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GIP_RAT
ID   GIP_RAT                 Reviewed;         144 AA.
AC   Q06145;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Gastric inhibitory polypeptide;
DE            Short=GIP;
DE   AltName: Full=Glucose-dependent insulinotropic polypeptide;
DE   Flags: Precursor;
GN   Name=Gip;
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 [GENOMIC DNA].
RC   STRAIN=Wistar; TISSUE=Duodenum;
RX   PubMed=1476614; DOI=10.1677/jme.0.0090265;
RA   Sharma S.K., Austin C., Howard A., Lo G., Nicholl C.G., Legon S.;
RT   "Characterization of rat gastric inhibitory peptide cDNA.";
RL   J. Mol. Endocrinol. 9:265-272(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Jejunum;
RX   PubMed=8446620; DOI=10.1073/pnas.90.5.1992;
RA   Tseng C.C., Jarboe L.A., Landau S.B., Williams E.K., Wolfe M.;
RT   "Glucose-dependent insulinotropic peptide: structure of the precursor and
RT   tissue-specific expression in rat.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:1992-1996(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Intestine;
RX   PubMed=1380834; DOI=10.1016/0167-4781(92)90054-4;
RA   Higashimoto Y., Liddle R.A., Simchock J.;
RT   "Molecular cloning of rat glucose-dependent insulinotropic peptide (GIP).";
RL   Biochim. Biophys. Acta 1132:72-74(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8503905; DOI=10.1006/bbrc.1993.1607;
RA   Higashimoto Y., Liddle R.A.;
RT   "Isolation and characterization of the gene encoding rat glucose-dependent
RT   insulinotropic peptide.";
RL   Biochem. Biophys. Res. Commun. 193:182-190(1993).
CC   -!- FUNCTION: Potent stimulator of insulin secretion and relatively poor
CC       inhibitor of gastric acid secretion.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the duodenum and jejunum.
CC   -!- SIMILARITY: Belongs to the glucagon family. {ECO:0000305}.
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DR   EMBL; X66724; CAA47256.1; -; Genomic_DNA.
DR   EMBL; Z19564; CAA79621.1; -; mRNA.
DR   EMBL; L08831; AAA41225.1; -; mRNA.
DR   EMBL; M92916; AAA41237.1; -; mRNA.
DR   PIR; JN0589; JN0589.
DR   RefSeq; NP_062604.1; NM_019630.3.
DR   AlphaFoldDB; Q06145; -.
DR   STRING; 10116.ENSRNOP00000008481; -.
DR   PaxDb; Q06145; -.
DR   Ensembl; ENSRNOT00000008481; ENSRNOP00000008481; ENSRNOG00000006306.
DR   GeneID; 25040; -.
DR   KEGG; rno:25040; -.
DR   UCSC; RGD:2709; rat.
DR   CTD; 2695; -.
DR   RGD; 2709; Gip.
DR   eggNOG; ENOG502S7ZH; Eukaryota.
DR   GeneTree; ENSGT00390000005121; -.
DR   HOGENOM; CLU_146415_0_0_1; -.
DR   InParanoid; Q06145; -.
DR   OMA; DQMEVCR; -.
DR   OrthoDB; 1564478at2759; -.
DR   PhylomeDB; Q06145; -.
DR   TreeFam; TF332333; -.
DR   Reactome; R-RNO-400511; Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
DR   Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR   PRO; PR:Q06145; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000006306; Expressed in duodenum and 5 other tissues.
DR   Genevisible; Q06145; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0031767; F:gastric inhibitory polypeptide receptor binding; ISO:RGD.
DR   GO; GO:0031769; F:glucagon receptor binding; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IMP:RGD.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR   GO; GO:0055123; P:digestive system development; IEP:RGD.
DR   GO; GO:0031018; P:endocrine pancreas development; ISO:RGD.
DR   GO; GO:0035640; P:exploration behavior; ISO:RGD.
DR   GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR   GO; GO:0038192; P:gastric inhibitory peptide signaling pathway; ISO:RGD.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IDA:RGD.
DR   GO; GO:0007613; P:memory; ISO:RGD.
DR   GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IMP:RGD.
DR   GO; GO:0070094; P:positive regulation of glucagon secretion; IDA:RGD.
DR   GO; GO:0010828; P:positive regulation of glucose transmembrane transport; IMP:RGD.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
DR   GO; GO:0050806; P:positive regulation of synaptic transmission; IDA:RGD.
DR   GO; GO:0042304; P:regulation of fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0050796; P:regulation of insulin secretion; TAS:RGD.
DR   GO; GO:0010447; P:response to acidic pH; IMP:RGD.
DR   GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR   GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR   GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR   GO; GO:0009749; P:response to glucose; IEP:RGD.
DR   GO; GO:0033993; P:response to lipid; IEP:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR   GO; GO:0010269; P:response to selenium ion; IEP:RGD.
DR   GO; GO:0042594; P:response to starvation; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
DR   GO; GO:0070328; P:triglyceride homeostasis; IMP:RGD.
DR   InterPro; IPR039078; GIP.
DR   InterPro; IPR000532; Glucagon_GIP_secretin_VIP.
DR   PANTHER; PTHR15211; PTHR15211; 1.
DR   Pfam; PF00123; Hormone_2; 1.
DR   SMART; SM00070; GLUCA; 1.
DR   PROSITE; PS00260; GLUCAGON; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Hormone; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   PROPEP          22..42
FT                   /id="PRO_0000011220"
FT   PEPTIDE         44..85
FT                   /note="Gastric inhibitory polypeptide"
FT                   /id="PRO_0000011221"
FT   PROPEP          87..144
FT                   /id="PRO_0000011222"
FT   REGION          92..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   144 AA;  16401 MW;  091D7617459C6032 CRC64;
     MVALKTCSLL LVLLFLAVGL GEKEEVEFRS HAKFAGPRPR GPRYAEGTFI SDYSIAMDKI
     RQQDFVNWLL AQKGKKNDWK HNLTQREARA LELAGQSQRN EEKEAQGSSL PKSLSDEDVL
     RDLLIQELLA WMADQAELCR LRSQ
 
 
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