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   27-MAR-2024, entry version 133.
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; 10090-ENSMUSP00000060591; -.
DR   Antibodypedia; 30179; 292 antibodies from 34 providers.
DR   DNASU; 236781; -.
DR   Ensembl; ENSMUST00000053970.4; ENSMUSP00000060591.4; ENSMUSG00000051209.4.
DR   GeneID; 236781; -.
DR   KEGG; mmu:236781; -.
DR   UCSC; uc009tcs.1; mouse.
DR   AGR; MGI:2668412; -.
DR   CTD; 139760; -.
DR   MGI; MGI:2668412; Gpr119.
DR   VEuPathDB; HostDB:ENSMUSG00000051209; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01060000248564; -.
DR   HOGENOM; CLU_009579_11_5_1; -.
DR   InParanoid; Q7TQP3; -.
DR   OMA; IFQQTTY; -.
DR   OrthoDB; 2913811at2759; -.
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 77 CRISPR screens.
DR   PRO; PR:Q7TQP3; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q7TQP3; Protein.
DR   Bgee; ENSMUSG00000051209; Expressed in mesodermal cell in embryo and 3 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   CDD; cd15104; 7tmA_GPR119_R_insulinotropic_receptor; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR028336; GPR119.
DR   PANTHER; PTHR22750; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR22750:SF7; GLUCOSE-DEPENDENT INSULINOTROPIC RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
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
//