GIPR_MESAU
ID GIPR_MESAU Reviewed; 462 AA.
AC P43218;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 85.
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 Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7811236; DOI=10.1006/bbrc.1994.2844;
RA Yasuda K., Inagaki N., Yamada Y., Kubota A., Seino S., Seino Y.;
RT "Hamster gastric inhibitory polypeptide receptor expressed in pancreatic
RT islets and clonal insulin-secreting cells: its structure and functional
RT properties.";
RL Biochem. Biophys. Res. Commun. 205:1556-1562(1994).
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: Widely distributed including pancreatic islets,
CC brain and various peripheral tissues.
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; D38103; BAA07284.1; -; mRNA.
DR AlphaFoldDB; P43218; -.
DR SMR; P43218; -.
DR eggNOG; KOG4564; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016519; F:gastric inhibitory peptide receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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..462
FT /note="Gastric inhibitory polypeptide receptor"
FT /id="PRO_0000012826"
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..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 421..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 59
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 462 AA; 52919 MW; D7A6204BCB9BB688 CRC64;
MPLRPRLLLL CLWGLLLQQA ETDSEGQTTG ELYQRWERYA RECEETLTAA DPPSGMVCNG
SFDMYVCWDY TAANTTAQAS CPWYLPWYRH VAAGYVFRQC GSDGQWGPWR DHTQCENPEK
NGAFQDQRLI LERLQVVYTV GYSLSLGTLL LALLILSLFR RLHCTRNYIH MNVFLSFMLR
AVAILTRDRL LPTLGPYPGD RTLTLRNQAL AACRTAQIVT QYCVGANYTW LLVEGVYLHH
LLVIVGGSEK GHFRCYLLLG WGAPALFVIP WVIVRYLLEN TQCWERNEVK AIWWIIRTPI
LITILINFFI FIRILGILVS KLRTRQMRCP DYRLRLARST LTLVPLLGVH EVVFAPVTEE
QAEGTLRFAK LAFEIFLSSF QGFLVSVLYC FINKEVQSEI RRSWRHRVLH LSLRDERPCP
HAELGPQALP SRSAPREVPI TGSTLPSGPL HGPGEEVLES YC
