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Free fatty acid receptor 1 (G-protein coupled receptor 40)

 FFAR1_HUMAN             Reviewed;         300 AA.
O14842; Q0VAS2; Q4VBL4;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 141.
RecName: Full=Free fatty acid receptor 1;
AltName: Full=G-protein coupled receptor 40;
Name=FFAR1; Synonyms=GPR40;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9344866; DOI=10.1006/bbrc.1997.7513;
Sawzdargo M., George S.R., Nguyen T., Xu S., Kolakowski L.F. Jr.,
O'Dowd B.F.;
"A cluster of four novel human G protein-coupled receptor genes
occurring in close proximity to CD22 gene on chromosome 19q13.1.";
Biochem. Biophys. Res. Commun. 239:543-547(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-211.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12496284; DOI=10.1074/jbc.M211495200;
Briscoe C.P., Tadayyon M., Andrews J.L., Benson W.G., Chambers J.K.,
Eilert M.M., Ellis C., Elshourbagy N.A., Goetz A.S., Minnick D.T.,
Murdock P.R., Sauls H.R. Jr., Shabon U., Spinage L.D., Strum J.C.,
Szekeres P.G., Tan K.B., Way J.M., Ignar D.M., Wilson S., Muir A.I.;
"The orphan G protein-coupled receptor GPR40 is activated by medium
and long-chain fatty acids.";
J. Biol. Chem. 278:11303-11311(2003).
[4]
TISSUE SPECIFICITY.
PubMed=16289108; DOI=10.1016/j.bbrc.2005.10.161;
Tomita T., Masuzaki H., Noguchi M., Iwakura H., Fujikura J.,
Tanaka T., Ebihara K., Kawamura J., Komoto I., Kawaguchi Y.,
Fujimoto K., Doi R., Shimada Y., Hosoda K., Imamura M., Nakao K.;
"GPR40 gene expression in human pancreas and insulinoma.";
Biochem. Biophys. Res. Commun. 338:1788-1790(2005).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-12; TYR-91;
HIS-137; ARG-183; TYR-240; ASN-244 AND ARG-258.
PubMed=17699519; DOI=10.1074/jbc.M705077200;
Sum C.S., Tikhonova I.G., Neumann S., Engel S., Raaka B.M.,
Costanzi S., Gershengorn M.C.;
"Identification of residues important for agonist recognition and
activation in GPR40.";
J. Biol. Chem. 282:29248-29255(2007).
[6]
FUNCTION, MUTAGENESIS OF GLU-145 AND GLU-172, AND SITE.
PubMed=19068482; DOI=10.1074/jbc.M806987200;
Sum C.S., Tikhonova I.G., Costanzi S., Gershengorn M.C.;
"Two arginine-glutamate ionic locks near the extracellular surface of
FFAR1 gate receptor activation.";
J. Biol. Chem. 284:3529-3536(2009).
[7]
FUNCTION, AND ENZYME REGULATION.
PubMed=21570468; DOI=10.1016/j.nbd.2011.04.020;
Kruska N., Reiser G.;
"Phytanic acid and pristanic acid, branched-chain fatty acids
associated with Refsum disease and other inherited peroxisomal
disorders, mediate intracellular Ca2+ signaling through activation of
free fatty acid receptor GPR40.";
Neurobiol. Dis. 43:465-472(2011).
[8]
FUNCTION, AND ENZYME REGULATION.
PubMed=24130766; DOI=10.1371/journal.pone.0076280;
Yabuki C., Komatsu H., Tsujihata Y., Maeda R., Ito R.,
Matsuda-Nagasumi K., Sakuma K., Miyawaki K., Kikuchi N., Takeuchi K.,
Habata Y., Mori M.;
"A novel antidiabetic drug, fasiglifam/TAK-875, acts as an ago-
allosteric modulator of FFAR1.";
PLoS ONE 8:E76280-E76280(2013).
[9]
X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 1-211 AND 214-300 IN COMPLEX
WITH THE AGONIST TAK-875, AGONIST BINDING SITES, SUBCELLULAR LOCATION,
TOPOLOGY, DISULFIDE BOND, AND MUTAGENESIS OF TYR-91; ARG-183; TYR-240;
ASN-244 AND ARG-258.
PubMed=25043059; DOI=10.1038/nature13494;
Srivastava A., Yano J., Hirozane Y., Kefala G., Gruswitz F., Snell G.,
Lane W., Ivetac A., Aertgeerts K., Nguyen J., Jennings A., Okada K.;
"High-resolution structure of the human GPR40 receptor bound to
allosteric agonist TAK-875.";
Nature 513:124-127(2014).
-!- FUNCTION: G-protein coupled receptor for medium and long chain
saturated and unsaturated fatty acids that plays an important role
in glucose homeostasis. Fatty acid binding increases glucose-
stimulated insulin secretion, and may also enhance the secretion
of glucagon-like peptide 1 (GLP-1). May also play a role in bone
homeostasis; receptor signaling activates pathways that inhibit
osteoclast differentiation (By similarity). Ligand binding leads
to a conformation change that triggers signaling via G-proteins
that activate phospholipase C, leading to an increase of the
intracellular calcium concentration. Seems to act through a G(q)
and G(i)-mediated pathway. {ECO:0000250|UniProtKB:Q76JU9,
ECO:0000269|PubMed:12496284, ECO:0000269|PubMed:17699519,
ECO:0000269|PubMed:24130766}.
