP00000005120; ENSBTAG00000003923.
DR GeneID; 317756; -.
DR KEGG; bta:317756; -.
DR CTD; 151306; -.
DR VEuPathDB; HostDB:ENSBTAG00000003923; -.
DR VGNC; VGNC:29521; GPBAR1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00390000010256; -.
DR HOGENOM; CLU_895831_0_0_1; -.
DR InParanoid; Q862A9; -.
DR OMA; KDICRLH; -.
DR OrthoDB; 1173007at2759; -.
DR TreeFam; TF333321; -.
DR Reactome; R-BTA-373076; Class A/1 (Rhodopsin-like receptors).
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000003923; Expressed in urinary bladder and 75 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0038182; F:G protein-coupled bile acid receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:1903413; P:cellular response to bile acid; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_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..329
FT /note="G-protein coupled bile acid receptor 1"
FT /id="PRO_0000069499"
FT TOPO_DOM 1..19
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..85
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..165
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 304..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 329 AA; 35104 MW; 407B9E2A310F3C3D CRC64;
MTSNSTREVP SPVPAGALGL SLALASLIVA ANLLLAVGIA GDRRLRSPPA GCFFLSLLLA
GLLTGLALPA LPVLWSQSRR GYWSCLFLYL APNFCFLSLL ANLLLVHGER YMAVLRPLRP
RGSMRLALLL TWAAPLLFAS LPALGWNHWA PGGNCSSQAV FPAPYLYLEI YGLLLPAVGA
AALLSVRVLV TAHRQLQDIR RLERAVCRGA PSALARALTW RQARAQAGAT LLFGLCWGPY
VATLLLSVLA FEQRPPLGPG TLLSLISLGS ASAAAVPVAM GLGDQRYTGP WRVAAQKWLR
MLRGRPQSSP GPSTAYHTSS QSSVDLDLN
