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Protein

Glucose-dependent insulinotropic receptor

Gene

GPR119

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for the endogenous fatty-acid ethanolamide oleoylethanolamide (OEA) and lysophosphatidylcholine (LPC). Functions as a glucose-dependent insulinotropic receptor. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Seems to act through a G(s) mediated pathway.1 Publication

GO - Molecular functioni

  1. G-protein coupled receptor activity Source: UniProtKB-KW
  2. phosphatidylcholine binding Source: Ensembl

GO - Biological processi

  1. insulin secretion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_23824. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-dependent insulinotropic receptor
Alternative name(s):
G-protein coupled receptor 119
Gene namesi
Name:GPR119
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:19060. GPR119.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212ExtracellularSequence AnalysisAdd
BLAST
Transmembranei13 – 3321Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini34 – 374CytoplasmicSequence Analysis
Transmembranei38 – 5821Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini59 – 8123ExtracellularSequence AnalysisAdd
BLAST
Transmembranei82 – 10221Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini103 – 12523CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei126 – 14621Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini147 – 16418ExtracellularSequence AnalysisAdd
BLAST
Transmembranei165 – 18521Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini186 – 22641CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei227 – 24721Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini248 – 26215ExtracellularSequence AnalysisAdd
BLAST
Transmembranei263 – 28321Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini284 – 33552CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
  3. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134928131.

Polymorphism and mutation databases

BioMutaiGPR119.
DMDMi62510696.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 335335Glucose-dependent insulinotropic receptorPRO_0000069607Add
BLAST

Proteomic databases

PaxDbiQ8TDV5.
PRIDEiQ8TDV5.

PTM databases

PhosphoSiteiQ8TDV5.

Expressioni

Tissue specificityi

Predominantly expressed in the pancreas, especially in the islets.1 Publication

Gene expression databases

BgeeiQ8TDV5.
CleanExiHS_GPR119.
GenevestigatoriQ8TDV5.

Interactioni

Protein-protein interaction databases

BioGridi126586. 2 interactions.
STRINGi9606.ENSP00000276218.

Structurei

3D structure databases

ProteinModelPortaliQ8TDV5.
SMRiQ8TDV5. Positions 1-287.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG246868.
GeneTreeiENSGT00550000074524.
HOGENOMiHOG000112765.
HOVERGENiHBG051773.
InParanoidiQ8TDV5.
KOiK08424.
OMAiSFFAVFH.
OrthoDBiEOG75B85V.
PhylomeDBiQ8TDV5.
TreeFamiTF325411.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR028336. GPR119.
[Graphical view]
PANTHERiPTHR22750:SF7. PTHR22750:SF7. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8TDV5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESSFSFGVI LAVLASLIIA TNTLVAVAVL LLIHKNDGVS LCFTLNLAVA
60 70 80 90 100
DTLIGVAISG LLTDQLSSPS RPTQKTLCSL RMAFVTSSAA ASVLTVMLIT
110 120 130 140 150
FDRYLAIKQP FRYLKIMSGF VAGACIAGLW LVSYLIGFLP LGIPMFQQTA
160 170 180 190 200
YKGQCSFFAV FHPHFVLTLS CVGFFPAMLL FVFFYCDMLK IASMHSQQIR
210 220 230 240 250
KMEHAGAMAG GYRSPRTPSD FKALRTVSVL IGSFALSWTP FLITGIVQVA
260 270 280 290 300
CQECHLYLVL ERYLWLLGVG NSLLNPLIYA YWQKEVRLQL YHMALGVKKV
310 320 330
LTSFLLFLSA RNCGPERPRE SSCHIVTISS SEFDG
Length:335
Mass (Da):36,889
Last modified:June 1, 2002 - v1
Checksum:i16BAF93AEA145FB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti325 – 3251I → T in AAI01167 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti309 – 3091S → L.
Corresponds to variant rs5975187 [ dbSNP | Ensembl ].
VAR_037221

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB083584 Genomic DNA. Translation: BAB89297.1.
AB065936 Genomic DNA. Translation: BAC06151.1.
AY288416 mRNA. Translation: AAP72125.1.
AL035423 Genomic DNA. Translation: CAI42442.1.
BC095502 mRNA. Translation: AAH95502.1.
BC101166 mRNA. Translation: AAI01167.1.
BC101167 mRNA. Translation: AAI01168.1.
BC101168 mRNA. Translation: AAI01169.1.
BC126179 mRNA. Translation: AAI26180.1.
BC126181 mRNA. Translation: AAI26182.1.
CCDSiCCDS14625.1.
RefSeqiNP_848566.1. NM_178471.2.
UniGeneiHs.496762.