-!- ENZYME REGULATION: The receptor is strongly activated by gamma-
linolenic acid, while myristate gives a lower response. It is also
activated by phytanic acid and pristanic acid (PubMed:21570468).
Is also activated by synthetic agonists, such as TAK-875
(fasiglifam); this compound is a partial agonist and potentiates
the activity of the endogenous ligand gamma-linolenic acid
(PubMed:24130766). {ECO:0000269|PubMed:21570468,
ECO:0000269|PubMed:24130766}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17699519,
ECO:0000269|PubMed:25043059}; Multi-pass membrane protein
{ECO:0000269|PubMed:25043059}.
-!- TISSUE SPECIFICITY: Detected in brain and pancreas. Detected in
pancreatic beta cells. {ECO:0000269|PubMed:12496284,
ECO:0000269|PubMed:16289108}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-----------------------------------------------------------------------
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EMBL; AF024687; AAB86710.1; -; Genomic_DNA.
EMBL; BC095536; AAH95536.1; -; mRNA.
EMBL; BC120944; AAI20945.1; -; mRNA.
CCDS; CCDS12458.1; -.
PIR; JC5714; JC5714.
RefSeq; NP_005294.1; NM_005303.2.
UniGene; Hs.248127; -.
PDB; 4PHU; X-ray; 2.33 A; A=1-211, A=214-300.
PDB; 5TZR; X-ray; 2.20 A; A=1-211, A=214-300.
PDB; 5TZY; X-ray; 3.22 A; A=1-211, A=214-300.
PDBsum; 4PHU; -.
PDBsum; 5TZR; -.
PDBsum; 5TZY; -.
ProteinModelPortal; O14842; -.
SMR; O14842; -.
STRING; 9606.ENSP00000246553; -.
BindingDB; O14842; -.
ChEMBL; CHEMBL4422; -.
DrugBank; DB00159; Icosapent.
GuidetoPHARMACOLOGY; 225; -.
SwissLipids; SLP:000001550; -.
iPTMnet; O14842; -.
PhosphoSitePlus; O14842; -.
BioMuta; FFAR1; -.
PaxDb; O14842; -.
PRIDE; O14842; -.
TopDownProteomics; O14842; -.
DNASU; 2864; -.
Ensembl; ENST00000246553; ENSP00000246553; ENSG00000126266.
GeneID; 2864; -.
KEGG; hsa:2864; -.
UCSC; uc002nzc.3; human.
CTD; 2864; -.
DisGeNET; 2864; -.
EuPathDB; HostDB:ENSG00000126266.3; -.
GeneCards; FFAR1; -.
HGNC; HGNC:4498; FFAR1.
MIM; 603820; gene.
neXtProt; NX_O14842; -.
OpenTargets; ENSG00000126266; -.
PharmGKB; PA28887; -.
eggNOG; ENOG410IV8D; Eukaryota.
eggNOG; ENOG4111572; LUCA.
GeneTree; ENSGT00900000140951; -.
HOGENOM; HOG000236290; -.
HOVERGEN; HBG080696; -.
InParanoid; O14842; -.
KO; K04325; -.
OMA; LHLGCSD; -.
OrthoDB; EOG091G0HSS; -.
PhylomeDB; O14842; -.
TreeFam; TF350010; -.
Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
Reactome; R-HSA-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
Reactome; R-HSA-444209; Free fatty acid receptors.
SIGNOR; O14842; -.
GeneWiki; Free_fatty_acid_receptor_1; -.
GenomeRNAi; 2864; -.
PRO; PR:O14842; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000126266; -.
CleanEx; HS_FFAR1; -.
Genevisible; O14842; HS.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045125; F:bioactive lipid receptor activity; IDA:UniProtKB.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:UniProtKB.
GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
GO; GO:0070542; P:response to fatty acid; IDA:UniProtKB.
CDD; cd15169; 7tmA_FFAR1; 1.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR013312; GPR40-rel_orph.
InterPro; IPR013313; GPR40_recept_FA.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR01905; FATTYACIDR.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR01904; GPR40FAMILY.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Lipid-binding; Membrane;
Polymorphism; Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 300 Free fatty acid receptor 1.
/FTId=PRO_0000069567.
