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GP119_RAT
ID   GP119_RAT               Reviewed;         468 AA.
AC   Q7TQN8;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Glucose-dependent insulinotropic receptor;
DE   AltName: Full=G-protein coupled receptor 119;
GN   Name=Gpr119;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
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   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   [3]
RP   TISSUE SPECIFICITY, AND FUNCTION.
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:15607732,
CC       ECO:0000269|PubMed:17289847}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AY288429; AAP72138.1; -; mRNA.
DR   RefSeq; NP_861435.1; NM_181770.1.
DR   AlphaFoldDB; Q7TQN8; -.
DR   SMR; Q7TQN8; -.
DR   STRING; 10116.ENSRNOP00000036164; -.
DR   BindingDB; Q7TQN8; -.
DR   ChEMBL; CHEMBL5262; -.
DR   PhosphoSitePlus; Q7TQN8; -.
DR   PaxDb; Q7TQN8; -.
DR   Ensembl; ENSRNOT00000033619; ENSRNOP00000036164; ENSRNOG00000024517.
DR   GeneID; 302813; -.
DR   KEGG; rno:302813; -.
DR   UCSC; RGD:727808; rat.
DR   CTD; 139760; -.
DR   RGD; 727808; Gpr119.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234510; -.
DR   HOGENOM; CLU_583888_0_0_1; -.
DR   InParanoid; Q7TQN8; -.
DR   OMA; HLAIRKP; -.
DR   OrthoDB; 1245021at2759; -.
DR   PhylomeDB; Q7TQN8; -.
DR   TreeFam; TF325411; -.
DR   Reactome; R-RNO-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR   Reactome; R-RNO-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
DR   PRO; PR:Q7TQN8; -.
DR   Proteomes; UP000002494; Chromosome X.
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:RGD.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0031210; F:phosphatidylcholine binding; ISO:RGD.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0030073; P:insulin secretion; ISO:RGD.
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..468
FT                   /note="Glucose-dependent insulinotropic receptor"
FT                   /id="PRO_0000069609"
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..468
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   468 AA;  51686 MW;  6D5E607B572BE45A CRC64;
     MESSFSFGVI LAVLTILIIA VNALVVVAML LSIYKNDGVG LCFTLNLAVA DTLIGVAISG
     LVTDQLSSSA QHTQKTLCSL RMAFVTSSAA ASVLTVMLIA FDRYLAIKQP LRYFQIMNGL
     VAGGCIAGLW LISYLIGFLP LGVSIFQQTT YHGPCTFFAV FHPRFVLTLS CAGFFPAVLL
     FVFFYCDMLK IASVHSQHIR KMEHAGAMVG ACRPPRPVND FKAVRTVSVL IGSFTLSWSP
     FLITSIVQVA CHKCCLYQVL EKYLWLLGVG NSLLNPLIYA YWQREVRQQL CHMALGLLAD
     GSTQPQIETL KGKEERKKVG RKTLYTCDAQ TLYTCDAQTL YTCDAQTLYT CDACDTQTLY
     TCDAQTLYTC DAQTLYTCDA QTLYTCDAQT LYTCDAQTLY TCDTQTLYTC DAQTLYTCDA
     QTLYTCDAQT LYTCDAQTLY TSSLVTGQTE QTPLKRANMS DPLRTCRG
 
 
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