ID   GPBAR_RABIT             Reviewed;         330 AA.
AC   Q862A8;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=G-protein coupled bile acid receptor 1;
GN   Name=GPBAR1; Synonyms=TGR5;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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   -!- TISSUE SPECIFICITY: Expressed at high level in spleen. Expressed at
CC       lower level in thymus, heart, lung, liver, kidney, ileum, blood and
CC       adherent alveolar macrophage cells. {ECO:0000269|PubMed:12524422}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AB089309; BAC55237.1; -; mRNA.
DR   RefSeq; NP_001076117.1; NM_001082648.1.
DR   AlphaFoldDB; Q862A8; -.
DR   SMR; Q862A8; -.
DR   STRING; 9986.ENSOCUP00000004791; -.
DR   GeneID; 100009346; -.
DR   KEGG; ocu:100009346; -.
DR   CTD; 151306; -.
DR   eggNOG; ENOG502SQ0C; Eukaryota.
DR   InParanoid; Q862A8; -.
DR   OrthoDB; 1173007at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
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..330
FT                   /note="G-protein coupled bile acid receptor 1"
FT                   /id="PRO_0000069502"
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..50
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..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..169
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..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..330
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          304..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..330
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   330 AA;  35224 MW;  432072D08CEE0FB1 CRC64;
     MTPNSTGEVP GPIPRGALEL SLALASLIIA ANLLLALGIA CDRRLRSPPA GCFFLSLLLA
     GLLTGLALPT LPGLWRQSHR GYWSCLLVYL APNFSFLSLL ANLLLVHGER YVAVLRPLQP
     PGSIRLALLL TWTGPLLFAS LPALGWNHWG PEANCSSQTI FPAPYLYLEV YGLLLPAVGA
     AALLSAHVLL AAHRQLQDIR RLERAVCRDA PSALARALTW RQARAQAGAT LLFGLCWGPY
     VATLFLSVLA YEQRPPLGPG TLLSLLSLGS ASAAAVPVAM GLGDHRYTAP WRAAARRWLR
     GLRGRGSQAS PGPSTAYHTS SQSSVDVDLN