FFAR1_MACFA
ID FFAR1_MACFA Reviewed; 300 AA.
AC Q76JV1;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Free fatty acid receptor 1;
DE AltName: Full=G-protein coupled receptor 40;
GN Name=FFAR1; Synonyms=GPR40;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12629551; DOI=10.1038/nature01478;
RA Itoh Y., Kawamata Y., Harada M., Kobayashi M., Fujii R., Fukusumi S.,
RA Ogi K., Hosoya M., Tanaka Y., Uejima H., Tanaka H., Maruyama M., Satoh R.,
RA Okubo S., Kizawa H., Komatsu H., Matsumura F., Noguchi Y., Shinohara T.,
RA Hinuma S., Fujisawa Y., Fujino M.;
RT "Free fatty acids regulate insulin secretion from pancreatic beta cells
RT through GPR40.";
RL Nature 422:173-176(2003).
CC -!- FUNCTION: G-protein coupled receptor for medium and long chain
CC saturated and unsaturated fatty acids that plays an important role in
CC glucose homeostasis. Fatty acid binding increases glucose-stimulated
CC insulin secretion, and may also enhance the secretion of glucagon-like
CC peptide 1 (GLP-1). May also play a role in bone homeostasis; receptor
CC signaling activates pathways that inhibit osteoclast differentiation.
CC Ligand binding leads to a conformation change that triggers signaling
CC via G-proteins that activate phospholipase C, leading to an increase of
CC the intracellular calcium concentration. Seems to act through a G(q)
CC and G(i)-mediated pathway. Mediates the anti-inflammatory effects of
CC omega-3 polyunsaturated fatty acids (PUFAs) via inhibition of NLRP3
CC inflammasome activation. {ECO:0000250|UniProtKB:O14842,
CC ECO:0000250|UniProtKB:Q76JU9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14842};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O14842}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB095743; BAC82553.1; -; Genomic_DNA.
DR RefSeq; XP_005588904.1; XM_005588847.2.
DR AlphaFoldDB; Q76JV1; -.
DR SMR; Q76JV1; -.
DR STRING; 9541.XP_005588904.1; -.
DR BindingDB; Q76JV1; -.
DR ChEMBL; CHEMBL3751659; -.
DR GeneID; 102132618; -.
DR KEGG; mcf:102132618; -.
DR CTD; 2864; -.
DR VEuPathDB; HostDB:ENSMFAG00000014904; -.
DR eggNOG; ENOG502QVCS; Eukaryota.
DR OMA; CWRKLGL; -.
DR OrthoDB; 1074213at2759; -.
DR Proteomes; UP000233100; Chromosome 19.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045125; F:bioactive lipid receptor activity; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0070542; P:response to fatty acid; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR013312; GPR40-rel_orph.
DR InterPro; IPR013313; GPR40_recept_FA.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01905; FATTYACIDR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01904; GPR40FAMILY.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..300
FT /note="Free fatty acid receptor 1"
FT /id="PRO_0000069568"
FT TOPO_DOM 1..8
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TRANSMEM 9..31
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TOPO_DOM 32..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TRANSMEM 42..64
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TOPO_DOM 65..79
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TRANSMEM 80..101
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TOPO_DOM 102..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TOPO_DOM 143..178
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TRANSMEM 179..200
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TOPO_DOM 201..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TRANSMEM 224..248
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TOPO_DOM 249..256
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TRANSMEM 257..279
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT TOPO_DOM 280..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O14842, ECO:0000255"
FT SITE 145
FT /note="Important for receptor activation"
FT /evidence="ECO:0000250|UniProtKB:O14842"
FT SITE 172
FT /note="Important for receptor activation"
FT /evidence="ECO:0000250|UniProtKB:O14842"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 79..170
FT /evidence="ECO:0000250|UniProtKB:O14842"
SQ SEQUENCE 300 AA; 31456 MW; EF7DC145ECCA22B4 CRC64;
MDLPPQLSFA LYVAAFALGF PLNVLAIRGA RAHARRRLTP SLVYALNLGC SDLLLTVSLP
LKAVEALASG AWPLPASLCP VFGVAHFAPL YAGGGFLAAL SAGRYLGAAF PLGYQAFRRP
CYSWGVCAAI WALVLCHLGL VFVLEAPGGW LDHSNTSLGI NTPVNGSPVC LEAWDPASAG
PARFSLSLLL FFLPLAITAF CYVGCLRALA HSGLTHRRKL RAAWVAGGAL LTLLLCVGPY
NASNVASFLN PNLGGSWRKL GLITGAWSVV LNPLVTGYLG RGPGLKTVCA ARTQGSTSQK
