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P09681 (GIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gastric inhibitory polypeptide

Short name=GIP
Alternative name(s):
Glucose-dependent insulinotropic polypeptide
Incretin hormone
Gene names
Name:GIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glucagon family.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHormone
   PTMCleavage on pair of basic residues
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

digestive system development

Inferred from electronic annotation. Source: Ensembl

endocrine pancreas development

Inferred from electronic annotation. Source: Ensembl

exploration behavior

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

long-term synaptic potentiation

Inferred from electronic annotation. Source: Ensembl

memory

Inferred from electronic annotation. Source: Ensembl

positive regulation of cAMP-mediated signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of glucagon secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of glucose transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

regulation of insulin secretion

Traceable author statement. Source: Reactome

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to lipid

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

response to selenium ion

Inferred from electronic annotation. Source: Ensembl

response to starvation

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

triglyceride homeostasis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

secretory granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionhormone activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 5029
PRO_0000011214
Peptide52 – 9342Gastric inhibitory polypeptide Ref.4
PRO_0000011215
Propeptide95 – 15359
PRO_0000011216

Natural variations

Natural variant1031S → G. Ref.3
Corresponds to variant rs2291725 [ dbSNP | Ensembl ].
VAR_021897
Natural variant1461N → S.
Corresponds to variant rs35703924 [ dbSNP | Ensembl ].
VAR_033973

Secondary structure

...... 153
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09681 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 51F5FC388A8897EC

FASTA15317,108
        10         20         30         40         50         60 
MVATKTFALL LLSLFLAVGL GEKKEGHFSA LPSLPVGSHA KVSSPQPRGP RYAEGTFISD 

        70         80         90        100        110        120 
YSIAMDKIHQ QDFVNWLLAQ KGKKNDWKHN ITQREARALE LASQANRKEE EAVEPQSSPA 

       130        140        150 
KNPSDEDLLR DLLIQELLAC LLDQTNLCRL RSR 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of an intestinal cDNA encoding human gastric inhibitory polypeptide precursor."
Takeda J., Seino Y., Tanaka K., Fukumoto H., Kayano T., Takahashi H., Mitani T., Kurono M., Suzuki T., Tobe T., Imura H.
Proc. Natl. Acad. Sci. U.S.A. 84:7005-7008(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Gastric inhibitory polypeptide: structure and chromosomal localization of the human gene."
Inagaki N., Seino Y., Takeda J., Yano H., Yamada Y., Bell G.I., Eddy R.L. Jr., Fukushima Y., Byers M.G., Shows T.B., Imura H.
Mol. Endocrinol. 3:1014-1021(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-103.
[4]"The isolation and sequencing of human gastric inhibitory peptide (GIP)."
Moody A.J., Thim L., Valverde I.
FEBS Lett. 172:142-148(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 52-93.
[5]"NMR structure of the glucose-dependent insulinotropic polypeptide fragment, GIP(1-30)amide."
Alana I., Hewage C.M., Malthouse J.P., Parker J.C., Gault V.A., O'Harte F.P.
Biochem. Biophys. Res. Commun. 325:281-286(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 52-81.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18185 mRNA. Translation: AAA88043.1.
M31679 expand/collapse EMBL AC list , M31675, M31676, M31677, M31678 Genomic DNA. Translation: AAA53192.1.
BC069100 mRNA. Translation: AAH69100.1.
BC069663 mRNA. Translation: AAH69663.1.
BC069686 mRNA. Translation: AAH69686.1.
BC069746 mRNA. Translation: AAH69746.1.
BC096146 mRNA. Translation: AAH96146.1.
BC096147 mRNA. Translation: AAH96147.1.
BC096148 mRNA. Translation: AAH96148.1.
BC096149 mRNA. Translation: AAH96149.1.
CCDSCCDS11542.1.
PIRA28406.
RefSeqNP_004114.1. NM_004123.2.
UniGeneHs.1454.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T5QNMR-A52-81[»]
2B4NNMR-A52-93[»]
2L70NMR-A52-93[»]
2L71NMR-A52-93[»]
2OBUNMR-A52-93[»]
2QKHX-ray1.90B52-93[»]
ProteinModelPortalP09681.
SMRP09681. Positions 52-93.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-46469N.
IntActP09681. 2 interactions.
MINTMINT-8090589.
STRING9606.ENSP00000350005.

Chemistry

BindingDBP09681.
ChEMBLCHEMBL5571.

PTM databases

PhosphoSiteP09681.

Polymorphism databases

DMDM121194.

Proteomic databases

PaxDbP09681.
PeptideAtlasP09681.
PRIDEP09681.

Protocols and materials databases

DNASU2695.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357424; ENSP00000350005; ENSG00000159224.
GeneID2695.
KEGGhsa:2695.
UCSCuc002iol.1. human.

Organism-specific databases

CTD2695.
GeneCardsGC17M047037.
HGNCHGNC:4270. GIP.
HPACAB016729.
HPA021612.
MIM137240. gene.
neXtProtNX_P09681.
PharmGKBPA28681.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44984.
HOGENOMHOG000112725.
HOVERGENHBG005839.
InParanoidP09681.
KOK05258.
OMALAWMVDQ.
OrthoDBEOG7C8GKZ.
PhylomeDBP09681.
TreeFamTF332333.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.

Gene expression databases

BgeeP09681.
CleanExHS_GIP.
GenevestigatorP09681.

Family and domain databases

InterProIPR000532. Glucagon_GIP_secretin_VIP.
[Graphical view]
PfamPF00123. Hormone_2. 1 hit.
[Graphical view]
SMARTSM00070. GLUCA. 1 hit.
[Graphical view]
PROSITEPS00260. GLUCAGON. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09681.
GenomeRNAi2695.
NextBio10660.
PROP09681.
SOURCESearch...

Entry information

Entry nameGIP_HUMAN
AccessionPrimary (citable) accession number: P09681
Secondary accession number(s): Q4VB42, Q6NTD3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM