GPBAR1
entrez
151306
canonical
uniprot
Q8TDU6
canonical
ensembl
ENSG00000179921
resolver
ensp
ENSP00000428824
resolver
ensp
ENSP00000430202
resolver
ensp
ENSP00000430698
resolver
ensp
ENSP00000430886
resolver
ensp
ENSP00000641070
resolver
ensp
ENSP00000641071
resolver
ensp
ENSP00000641072
resolver
enst
ENST00000479077
resolver
enst
ENST00000519574
resolver
enst
ENST00000521462
resolver
enst
ENST00000522678
resolver
enst
ENST00000971011
resolver
enst
ENST00000971012
resolver
enst
ENST00000971013
resolver
genesymbol
GPBAR1
resolver
genesymbol_syn
TGR5
resolver
hgnc
HGNC:19680
resolver
uniprot
B3KV35
resolver
uniprot_entry
GPBAR_HUMAN
resolver
uniprot_sec
B3KV35
resolver
amino_acid_sequence
MTPNSTGEVPSPIPKGALGLSLALASLIITANLLLALGIAWDRRLRSPPAGCFFLSLLLAGLLTGLALPTLPGLWNQSRRGYWSCLLVYLAPNFSFLSLLANLLLVHGERYMAVLRPLQPPGSIRLALLLTWAGPLLFASLPALGWNHWTPGANCSSQAIFPAPYLYLEVYGLLLPAVGAAAFLSVRVLATAHRQLQDICRLERAVCRDEPSALARALTWRQARAQAGAMLLFGLCWGPYVATLLLSVLAYEQRPPLGPGTLLSLLSLGSASAAAVPVAMGLGDQRYTAPWRAAAQRCLQGLWGRASRDSPGPSIAYHPSSQSSVDLDLN
uniprot
proteins
function
FUNCTION: G protein-coupled receptor for bile acid (PubMed:12419312, PubMed:12524422, PubMed:32698187, PubMed:32747649, PubMed:35858343). Bile acid-binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:12419312, PubMed:12524422, PubMed:32698187, PubMed:32747649, PubMed:35858343). GPBAR1 is coupled to G(s) G proteins and mediates activation of adenylate cyclase activity (PubMed:12419312, PubMed:12524422, PubMed:32698187, PubMed:32747649, PubMed:35858343). Activated by bile acids, such as lithocholate, deoxycholate, chenodeoxycholate and cholate, in descending order (PubMed:12524422, PubMed:32698187). Apart from their role in lipid dietary absorption and cholesterol catabolism, bile acids act as an important signaling molecule, involved in processes, such as energy expenditure or tissue inflammation (PubMed:26541439). GPBAR1-mediated signaling promotes energy expenditure and adiposity reduction in brown adipose tissue by activating adenylate cyclase, leading to DIO2 activation (By similarity). Involved in bile acid promoted GLP-1 secretion (By similarity). {ECO:0000250|UniProtKB:Q80SS6, ECO:0000269|PubMed:12419312, ECO:0000269|PubMed:12524422, ECO:0000269|PubMed:32698187, ECO:0000269|PubMed:32747649, ECO:0000269|PubMed:35858343, ECO:0000303|PubMed:26541439}.
