GPBAR_HUMAN
ID GPBAR_HUMAN Reviewed; 330 AA.
AC Q8TDU6; B3KV35;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=G-protein coupled bile acid receptor 1;
DE AltName: Full=G-protein coupled receptor GPCR19;
DE Short=hGPCR19;
DE AltName: Full=Membrane-type receptor for bile acids;
DE Short=M-BAR;
DE AltName: Full=hBG37;
DE Short=BG37;
GN Name=GPBAR1; Synonyms=TGR5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP 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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=12044878; DOI=10.1016/s0014-5793(02)02775-8;
RA Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.;
RT "Identification of G protein-coupled receptor genes from the human genome
RT sequence.";
RL FEBS Lett. 520:97-101(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. {ECO:0000269|PubMed:12419312,
CC ECO:0000269|PubMed:12524422}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12524422};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12524422}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher level
CC in spleen and placenta. Expressed at lower level in other tissues. In
CC digestive tissues, it is expressed in stomach, duodenum, ileocecum,
CC ileum, jejunum, ascending colon, transverse colon, descending colon,
CC cecum and liver, but not in esophagus and rectum.
CC {ECO:0000269|PubMed:12044878, ECO:0000269|PubMed:12419312,
CC 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; AB086170; BAC65343.1; -; mRNA.
DR EMBL; AB089307; BAC55235.1; -; mRNA.
DR EMBL; AB083601; BAB89314.1; -; Genomic_DNA.
DR EMBL; AK122658; BAG53647.1; -; mRNA.
DR EMBL; AK122660; BAG53648.1; -; mRNA.
DR EMBL; CH471063; EAW70598.1; -; Genomic_DNA.
DR EMBL; BC033625; AAH33625.1; -; mRNA.
DR CCDS; CCDS46515.1; -.
DR RefSeq; NP_001070659.1; NM_001077191.1.
DR RefSeq; NP_001070662.1; NM_001077194.1.
DR RefSeq; NP_001308879.1; NM_001321950.1.
DR RefSeq; NP_733800.1; NM_170699.2.
DR RefSeq; XP_011509045.1; XM_011510743.1.
DR RefSeq; XP_016858956.1; XM_017003467.1.
DR RefSeq; XP_016858957.1; XM_017003468.1.
DR RefSeq; XP_016858958.1; XM_017003469.1.
DR PDB; 7BW0; EM; 3.90 A; R=6-307.
DR PDB; 7CFM; EM; 3.00 A; R=1-330.
DR PDB; 7CFN; EM; 3.00 A; R=1-330.
DR PDBsum; 7BW0; -.
DR PDBsum; 7CFM; -.
DR PDBsum; 7CFN; -.
DR AlphaFoldDB; Q8TDU6; -.
DR SMR; Q8TDU6; -.
DR BioGRID; 127367; 30.
DR IntAct; Q8TDU6; 8.
DR STRING; 9606.ENSP00000430886; -.
DR BindingDB; Q8TDU6; -.
DR ChEMBL; CHEMBL5409; -.
DR DrugBank; DB06777; Chenodeoxycholic acid.
DR DrugBank; DB02659; Cholic Acid.
DR DrugBank; DB03619; Deoxycholic acid.
DR DrugCentral; Q8TDU6; -.
DR GuidetoPHARMACOLOGY; 37; -.
DR SwissLipids; SLP:000001566; -.
DR TCDB; 9.A.14.21.1; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q8TDU6; 2 sites.
DR BioMuta; GPBAR1; -.
DR DMDM; 74762624; -.
DR PaxDb; Q8TDU6; -.
DR PeptideAtlas; Q8TDU6; -.
DR PRIDE; Q8TDU6; -.
DR ProteomicsDB; 74340; -.
DR Antibodypedia; 34258; 315 antibodies from 31 providers.
DR DNASU; 151306; -.
DR Ensembl; ENST00000479077.5; ENSP00000430698.1; ENSG00000179921.15.
DR Ensembl; ENST00000519574.2; ENSP00000430202.1; ENSG00000179921.15.
DR Ensembl; ENST00000521462.1; ENSP00000428824.1; ENSG00000179921.15.
