GP119_MOUSE
ID GP119_MOUSE Reviewed; 335 AA.
AC Q7TQP3; Q2ABS2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Glucose-dependent insulinotropic receptor;
DE AltName: Full=G-protein coupled receptor 119;
GN Name=Gpr119;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=17070774; DOI=10.1016/j.bbrc.2006.10.076;
RA Sakamoto Y., Inoue H., Kawakami S., Miyawaki K., Miyamoto T., Mizuta K.,
RA Itakura M.;
RT "Expression and distribution of Gpr119 in the pancreatic islets of mice and
RT rats: predominant localization in pancreatic polypeptide-secreting PP-
RT cells.";
RL Biochem. Biophys. Res. Commun. 351:474-480(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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 [5]
RP 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 [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17289847; DOI=10.1210/en.2006-1608;
RA Chu Z.L., Jones R.M., He H., Carroll C., Gutierrez V., Lucman A.,
RA Moloney M., Gao H., Mondala H., Bagnol D., Unett D., Liang Y., Demarest K.,
RA Semple G., Behan D.P., Leonard J.;
RT "A role for beta-cell-expressed G protein-coupled receptor 119 in glycemic
RT control by enhancing glucose-dependent insulin release.";
RL Endocrinology 148:2601-2609(2007).
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:17289847}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expression restricted to the beta-cells of
CC pancreatic islets. {ECO:0000269|PubMed:17070774,
CC ECO:0000269|PubMed:17289847}.
CC -!- INDUCTION: Up-regulated in islets of obese hyperglycemic db/db mice.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY288423; AAP72132.1; -; mRNA.
DR EMBL; AB233291; BAE80212.1; -; mRNA.
DR EMBL; AL672042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115557; AAI15558.1; -; mRNA.
DR EMBL; BC115558; AAI15559.1; -; mRNA.
DR CCDS; CCDS30113.1; -.
DR RefSeq; NP_861416.1; NM_181751.2.
DR AlphaFoldDB; Q7TQP3; -.
DR SMR; Q7TQP3; -.
DR STRING; 10090.ENSMUSP00000060591; -.
DR BindingDB; Q7TQP3; -.
DR ChEMBL; CHEMBL5263; -.
DR iPTMnet; Q7TQP3; -.
DR PhosphoSitePlus; Q7TQP3; -.
DR PaxDb; Q7TQP3; -.
DR PRIDE; Q7TQP3; -.
DR Antibodypedia; 30179; 273 antibodies from 33 providers.
DR DNASU; 236781; -.
DR Ensembl; ENSMUST00000053970; ENSMUSP00000060591; ENSMUSG00000051209.
DR GeneID; 236781; -.
DR KEGG; mmu:236781; -.
DR UCSC; uc009tcs.1; mouse.
DR CTD; 139760; -.
DR MGI; MGI:2668412; Gpr119.
DR VEuPathDB; HostDB:ENSMUSG00000051209; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_11_5_1; -.
DR InParanoid; Q7TQP3; -.
DR OMA; HLAIRKP; -.
DR OrthoDB; 1245021at2759; -.
DR PhylomeDB; Q7TQP3; -.
DR TreeFam; TF325411; -.
DR Reactome; R-MMU-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-MMU-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
DR BioGRID-ORCS; 236781; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q7TQP3; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q7TQP3; protein.
DR Bgee; ENSMUSG00000051209; Expressed in islet of Langerhans and 2 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; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030073; P:insulin secretion; IDA:MGI.
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_0000069608"
FT TOPO_DOM 1..6
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..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"
SQ SEQUENCE 335 AA; 36995 MW; 16AAF4D518A06ECD CRC64;
MESSFSFGVI LAVLTILIIA VNALVVVAML LSIYKNDGVG LCFTLNLAVA DTLIGVAISG
LVTDQLSSSA QHTQKTLCSL RMAFVTSSAA ASVLTVMLIA FDRYLAIKQP LRYFQIMNGL
VAGACIAGLW LVSYLIGFLP LGVSIFQQTT YHGPCSFFAV FHPRFVLTLS CAGFFPAVLL
FVFFYCDMLK IASVHSQQIR KMEHAGAMAG AYRPPRSVND FKAVRTIAVL IGSFTLSWSP
FLITSIVQVA CHKCCLYQVL EKYLWLLGVG NSLLNPLIYA YWQREVRQQL YHMALGVKKF
FTSILLLLPA RNRGPERTRE SAYHIVTISH PELDG