uniprot
proteins
mass_dalton
35248
uniprot
proteins
mutagenesis
MUTAGEN 71; /note="L->W: Decreased activation in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32747649"; MUTAGEN 74; /note="L->W: Decreased activation in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32747649"; MUTAGEN 75; /note="W->A: Does not affect activation in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32747649"; MUTAGEN 89; /note="Y->A: Does not affect activation in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32747649"; MUTAGEN 96; /note="F->A: Decreased activation in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32747649"; MUTAGEN 97; /note="L->W: Decreased activation in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32747649"; MUTAGEN 104; /note="L->A: Decreased G(s)-mediated signaling in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32698187"; MUTAGEN 120; /note="P->G: Does not affect G(s)-mediated signaling in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32698187"; MUTAGEN 121; /note="P->G: Does not affect G(s)-mediated signaling in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32698187"; MUTAGEN 130; /note="L->A: Decreased G(s)-mediated signaling in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32698187"; MUTAGEN 166; /note="L->W: Decreased G(s)-mediated signaling in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32747649"; MUTAGEN 169; /note="E->W: Decreased G(s)-mediated signaling in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32747649"; MUTAGEN 240; /note="Y->A: Increased constitutive activity but strongly decreased G(s)-mediated signaling in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32698187, ECO:0000269|PubMed:32747649"; MUTAGEN 240; /note="Y->F: Increased constitutive activity but strongly decreased G(s)-mediated signaling in response to bile acid-binding."; /evidence="ECO:0000269|PubMed:32698187, ECO:0000269|PubMed:32747649"; MUTAGEN 244; /note="L->A: Decreased G(s)-mediated signaling in response to bile acids with a hydroxyl group at position R1."; /evidence="ECO:0000269|PubMed:32698187"; MUTAGEN 263; /note="L->A: Slightly decreased G(s)-mediated signaling in response to bile acids with a hydroxyl group at position R3."; /evidence="ECO:0000269|PubMed:32698187"; MUTAGEN 266; /note="L->A: Decreased G(s)-mediated signaling in response to bile acids with a hydroxyl group at position R2."; /evidence="ECO:0000269|PubMed:32698187
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
12044878
uniprot
proteins
pubmed
12419312
uniprot
proteins
pubmed
12524422
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
26541439
uniprot
proteins
pubmed
32698187
uniprot
proteins
pubmed
32747649
uniprot
proteins
pubmed
35858343
uniprot
proteins
sequence_length
330
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12419312, ECO:0000269|PubMed:12524422}; Multi-pass membrane protein {ECO:0000269|PubMed:32698187, ECO:0000269|PubMed:32747649, ECO:0000269|PubMed:35858343}.
uniprot
proteins
transmembrane_region
TRANSMEM 22..41; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:32698187, ECO:0000269|PubMed:32747649, ECO:0000269|PubMed:35858343, ECO:0007744|PDB:7BW0, ECO:0007744|PDB:7CFM, ECO:0007744|PDB:7CFN, ECO:0007744|PDB:7XTQ"; TRANSMEM 51..72; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:32698187, ECO:0000269|PubMed:32747649, ECO:0000269|PubMed:35858343, ECO:0007744|PDB:7BW0, ECO:0007744|PDB:7CFM, ECO:0007744|PDB:7CFN, ECO:0007744|PDB:7XTQ"; TRANSMEM 86..108; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:32698187, ECO:0000269|PubMed:32747649, ECO:0000269|PubMed:35858343, ECO:0007744|PDB:7BW0, ECO:0007744|PDB:7CFM, ECO:0007744|PDB:7CFN, ECO:0007744|PDB:7XTQ"; TRANSMEM 124..144; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:32698187, ECO:0000269|PubMed:32747649, ECO:0000269|PubMed:35858343, ECO:0007744|PDB:7BW0, ECO:0007744|PDB:7CFM, ECO:0007744|PDB:7CFN, ECO:0007744|PDB:7XTQ"; TRANSMEM 161..186; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:32698187, ECO:0000269|PubMed:32747649, ECO:0000269|PubMed:35858343, ECO:0007744|PDB:7BW0, ECO:0007744|PDB:7CFM, ECO:0007744|PDB:7CFN, ECO:0007744|PDB:7XTQ"; TRANSMEM 226..249; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:32698187, ECO:0000269|PubMed:32747649, ECO:0000269|PubMed:35858343, ECO:0007744|PDB:7BW0, ECO:0007744|PDB:7CFM, ECO:0007744|PDB:7CFN, ECO:0007744|PDB:7XTQ"; TRANSMEM 262..283; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:32698187, ECO:0000269|PubMed:32747649, ECO:0000269|PubMed:35858343, ECO:0007744|PDB:7BW0, ECO:0007744|PDB:7CFM, ECO:0007744|PDB:7CFN, ECO:0007744|PDB:7XTQ
uniprot
proteins