DR Ensembl; ENST00000522678.5; ENSP00000430886.1; ENSG00000179921.15.
DR GeneID; 151306; -.
DR KEGG; hsa:151306; -.
DR MANE-Select; ENST00000519574.2; ENSP00000430202.1; NM_170699.3; NP_733800.1.
DR UCSC; uc010zjw.1; human.
DR CTD; 151306; -.
DR DisGeNET; 151306; -.
DR GeneCards; GPBAR1; -.
DR HGNC; HGNC:19680; GPBAR1.
DR HPA; ENSG00000179921; Tissue enhanced (adipose tissue, breast, gallbladder).
DR MIM; 610147; gene.
DR neXtProt; NX_Q8TDU6; -.
DR OpenTargets; ENSG00000179921; -.
DR PharmGKB; PA134903170; -.
DR VEuPathDB; HostDB:ENSG00000179921; -.
DR eggNOG; ENOG502SQ0C; Eukaryota.
DR GeneTree; ENSGT00390000010256; -.
DR HOGENOM; CLU_895831_0_0_1; -.
DR InParanoid; Q8TDU6; -.
DR OMA; KDICRLH; -.
DR OrthoDB; 1173007at2759; -.
DR PhylomeDB; Q8TDU6; -.
DR TreeFam; TF333321; -.
DR PathwayCommons; Q8TDU6; -.
DR Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; Q8TDU6; -.
DR BioGRID-ORCS; 151306; 16 hits in 1068 CRISPR screens.
DR GeneWiki; G_protein-coupled_bile_acid_receptor; -.
DR GenomeRNAi; 151306; -.
DR Pharos; Q8TDU6; Tchem.
DR PRO; PR:Q8TDU6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8TDU6; protein.
DR Bgee; ENSG00000179921; Expressed in monocyte and 95 other tissues.
DR Genevisible; Q8TDU6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
DR GO; GO:0038181; F:bile acid receptor activity; IDA:UniProtKB.
DR GO; GO:0038182; F:G protein-coupled bile acid receptor activity; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0038184; P:cell surface bile acid receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:1903413; P:cellular response to bile acid; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1904056; P:positive regulation of cholangiocyte proliferation; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
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 PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..330
FT /note="G-protein coupled bile acid receptor 1"
FT /id="PRO_0000069500"
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..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..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..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 309..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..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 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 85..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT HELIX 22..41
FT /evidence="ECO:0007829|PDB:7CFM"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:7CFM"
FT HELIX 49..67
FT /evidence="ECO:0007829|PDB:7CFM"
FT TURN 69..74
FT /evidence="ECO:0007829|PDB:7CFM"
FT HELIX 82..115
FT /evidence="ECO:0007829|PDB:7CFM"
FT HELIX 124..144
FT /evidence="ECO:0007829|PDB:7CFM"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:7CFM"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:7CFM"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:7CFM"
FT HELIX 174..206
FT /evidence="ECO:0007829|PDB:7CFM"
FT HELIX 213..251
FT /evidence="ECO:0007829|PDB:7CFM"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:7CFM"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:7CFM"
FT HELIX 263..283
FT /evidence="ECO:0007829|PDB:7CFM"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:7CFM"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:7CFM"
SQ SEQUENCE 330 AA; 35248 MW; B3A1AEDADEAFE021 CRC64;
MTPNSTGEVP SPIPKGALGL SLALASLIIT ANLLLALGIA WDRRLRSPPA GCFFLSLLLA
GLLTGLALPT LPGLWNQSRR GYWSCLLVYL APNFSFLSLL ANLLLVHGER YMAVLRPLQP
PGSIRLALLL TWAGPLLFAS LPALGWNHWT PGANCSSQAI FPAPYLYLEV YGLLLPAVGA
AAFLSVRVLA TAHRQLQDIC RLERAVCRDE PSALARALTW RQARAQAGAM LLFGLCWGPY
VATLLLSVLA YEQRPPLGPG TLLSLLSLGS ASAAAVPVAM GLGDQRYTAP WRAAAQRCLQ
GLWGRASRDS PGPSIAYHPS SQSSVDLDLN
