ID O3FA1_HUMAN Reviewed; 377 AA. AC Q5NUL3; Q495H1; Q5VY25; Q5VY26; Q7Z605; Q86SM7; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 2. DT 31-MAY-2011, entry version 61. DE RecName: Full=Omega-3 fatty acid receptor 1; DE AltName: Full=G-protein coupled receptor 120; DE AltName: Full=G-protein coupled receptor 129; DE AltName: Full=G-protein coupled receptor GT01; DE AltName: Full=G-protein coupled receptor PGR4; GN Name=O3FAR1; Synonyms=GPR120, GPR129, PGR4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX MEDLINE=22985413; PubMed=14623098; DOI=10.1016/S0014-5793(03)01196-7; RA Fredriksson R., Hoeglund P.J., Gloriam D.E.I., Lagerstroem M.C., RA Schioeth H.B.; RT "Seven evolutionarily conserved human rhodopsin G protein-coupled RT receptors lacking close relatives."; RL FEBS Lett. 554:381-388(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND RP FUNCTION. RX PubMed=15619630; DOI=10.1038/nm1168; RA Hirasawa A., Tsumaya K., Awaji T., Katsuma S., Adachi T., Yamada M., RA Sugimoto Y., Miyazaki S., Tsujimoto G.; RT "Free fatty acids regulate gut incretin glucagon-like peptide-1 RT secretion through GPR120."; RL Nat. Med. 11:90-94(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-312 (ISOFORM 2). RX MEDLINE=22584407; PubMed=12679517; DOI=10.1073/pnas.0230374100; RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E., RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C., RA Bergmann J.E., Gaitanaris G.A.; RT "The G protein-coupled receptor repertoires of human and mouse."; RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003). RN [7] RP PHOSPHORYLATION. RX PubMed=20471368; DOI=10.1016/j.bbrc.2010.05.057; RA Burns R.N., Moniri N.H.; RT "Agonism with the omega-3 fatty acids alpha-linolenic acid and RT docosahexaenoic acid mediates phosphorylation of both the short and RT long isoforms of the human GPR120 receptor."; RL Biochem. Biophys. Res. Commun. 396:1030-1035(2010). CC -!- FUNCTION: Receptor for medium and long-chain free fatty acid CC (FAA). Signals via a G(q)/G(11)-coupled pathway. Acts as a CC receptor for omega-3 fatty acids and mediates robust anti- CC inflammatory effects particulary in macrophages and fat cells. The CC anti-inflammatory effects involve inhibition of TAK1 through a CC beta-arrestin 2 (ARRB2)/TAB1 dependent effect but independent of CC G(q)/G(11)-coupled pathway. Mediates potent insulin sensitizing CC and antidiabetic effects by repressing macrophage-induced tissue CC inflammation. May mediates the taste of fatty acids (By CC similarity). CC -!- SUBUNIT: Interacts with ARRB2 following docosahexaenoic acid (DHA) CC stimulation (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein CC (By similarity). Note=Colocalized with ARRB2 following DHA CC treatment (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5NUL3-1; Sequence=Displayed; CC Note=Specific to human; CC Name=2; CC IsoId=Q5NUL3-2; Sequence=VSP_013684; CC -!- TISSUE SPECIFICITY: Abundant expression in the intestinal tract. CC -!- PTM: Phosphorylated. FFA stimulation facilitates phosphorylation. CC -!- MISCELLANEOUS: It has been shown that FFA alpha-linolenic acid CC stimulate secretion of glucagon-like peptide 1 (GLP-1) from the CC gastro-intestinal tract (PubMed:15619630). However this ligand is CC an agonist of both GPR120 and FFA1 and the latter has been shown CC to mediate GLP-1 release too (PubMed:18519800). So the precise CC role of GPR120 in mediating needs to be confirmed. