GIPR_MOUSE
ID GIPR_MOUSE Reviewed; 460 AA.
AC Q0P543; Q80UB4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
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 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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-178.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
CC -!- FUNCTION: This is a receptor for GIP. The activity of this receptor is
CC mediated by G proteins which activate adenylyl cyclase (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: May form homodimers and heterodimers with GLP1R.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0P543-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0P543-2; Sequence=VSP_028433, VSP_028434;
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; AC145199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC120671; AAI20672.1; -; mRNA.
DR EMBL; BC120673; AAI20674.1; -; mRNA.
DR EMBL; AY255568; AAO85080.1; -; mRNA.
DR CCDS; CCDS39795.1; -. [Q0P543-1]
DR RefSeq; NP_001074284.1; NM_001080815.1. [Q0P543-1]
DR PDB; 6O9H; X-ray; 2.10 A; C/D=19-134.
DR PDB; 6O9I; X-ray; 2.60 A; C=19-134.
DR PDBsum; 6O9H; -.
DR PDBsum; 6O9I; -.
DR AlphaFoldDB; Q0P543; -.
DR SMR; Q0P543; -.
DR BioGRID; 238129; 1.
DR STRING; 10090.ENSMUSP00000092384; -.
DR GlyGen; Q0P543; 3 sites.
DR PhosphoSitePlus; Q0P543; -.
DR PaxDb; Q0P543; -.
DR PRIDE; Q0P543; -.
DR ProteomicsDB; 265748; -. [Q0P543-1]
DR ABCD; Q0P543; 2 sequenced antibodies.
DR Antibodypedia; 17982; 610 antibodies from 32 providers.
DR Ensembl; ENSMUST00000094790; ENSMUSP00000092384; ENSMUSG00000030406. [Q0P543-1]
DR GeneID; 381853; -.
DR KEGG; mmu:381853; -.
DR UCSC; uc009fkw.1; mouse. [Q0P543-1]
DR UCSC; uc009fkx.1; mouse. [Q0P543-2]
DR CTD; 2696; -.
DR MGI; MGI:1352753; Gipr.
DR VEuPathDB; HostDB:ENSMUSG00000030406; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000161988; -.
DR HOGENOM; CLU_002753_4_0_1; -.
DR InParanoid; Q0P543; -.
DR OMA; LNCPPWR; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; Q0P543; -.
DR TreeFam; TF315710; -.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR BioGRID-ORCS; 381853; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Gipr; mouse.
DR PRO; PR:Q0P543; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q0P543; protein.
DR Bgee; ENSMUSG00000030406; Expressed in cortical plate and 32 other tissues.
DR ExpressionAtlas; Q0P543; baseline and differential.
DR Genevisible; Q0P543; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0016519; F:gastric inhibitory peptide receptor activity; ISO:MGI.
DR GO; GO:0120022; F:glucagon family peptide binding; ISO:MGI.
DR GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; TAS:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0031018; P:endocrine pancreas development; IMP:MGI.
DR GO; GO:0038192; P:gastric inhibitory peptide signaling pathway; ISO:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; TAS:MGI.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..460
FT /note="Gastric inhibitory polypeptide receptor"
FT /id="PRO_0000306251"
FT TOPO_DOM 19..134
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..255
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..460
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..66
FT /evidence="ECO:0000250"
FT DISULFID 57..99
FT /evidence="ECO:0000250"
FT DISULFID 80..114
FT /evidence="ECO:0000250"
FT VAR_SEQ 208..230
FT /note="ALAACRTAQIMTQYCVGANYTWL -> VLHRLLPGGTKTFPIYFRTFPHH
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028433"
FT VAR_SEQ 231..460
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028434"
FT CONFLICT 122
FT /note="A -> V (in Ref. 3; AAO85080)"
FT /evidence="ECO:0000305"
FT HELIX 30..47
FT /evidence="ECO:0007829|PDB:6O9H"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6O9H"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:6O9H"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:6O9H"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:6O9H"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:6O9I"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:6O9H"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6O9I"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:6O9I"
SQ SEQUENCE 460 AA; 52992 MW; 41ABC3F1E0A7DF98 CRC64;
MPLRLLLLLL WLWGLQWAET DSEGQTTTGE LYQRWEHYGQ ECQKMLETTE PPSGLACNGS
FDMYACWNYT AANTTARVSC PWYLPWFRQV SAGFVFRQCG SDGQWGSWRD HTQCENPEKN
GAFQDQTLIL ERLQIMYTVG YSLSLTTLLL ALLILSLFRR LHCTRNYIHM NLFTSFMLRA
AAILTRDQLL PPLGPYTGDQ APTPWNQALA ACRTAQIMTQ YCVGANYTWL LVEGVYLHHL
LVIVGRSEKG HFRCYLLLGW GAPALFVIPW VIVRYLRENT QCWERNEVKA IWWIIRTPIL
ITILINFLIF IRILGILVSK LRTRQMRCPD YRLRLARSTL TLVPLLGVHE VVFAPVTEEQ
VEGSLRFAKL AFEIFLSSFQ GFLVSVLYCF INKEVQSEIR QGWRHRRLRL SLQEQRPRPH
QELAPRAVPL SSACREAAVG NALPSGMLHV PGDEVLESYC
