LOCUS       NP_001074284             460 aa            linear   ROD 07-OCT-2024
DEFINITION  gastric inhibitory polypeptide receptor precursor [Mus musculus].
ACCESSION   NP_001074284 XP_889771
VERSION     NP_001074284.1
DBSOURCE    REFSEQ: accession NM_001080815.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 460)
  AUTHORS   Akindehin,S., Liskiewicz,A., Liskiewicz,D., Bernecker,M.,
            Garcia-Caceres,C., Drucker,D.J., Finan,B., Grandl,G., Gutgesell,R.,
            Hofmann,S.M., Khalil,A., Liu,X., Cota,P., Bakhti,M., Czarnecki,O.,
            Bastidas-Ponce,A., Lickert,H., Kang,L., Maity,G., Novikoff,A.,
            Parlee,S., Pathak,E., Schriever,S.C., Sterr,M., Ussar,S., Zhang,Q.,
            DiMarchi,R., Tschop,M.H., Pfluger,P.T., Douros,J.D. and Muller,T.D.
  TITLE     Loss of GIPR in LEPR cells impairs glucose control by GIP and
            GIP:GLP-1 co-agonism without affecting body weight and food intake
            in mice
  JOURNAL   Mol Metab 83, 101915 (2024)
   PUBMED   38492844
  REMARK    GeneRIF: Loss of GIPR in LEPR cells impairs glucose control by GIP
            and GIP:GLP-1 co-agonism without affecting body weight and food
            intake in mice.
REFERENCE   2  (residues 1 to 460)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 460)
  AUTHORS   Furber,E.C., Hyatt,K., Collins,K., Yu,X., Droz,B.A., Holland,A.,
            Friedrich,J.L., Wojnicki,S., Konkol,D.L., O'Farrell,L.S.,
            Baker,H.E., Coskun,T., Scherer,P.E., Kusminski,C.M., Christe,M.E.,
            Sloop,K.W. and Samms,R.J.
  TITLE     GIPR Agonism Enhances TZD-Induced Insulin Sensitivity in Obese IR
            Mice
  JOURNAL   Diabetes 73 (2), 292-305 (2024)
   PUBMED   37934926
REFERENCE   4  (residues 1 to 460)
  AUTHORS   Yammine,L., Picatoste,B., Abdullah,N., Leahey,R.A., Johnson,E.F.,
            Gomez-Banoy,N., Rosselot,C., Wen,J., Hossain,T., Goncalves,M.D.,
            Lo,J.C., Garcia-Ocana,A. and McGraw,T.E.
  TITLE     Spatiotemporal regulation of GIPR signaling impacts glucose
            homeostasis as revealed in studies of a common GIPR variant
  JOURNAL   Mol Metab 78, 101831 (2023)
   PUBMED   37925022
REFERENCE   5  (residues 1 to 460)
  AUTHORS   Takahashi,Y., Fujita,H., Seino,Y., Hattori,S., Hidaka,S.,
            Miyakawa,T., Suzuki,A., Waki,H., Yabe,D., Seino,Y. and Yamada,Y.
  TITLE     Gastric inhibitory polypeptide receptor antagonism suppresses
            intramuscular adipose tissue accumulation and ameliorates
            sarcopenia
  JOURNAL   J Cachexia Sarcopenia Muscle 14 (6), 2703-2718 (2023)
   PUBMED   37897141
  REMARK    GeneRIF: Gastric inhibitory polypeptide receptor antagonism
            suppresses intramuscular adipose tissue accumulation and
            ameliorates sarcopenia.
REFERENCE   6  (residues 1 to 460)
  AUTHORS   Pamir,N., Lynn,F.C., Buchan,A.M., Ehses,J., Hinke,S.A.,
            Pospisilik,J.A., Miyawaki,K., Yamada,Y., Seino,Y., McIntosh,C.H.
            and Pederson,R.A.
  TITLE     Glucose-dependent insulinotropic polypeptide receptor null mice
            exhibit compensatory changes in the enteroinsular axis
  JOURNAL   Am J Physiol Endocrinol Metab 284 (5), E931-E939 (2003)
   PUBMED   12540373
  REMARK    GeneRIF: GIPR(-/-) mice exhibit altered islet structure and
            topography and increased islet sensitivity to glucagon-like
            peptide-1 despite a decrease in pancreatic insulin content and gene
            expression
REFERENCE   7  (residues 1 to 460)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   8  (residues 1 to 460)
  AUTHORS   Miyawaki,K., Yamada,Y., Ban,N., Ihara,Y., Tsukiyama,K., Zhou,H.,
            Fujimoto,S., Oku,A., Tsuda,K., Toyokuni,S., Hiai,H., Mizunoya,W.,
            Fushiki,T., Holst,J.J., Makino,M., Tashita,A., Kobara,Y.,
            Tsubamoto,Y., Jinnouchi,T., Jomori,T. and Seino,Y.
  TITLE     Inhibition of gastric inhibitory polypeptide signaling prevents
            obesity
  JOURNAL   Nat Med 8 (7), 738-742 (2002)
   PUBMED   12068290
REFERENCE   9  (residues 1 to 460)
  AUTHORS   Miyawaki,K., Yamada,Y., Yano,H., Niwa,H., Ban,N., Ihara,Y.,
            Kubota,A., Fujimoto,S., Kajikawa,M., Kuroe,A., Tsuda,K.,
            Hashimoto,H., Yamashita,T., Jomori,T., Tashiro,F., Miyazaki,J. and
            Seino,Y.