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY288417; AAP72126.1; -; mRNA. DR EMBL; AB115768; BAD83368.1; -; mRNA. DR EMBL; AL356214; CAH72326.1; -; Genomic_DNA. DR EMBL; AL356214; CAH72327.1; -; Genomic_DNA. DR EMBL; CH471066; EAW50069.1; -; Genomic_DNA. DR EMBL; BC101175; AAI01176.1; -; mRNA. DR EMBL; AY255573; AAO85085.1; -; mRNA. DR IPI; IPI00376213; -. DR IPI; IPI00383963; -. DR RefSeq; NP_001182684.1; NM_001195755.1. DR RefSeq; NP_859529.2; NM_181745.3. DR UniGene; Hs.661022; -. DR ProteinModelPortal; Q5NUL3; -. DR SMR; Q5NUL3; 123-154. DR STRING; Q5NUL3; -. DR PRIDE; Q5NUL3; -. DR Ensembl; ENST00000371483; ENSP00000360538; ENSG00000186188. DR GeneID; 338557; -. DR KEGG; hsa:338557; -. DR UCSC; uc001kir.1; human. DR UCSC; uc001kis.1; human. DR CTD; 338557; -. DR GeneCards; GC10P088954; -. DR H-InvDB; HIX0035308; -. DR HGNC; HGNC:19061; O3FAR1. DR MIM; 609044; gene. DR neXtProt; NX_Q5NUL3; -. DR PharmGKB; PA134924595; -. DR GeneTree; ENSGT00390000009371; -. DR HOGENOM; HBG268165; -. DR HOVERGEN; HBG051775; -. DR InParanoid; Q5NUL3; -. DR OMA; VIWPSLF; -. DR PhylomeDB; Q5NUL3; -. DR Reactome; REACT_14797; Signaling by GPCR. DR NextBio; 97032; -. DR ArrayExpress; Q5NUL3; -. DR Bgee; Q5NUL3; -. DR CleanEx; HS_GPR120; -. DR Genevestigator; Q5NUL3; -. DR GermOnline; ENSG00000186188; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0005504; F:fatty acid binding; ISS:UniProtKB. DR GO; GO:0050710; P:negative regulation of cytokine secretion; ISS:UniProtKB. DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB. DR GO; GO:0010827; P:regulation of glucose transport; ISS:UniProtKB. DR InterPro; IPR000276; 7TM_GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_supfam. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Complete proteome; KW G-protein coupled receptor; Glycoprotein; Lipid-binding; Membrane; KW Phosphoprotein; Receptor; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1 377 Omega-3 fatty acid receptor 1. FT /FTId=PRO_0000069610. FT TOPO_DOM 1 45 Extracellular (Potential). FT TRANSMEM 46 66 Helical; Name=1; (Potential). FT TOPO_DOM 67 77 Cytoplasmic (Potential). FT TRANSMEM 78 98 Helical; Name=2; (Potential). FT TOPO_DOM 99 112 Extracellular (Potential). FT TRANSMEM 113 133 Helical; Name=3; (Potential). FT TOPO_DOM 134 156 Cytoplasmic (Potential). FT TRANSMEM 157 177 Helical; Name=4; (Potential). FT TOPO_DOM 178 204 Extracellular (Potential). FT TRANSMEM 205 225 Helical; Name=5; (Potential). FT TOPO_DOM 226 284 Cytoplasmic (Potential). FT TRANSMEM 285 305 Helical; Name=6; (Potential). FT TOPO_DOM 306 311 Extracellular (Potential). FT TRANSMEM 312 332 Helical; Name=7; (Potential). FT TOPO_DOM 333 377 Cytoplasmic (Potential). FT COMPBIAS 67 71 Poly-Arg. FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 233 248 Missing (in isoform 2). FT /FTId=VSP_013684. FT CONFLICT 67 67 R -> C (in Ref. 2; BAD83368). FT CONFLICT 67 67 Missing (in Ref. 1; AAP72126). FT CONFLICT 274 274 Q -> H (in Ref. 2; BAD83368). FT CONFLICT 297 297 I -> T (in Ref. 2; BAD83368). SQ SEQUENCE 377 AA; 42241 MW; 28BB8C3A939A7EFF CRC64; MSPECARAAG DAPLRSLEQA NRTRFPFFSD VKGDHRLVLA AVETTVLVLI FAVSLLGNVC ALVLVARRRR RGATACLVLN LFCADLLFIS AIPLVLAVRW TEAWLLGPVA CHLLFYVMTL SGSVTILTLA AVSLERMVCI VHLQRGVRGP GRRARAVLLA LIWGYSAVAA LPLCVFFRVV PQRLPGADQE ISICTLIWPT IPGEISWDVS FVTLNFLVPG LVIVISYSKI LQTSEHLLDA RAVVTHSEIT KASRKRLTVS LAYSESHQIR VSQQDFRLFR TLFLLMVSFF IMWSPIIITI LLILIQNFKQ DLVIWPSLFF WVVAFTFANS ALNPILYNMT LCRNEWKKIF CCFWFPEKGA ILTDTSVKRN DLSIISG //