Genome annotation databases

EnsembliENST00000276218; ENSP00000276218; ENSG00000147262.
GeneIDi139760.
KEGGihsa:139760.
UCSCiuc011muv.2. human.

Polymorphism and mutation databases

BioMutaiGPR119.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB083584 Genomic DNA. Translation: BAB89297.1.
AB065936 Genomic DNA. Translation: BAC06151.1.
AY288416 mRNA. Translation: AAP72125.1.
AL035423 Genomic DNA. Translation: CAI42442.1.
BC095502 mRNA. Translation: AAH95502.1.
BC101166 mRNA. Translation: AAI01167.1.
BC101167 mRNA. Translation: AAI01168.1.
BC101168 mRNA. Translation: AAI01169.1.
BC126179 mRNA. Translation: AAI26180.1.
BC126181 mRNA. Translation: AAI26182.1.
CCDSiCCDS14625.1.
RefSeqiNP_848566.1. NM_178471.2.
UniGeneiHs.496762.

3D structure databases

ProteinModelPortaliQ8TDV5.
SMRiQ8TDV5. Positions 1-287.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126586. 2 interactions.
STRINGi9606.ENSP00000276218.

Chemistry

BindingDBiQ8TDV5.
ChEMBLiCHEMBL5652.
GuidetoPHARMACOLOGYi126.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiQ8TDV5.

Polymorphism and mutation databases

BioMutaiGPR119.
DMDMi62510696.

Proteomic databases

PaxDbiQ8TDV5.
PRIDEiQ8TDV5.

Protocols and materials databases

DNASUi139760.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000276218; ENSP00000276218; ENSG00000147262.
GeneIDi139760.
KEGGihsa:139760.
UCSCiuc011muv.2. human.

Organism-specific databases

CTDi139760.
GeneCardsiGC0XM129518.
HGNCiHGNC:19060. GPR119.
MIMi300513. gene.
neXtProtiNX_Q8TDV5.
PharmGKBiPA134928131.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG246868.
GeneTreeiENSGT00550000074524.
HOGENOMiHOG000112765.
HOVERGENiHBG051773.
InParanoidiQ8TDV5.
KOiK08424.
OMAiSFFAVFH.
OrthoDBiEOG75B85V.
PhylomeDBiQ8TDV5.
TreeFamiTF325411.

Enzyme and pathway databases

ReactomeiREACT_23824. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).

Miscellaneous databases

GeneWikiiGPR119.
GenomeRNAii139760.
NextBioi84036.
PROiQ8TDV5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TDV5.
CleanExiHS_GPR119.
GenevestigatoriQ8TDV5.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR028336. GPR119.
[Graphical view]
PANTHERiPTHR22750:SF7. PTHR22750:SF7. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of G protein-coupled receptor genes from the human genome sequence."
    Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.
    FEBS Lett. 520:97-101(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Genome-wide discovery and analysis of human seven transmembrane helix receptor genes."
    Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Seven evolutionarily conserved human rhodopsin G protein-coupled receptors lacking close relatives."
    Fredriksson R., Hoeglund P.J., Gloriam D.E.I., Lagerstroem M.C., Schioeth H.B.
    FEBS Lett. 554:381-388(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Lysophosphatidylcholine enhances glucose-dependent insulin secretion via an orphan G-protein-coupled receptor."
    Soga T., Ohishi T., Matsui T., Saito T., Matsumoto M., Takasaki J., Matsumoto S., Kamohara M., Hiyama H., Yoshida S., Momose K., Ueda Y., Matsushime H., Kobori M., Furuichi K.
    Biochem. Biophys. Res. Commun. 326:744-751(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, CHARACTERIZATION.
  7. "Deorphanization of a G protein-coupled receptor for oleoylethanolamide and its use in the discovery of small-molecule hypophagic agents."
    Overton H.A., Babbs A.J., Doel S.M., Fyfe M.C.T., Gardner L.S., Griffin G., Jackson H.C., Procter M.J., Rasamison C.M., Tang-Christensen M., Widdowson P.S., Williams G.M., Reynet C.
    Cell Metab. 3:167-175(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIGAND-BINDING, FUNCTION.

Entry informationi

Entry nameiGP119_HUMAN
AccessioniPrimary (citable) accession number: Q8TDV5
Secondary accession number(s): Q495H7, Q4VBN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: June 1, 2002
Last modified: April 29, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.