  TITLE     Glucose intolerance caused by a defect in the entero-insular axis:
            a study in gastric inhibitory polypeptide receptor knockout mice
  JOURNAL   Proc Natl Acad Sci U S A 96 (26), 14843-14847 (1999)
   PUBMED   10611300
REFERENCE   10 (residues 1 to 460)
  AUTHORS   Gelling,R.W., Wheeler,M.B., Xue,J., Gyomorey,S., Nian,C.,
            Pederson,R.A. and McIntosh,C.H.
  TITLE     Localization of the domains involved in ligand binding and
            activation of the glucose-dependent insulinotropic polypeptide
            receptor
  JOURNAL   Endocrinology 138 (6), 2640-2643 (1997)
   PUBMED   9165060
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AC145199.3.
            
            On Jan 28, 2007 this sequence version replaced XP_889771.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: single sample supports all introns SAMN01164139
                              [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..460
                     /organism="Mus musculus"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 9.46 cM"
     Protein         1..460
                     /product="gastric inhibitory polypeptide receptor
                     precursor"
                     /note="glucose-dependent insulinotropic polypeptide
                     receptor"
                     /calculated_mol_wt=50774
     sig_peptide     1..18
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q0P543.2)"
                     /calculated_mol_wt=2236
     mat_peptide     19..460
                     /product="Gastric inhibitory polypeptide receptor.
                     /id=PRO_0000306251"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0P543.2)"
                     /calculated_mol_wt=50774
     Region          54..117
                     /region_name="HRM"
                     /note="Hormone receptor domain; pfam02793"
                     /db_xref="CDD:397086"
     Site            58
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q0P543.2)"
     Site            68
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q0P543.2)"
     Site            73
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q0P543.2)"
     Region          130..405
                     /region_name="7tmB1_GlucagonR-like"
                     /note="glucagon receptor-like subfamily, member of the
                     class B family of seven-transmembrane G protein-coupled
                     receptors; cd15929"
                     /db_xref="CDD:341353"
     Site            order(131,137,141,179,183,186..187,190,213,219..220,223,
                     227,283..284,291..292,294..296,350,353,370..371,374)
                     /site_type="other"
                     /note="putative polypeptide ligand binding pocket
                     [polypeptide binding]"
                     /db_xref="CDD:341353"
     Region          132..157
                     /region_name="TM helix 1"
                     /note="TM helix 1 [structural motif]"
                     /db_xref="CDD:341353"
     Site            135..155
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0P543.2)"
     Site            order(160,169,237,240..242,317,320,338..339,342,345,
                     387..388,391..392,394,398,401,405)
                     /site_type="other"
                     /note="G protein interaction site [polypeptide binding]"
                     /db_xref="CDD:341353"
     Region          166..188
                     /region_name="TM helix 2"
                     /note="TM helix 2 [structural motif]"
                     /db_xref="CDD:341353"
     Site            167..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0P543.2)"
     Region          213..240
                     /region_name="TM helix 3"
                     /note="TM helix 3 [structural motif]"
                     /db_xref="CDD:341353"
     Site            223..243
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0P543.2)"
     Region          252..272
                     /region_name="TM helix 4"
                     /note="TM helix 4 [structural motif]"
                     /db_xref="CDD:341353"
     Site            256..276
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0P543.2)"
     Region          288..317
                     /region_name="TM helix 5"
                     /note="TM helix 5 [structural motif]"
                     /db_xref="CDD:341353"
     Site            298..318
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0P543.2)"
     Site            order(317,333..334,336..338,340..341,383,387,391..393)
                     /site_type="other"
                     /note="allosteric modulator binding site [chemical
                     binding]"
                     /db_xref="CDD:341353"
     Region          331..358
                     /region_name="TM helix 6"
                     /note="TM helix 6 [structural motif]"
                     /db_xref="CDD:341353"
     Site            338..358
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0P543.2)"
     Region          367..392
                     /region_name="TM helix 7"
                     /note="TM helix 7 [structural motif]"
                     /db_xref="CDD:341353"
     Site            371..391
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q0P543.2)"
     CDS             1..460
                     /gene="Gipr"
                     /gene_synonym="GIP-R; Gm1081; Gm160"
                     /coded_by="NM_001080815.1:167..1549"
                     /db_xref="CCDS:CCDS39795.1"
                     /db_xref="GeneID:381853"
                     /db_xref="MGI:MGI:1352753"
ORIGIN      
        1 mplrllllll wlwglqwaet dsegqtttge lyqrwehygq ecqkmlette ppsglacngs
       61 fdmyacwnyt aanttarvsc pwylpwfrqv sagfvfrqcg sdgqwgswrd htqcenpekn
      121 gafqdqtlil erlqimytvg yslslttlll allilslfrr lhctrnyihm nlftsfmlra
      181 aailtrdqll pplgpytgdq aptpwnqala acrtaqimtq ycvganytwl lvegvylhhl
      241 lvivgrsekg hfrcylllgw gapalfvipw vivrylrent qcwernevka iwwiirtpil
      301 itilinflif irilgilvsk lrtrqmrcpd yrlrlarstl tlvpllgvhe vvfapvteeq
      361 vegslrfakl afeiflssfq gflvsvlycf inkevqseir qgwrhrrlrl slqeqrprph
      421 qelapravpl ssacreaavg nalpsgmlhv pgdevlesyc
//
