GPBAR_RAT
ID GPBAR_RAT Reviewed; 329 AA.
AC Q80T02;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=G-protein coupled bile acid receptor 1;
DE AltName: Full=Membrane-type receptor for bile acids;
DE Short=M-BAR;
GN Name=Gpbar1; Synonyms=Tgr5;
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].
RX PubMed=12419312; DOI=10.1016/s0006-291x(02)02550-0;
RA Maruyama T., Miyamoto Y., Nakamura T., Tamai Y., Okada H., Sugiyama E.,
RA Nakamura T., Itadani H., Tanaka K.;
RT "Identification of membrane-type receptor for bile acids (M-BAR).";
RL Biochem. Biophys. Res. Commun. 298:714-719(2002).
RN [2]
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).
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; AB086172; BAC65345.1; -; mRNA.
DR EMBL; AB089310; BAC55238.1; -; mRNA.
DR RefSeq; NP_808797.1; NM_177936.1.
DR RefSeq; XP_006245297.1; XM_006245235.3.
DR AlphaFoldDB; Q80T02; -.
DR SMR; Q80T02; -.
DR BindingDB; Q80T02; -.
DR ChEMBL; CHEMBL1075223; -.
DR GlyGen; Q80T02; 3 sites.
DR Ensembl; ENSRNOT00000089698; ENSRNOP00000075574; ENSRNOG00000058260.
DR GeneID; 338443; -.
DR KEGG; rno:338443; -.
DR UCSC; RGD:631400; rat.
DR CTD; 151306; -.
DR RGD; 631400; Gpbar1.
DR GeneTree; ENSGT00390000010256; -.
DR HOGENOM; CLU_895831_0_0_1; -.
DR InParanoid; Q80T02; -.
DR OMA; KDICRLH; -.
DR OrthoDB; 1173007at2759; -.
DR PhylomeDB; Q80T02; -.
DR TreeFam; TF333321; -.
DR Reactome; R-RNO-373076; Class A/1 (Rhodopsin-like receptors).
DR PRO; PR:Q80T02; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000058260; Expressed in stomach and 2 other tissues.
DR ExpressionAtlas; Q80T02; baseline.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0038181; F:bile acid receptor activity; ISO:RGD.
DR GO; GO:0038182; F:G protein-coupled bile acid receptor activity; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:RGD.
DR GO; GO:0038184; P:cell surface bile acid receptor signaling pathway; ISO:RGD.
DR GO; GO:1903413; P:cellular response to bile acid; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1904056; P:positive regulation of cholangiocyte proliferation; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
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_0000069503"
FT TOPO_DOM 1..18
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..84
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 306..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 329 AA; 35791 MW; 03ED6F91C5FC7653 CRC64;
MMSHNTTELS AIPRGVQELS LVLASLIVIA NLLLALGIVL DRHLRSPPAG CFFLSLLLAG
LLTGLALPTL PGLWNRSHQG YWSCLLLHLA PNFCFLSLLA NLLLVHGERY MAVLQPLRPH
GSVRLALFLT WISSLLFASL PALGWNHWSP GANCSSQAIF PAPYLYLEVY GLLLPAVGAT
ALLSVRVLAT AHHQLREIRR LERAVCRDAP STLARALTWR QARAQAGATL LFLLCWGPYV
ATLLLSVLAY ERRPPLGPVT LLSLISLGSA SAAVVPVAMG LGDQRYTAPW RTAAQRWLQV
LRGRPKRANP GPSTAYHSSS QCSTDLDLN
