GP119_HUMAN
ID GP119_HUMAN Reviewed; 335 AA.
AC Q8TDV5; Q495H7; Q4VBN3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Glucose-dependent insulinotropic receptor;
DE AltName: Full=G-protein coupled receptor 119;
GN Name=GPR119;
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 [LARGE SCALE GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX 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 receptors
RT lacking close relatives.";
RL FEBS Lett. 554:381-388(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [6]
RP TISSUE SPECIFICITY, AND CHARACTERIZATION.
RX PubMed=15607732; DOI=10.1016/j.bbrc.2004.11.120;
RA Soga T., Ohishi T., Matsui T., Saito T., Matsumoto M., Takasaki J.,
RA Matsumoto S., Kamohara M., Hiyama H., Yoshida S., Momose K., Ueda Y.,
RA Matsushime H., Kobori M., Furuichi K.;
RT "Lysophosphatidylcholine enhances glucose-dependent insulin secretion via
RT an orphan G-protein-coupled receptor.";
RL Biochem. Biophys. Res. Commun. 326:744-751(2005).
RN [7]
RP LIGAND-BINDING, AND FUNCTION.
RX PubMed=16517404; DOI=10.1016/j.cmet.2006.02.004;
RA Overton H.A., Babbs A.J., Doel S.M., Fyfe M.C.T., Gardner L.S., Griffin G.,
RA Jackson H.C., Procter M.J., Rasamison C.M., Tang-Christensen M.,
RA Widdowson P.S., Williams G.M., Reynet C.;
RT "Deorphanization of a G protein-coupled receptor for oleoylethanolamide and
RT its use in the discovery of small-molecule hypophagic agents.";
RL Cell Metab. 3:167-175(2006).
CC -!- FUNCTION: Receptor for the endogenous fatty-acid ethanolamide
CC oleoylethanolamide (OEA) and lysophosphatidylcholine (LPC). Functions
CC as a glucose-dependent insulinotropic receptor. The activity of this
CC receptor is mediated by G proteins which activate adenylate cyclase.
CC Seems to act through a G(s) mediated pathway.
CC {ECO:0000269|PubMed:16517404}.
CC -!- INTERACTION:
CC Q8TDV5; Q12797-6: ASPH; NbExp=3; IntAct=EBI-17253531, EBI-12092171;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the pancreas, especially
CC in the islets. {ECO:0000269|PubMed:15607732}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB083584; BAB89297.1; -; Genomic_DNA.
DR EMBL; AB065936; BAC06151.1; -; Genomic_DNA.
DR EMBL; AY288416; AAP72125.1; -; mRNA.
DR EMBL; AL035423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC095502; AAH95502.1; -; mRNA.
DR EMBL; BC101166; AAI01167.1; -; mRNA.
DR EMBL; BC101167; AAI01168.1; -; mRNA.
DR EMBL; BC101168; AAI01169.1; -; mRNA.
DR EMBL; BC126179; AAI26180.1; -; mRNA.
DR EMBL; BC126181; AAI26182.1; -; mRNA.
DR CCDS; CCDS14625.1; -.
DR RefSeq; NP_848566.1; NM_178471.2.
DR AlphaFoldDB; Q8TDV5; -.
DR SMR; Q8TDV5; -.
DR BioGRID; 126586; 5.
DR IntAct; Q8TDV5; 1.
DR STRING; 9606.ENSP00000276218; -.
DR BindingDB; Q8TDV5; -.
DR ChEMBL; CHEMBL5652; -.
DR DrugBank; DB05166; APD668.
DR GuidetoPHARMACOLOGY; 126; -.
DR iPTMnet; Q8TDV5; -.
DR PhosphoSitePlus; Q8TDV5; -.
DR BioMuta; GPR119; -.
DR DMDM; 62510696; -.
DR jPOST; Q8TDV5; -.
DR PaxDb; Q8TDV5; -.
DR PeptideAtlas; Q8TDV5; -.
DR PRIDE; Q8TDV5; -.
DR ProteomicsDB; 74344; -.
DR Antibodypedia; 30179; 273 antibodies from 33 providers.
DR DNASU; 139760; -.
DR Ensembl; ENST00000276218.4; ENSP00000276218.2; ENSG00000147262.5.
DR Ensembl; ENST00000682440.1; ENSP00000508182.1; ENSG00000147262.5.
DR GeneID; 139760; -.
DR KEGG; hsa:139760; -.
DR MANE-Select; ENST00000682440.1; ENSP00000508182.1; NM_178471.3; NP_848566.1.
DR UCSC; uc011muv.3; human.
DR CTD; 139760; -.
DR DisGeNET; 139760; -.
DR GeneCards; GPR119; -.
DR HGNC; HGNC:19060; GPR119.
DR HPA; ENSG00000147262; Tissue enriched (pancreas).
DR MIM; 300513; gene.
DR neXtProt; NX_Q8TDV5; -.
DR OpenTargets; ENSG00000147262; -.
DR PharmGKB; PA134928131; -.
DR VEuPathDB; HostDB:ENSG00000147262; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_11_5_1; -.
DR InParanoid; Q8TDV5; -.
DR OMA; HLAIRKP; -.
DR OrthoDB; 1245021at2759; -.
DR PhylomeDB; Q8TDV5; -.
DR TreeFam; TF325411; -.
DR PathwayCommons; Q8TDV5; -.
DR Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-HSA-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
DR SignaLink; Q8TDV5; -.
DR SIGNOR; Q8TDV5; -.
DR BioGRID-ORCS; 139760; 9 hits in 697 CRISPR screens.
DR GeneWiki; GPR119; -.
DR GenomeRNAi; 139760; -.
DR Pharos; Q8TDV5; Tchem.
DR PRO; PR:Q8TDV5; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8TDV5; protein.
DR Bgee; ENSG00000147262; Expressed in islet of Langerhans and 10 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR028336; GPR119.
DR PANTHER; PTHR22750:SF7; PTHR22750:SF7; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; G-protein coupled receptor; Lipid-binding; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..335
FT /note="Glucose-dependent insulinotropic receptor"
FT /id="PRO_0000069607"
FT TOPO_DOM 1..12
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..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..164
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VARIANT 309
FT /note="S -> L (in dbSNP:rs5975187)"
FT /id="VAR_037221"
FT CONFLICT 325
FT /note="I -> T (in Ref. 5; AAI01167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 36889 MW; 16BAF93AEA145FB0 CRC64;
MESSFSFGVI LAVLASLIIA TNTLVAVAVL LLIHKNDGVS LCFTLNLAVA DTLIGVAISG
LLTDQLSSPS RPTQKTLCSL RMAFVTSSAA ASVLTVMLIT FDRYLAIKQP FRYLKIMSGF
VAGACIAGLW LVSYLIGFLP LGIPMFQQTA YKGQCSFFAV FHPHFVLTLS CVGFFPAMLL
FVFFYCDMLK IASMHSQQIR KMEHAGAMAG GYRSPRTPSD FKALRTVSVL IGSFALSWTP
FLITGIVQVA CQECHLYLVL ERYLWLLGVG NSLLNPLIYA YWQKEVRLQL YHMALGVKKV
LTSFLLFLSA RNCGPERPRE SSCHIVTISS SEFDG