TOPO_DOM 1 8 Extracellular. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TRANSMEM 9 31 Helical; Name=1. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TOPO_DOM 32 41 Cytoplasmic. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TRANSMEM 42 64 Helical; Name=2. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TOPO_DOM 65 79 Extracellular. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TRANSMEM 80 101 Helical; Name=3. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TOPO_DOM 102 121 Cytoplasmic. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TRANSMEM 122 142 Helical; Name=4. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TOPO_DOM 143 178 Extracellular. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TRANSMEM 179 200 Helical; Name=5. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TOPO_DOM 201 223 Cytoplasmic. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TRANSMEM 224 248 Helical; Name=6. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TOPO_DOM 249 256 Extracellular. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TRANSMEM 257 279 Helical; Name=7. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
TOPO_DOM 280 300 Cytoplasmic. {ECO:0000255,
ECO:0000269|PubMed:25043059}.
REGION 87 91 Agonist binding.
{ECO:0000269|PubMed:25043059}.
BINDING 183 183 Agonist. {ECO:0000269|PubMed:25043059}.
BINDING 240 240 Agonist. {ECO:0000269|PubMed:25043059}.
BINDING 258 258 Agonist. {ECO:0000269|PubMed:25043059}.
SITE 145 145 Important for receptor activation.
{ECO:0000269|PubMed:19068482}.
SITE 172 172 Important for receptor activation.
{ECO:0000269|PubMed:19068482}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 79 170 {ECO:0000269|PubMed:25043059}.
VARIANT 211 211 R -> H (in dbSNP:rs2301151).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_020076.
MUTAGEN 12 12 Y->A: Reduces cell surface expression and
response to linolenic acid and synthetic
agonists. {ECO:0000269|PubMed:17699519}.
MUTAGEN 91 91 Y->A: Reduces response to linolenic acid.
Reduces response to synthetic agonists.
{ECO:0000269|PubMed:17699519,
ECO:0000269|PubMed:25043059}.
MUTAGEN 137 137 H->A: Reduces response to linolenic acid.
Reduces response to synthetic agonists.
{ECO:0000269|PubMed:17699519,
ECO:0000269|PubMed:25043059}.
MUTAGEN 145 145 E->A: Constitutive receptor signaling.
{ECO:0000269|PubMed:19068482}.
MUTAGEN 172 172 E->A: Constitutive receptor signaling.
{ECO:0000269|PubMed:19068482}.
MUTAGEN 183 183 R->A: Reduces response to linolenic acid.
Strongly reduces response to synthetic
agonists. {ECO:0000269|PubMed:17699519,
ECO:0000269|PubMed:25043059}.
MUTAGEN 240 240 Y->A: Reduces response to linolenic acid.
Reduces response to synthetic agonists.
{ECO:0000269|PubMed:17699519,
ECO:0000269|PubMed:25043059}.
MUTAGEN 244 244 N->A: Reduces response to linolenic acid.
Reduces response to synthetic agonists.
{ECO:0000269|PubMed:17699519,
ECO:0000269|PubMed:25043059}.
MUTAGEN 258 258 R->A: Strongly reduces response to
linolenic acid. Strongly reduces response
to synthetic agonists.
{ECO:0000269|PubMed:17699519,
ECO:0000269|PubMed:25043059}.
MUTAGEN 258 258 R->K: Reduces response to linolenic acid.
Strongly reduces response to synthetic
agonists. {ECO:0000269|PubMed:17699519}.
CONFLICT 24 24 V -> A (in Ref. 2; AAH95536).
{ECO:0000305}.
HELIX 5 36 {ECO:0000244|PDB:5TZR}.
HELIX 40 67 {ECO:0000244|PDB:5TZR}.
TURN 68 70 {ECO:0000244|PDB:5TZR}.
HELIX 76 78 {ECO:0000244|PDB:5TZR}.
HELIX 79 109 {ECO:0000244|PDB:5TZR}.
HELIX 111 117 {ECO:0000244|PDB:5TZY}.
HELIX 121 145 {ECO:0000244|PDB:5TZR}.
STRAND 149 151 {ECO:0000244|PDB:5TZR}.
STRAND 169 171 {ECO:0000244|PDB:5TZR}.
HELIX 176 190 {ECO:0000244|PDB:5TZR}.
HELIX 192 211 {ECO:0000244|PDB:5TZR}.
HELIX 214 235 {ECO:0000244|PDB:5TZR}.
HELIX 237 249 {ECO:0000244|PDB:5TZR}.
HELIX 256 266 {ECO:0000244|PDB:5TZR}.
HELIX 268 275 {ECO:0000244|PDB:5TZR}.
SEQUENCE 300 AA; 31457 MW; 77EF27DACD93E80B CRC64;
MDLPPQLSFG LYVAAFALGF PLNVLAIRGA TAHARLRLTP SLVYALNLGC SDLLLTVSLP
LKAVEALASG AWPLPASLCP VFAVAHFFPL YAGGGFLAAL SAGRYLGAAF PLGYQAFRRP
CYSWGVCAAI WALVLCHLGL VFGLEAPGGW LDHSNTSLGI NTPVNGSPVC LEAWDPASAG
PARFSLSLLL FFLPLAITAF CYVGCLRALA RSGLTHRRKL RAAWVAGGAL LTLLLCVGPY
NASNVASFLY PNLGGSWRKL GLITGAWSVV LNPLVTGYLG RGPGLKTVCA ARTQGGKSQK


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