GIPR_RAT
ID GIPR_RAT Reviewed; 455 AA.
AC P43219;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Gastric inhibitory polypeptide receptor;
DE Short=GIP-R;
DE AltName: Full=Glucose-dependent insulinotropic polypeptide receptor;
DE Flags: Precursor;
GN Name=Gipr;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8243312; DOI=10.1210/endo.133.6.8243312;
RA Usdin T.B., Mezey E., Button D.C., Brownstein M.J., Bonner T.I.;
RT "Gastric inhibitory polypeptide receptor, a member of the secretin-
RT vasoactive intestinal peptide receptor family, is widely distributed in
RT peripheral organs and the brain.";
RL Endocrinology 133:2861-2871(1993).
CC -!- FUNCTION: This is a receptor for GIP. The activity of this receptor is
CC mediated by G proteins which activate adenylyl cyclase.
CC -!- SUBUNIT: May form homodimers and heterodimers with GLP1R.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Present in the pancreas as well as the gut, adipose
CC tissue, heart, pituitary, and inner layers of the adrenal cortex,
CC whereas it is not found in kidney, spleen, or liver. It is also
CC expressed in several brain regions, including the cerebral cortex,
CC hippocampus, and olfactory bulb.
CC -!- PTM: N-glycosylation is required for cell surface expression and
CC lengthens receptor half-life by preventing degradation in the ER.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; L19660; AAC37637.1; -; mRNA.
DR PIR; I53273; I53273.
DR RefSeq; NP_036846.1; NM_012714.1.
DR RefSeq; XP_017444289.1; XM_017588800.1.
DR AlphaFoldDB; P43219; -.
DR SMR; P43219; -.
DR STRING; 10116.ENSRNOP00000021456; -.
DR BindingDB; P43219; -.
DR ChEMBL; CHEMBL5001; -.
DR GuidetoPHARMACOLOGY; 248; -.
DR GlyGen; P43219; 3 sites.
DR PhosphoSitePlus; P43219; -.
DR PaxDb; P43219; -.
DR Ensembl; ENSRNOT00000021456; ENSRNOP00000021456; ENSRNOG00000015860.
DR GeneID; 25024; -.
DR KEGG; rno:25024; -.
DR UCSC; RGD:2689; rat.
DR CTD; 2696; -.
DR RGD; 2689; Gipr.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000161988; -.
DR HOGENOM; CLU_002753_4_0_1; -.
DR InParanoid; P43219; -.
DR OMA; LNCPPWR; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P43219; -.
DR TreeFam; TF315710; -.
DR Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR PRO; PR:P43219; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000015860; Expressed in frontal cortex and 9 other tissues.
DR Genevisible; P43219; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0016519; F:gastric inhibitory peptide receptor activity; IDA:RGD.
DR GO; GO:0120022; F:glucagon family peptide binding; ISO:RGD.
DR GO; GO:0017046; F:peptide hormone binding; IPI:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0002029; P:desensitization of G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0031018; P:endocrine pancreas development; ISO:RGD.
DR GO; GO:0038192; P:gastric inhibitory peptide signaling pathway; ISO:RGD.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0051592; P:response to calcium ion; IMP:RGD.
DR GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR001749; GPCR_2_GIP_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR01129; GIPRECEPTOR.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..455
FT /note="Gastric inhibitory polypeptide receptor"
FT /id="PRO_0000012827"
FT TOPO_DOM 19..135
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..158
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..186
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..239
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..275
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..316
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..67
FT /evidence="ECO:0000250"
FT DISULFID 58..100
FT /evidence="ECO:0000250"
FT DISULFID 81..115
FT /evidence="ECO:0000250"
SQ SEQUENCE 455 AA; 52257 MW; 5454B0638ABF9A06 CRC64;
MPLRLLLLLL WLWGLSLQRA ETDSEGQTTG ELYQRWERYG WECQNTLEAT EPPSGLACNG
SFDMYACWNY TAANTTARVS CPWYLPWYRQ VAAGFVFRQC GSDGQWGSWR DHTQCENPEK
NGAFQDQKLI LERLQVVYTV GYSLSLATLL LALLILSLFR RLHCTRNYIH MNLFTSFMLR
AGAILTRDQL LPPLGPYTGN QTPTLWNQAL AACRTAQILT QYCVGANYTW LLVEGVYLHH
LLVVVRRSEK GHFRCYLLLG WGAPALFVIP WVIVRYLYEN TQCWERNEVK AIWWIIRTPI
LITILINFLI FIRILGILVS KLRTRQMRCP DYRLRLARST LTLMPLLGVH EVVFAPVTEE
QAEGSLRFAK LAFEIFLSSF QGFLVSVLYC FINKEVQSEI RRLRLSLQEQ CPRPHLGQAP
RAVPLSSAPQ EAAIRNALPS GMLHVPGDEV LESYC
