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Protein

Gastrin

Gene

GAST

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine.

GO - Molecular functioni

GO - Biological processi

  • G-protein coupled receptor signaling pathway Source: GO_Central
  • response to food Source: GO_Central
  • signal transduction Source: ProtInc

Keywordsi

Molecular functionHormone

Enzyme and pathway databases

ReactomeiR-HSA-416476 G alpha (q) signalling events
R-HSA-881907 Gastrin-CREB signalling pathway via PKC and MAPK
SIGNORiP01350

Names & Taxonomyi

Protein namesi
Recommended name:
Gastrin
Cleaved into the following 6 chains:
Alternative name(s):
Gastrin component I
Gastrin-52
Short name:
G52
Alternative name(s):
Gastrin component II
Gastrin-34
Short name:
G34
Alternative name(s):
Gastrin component III
Gastrin-17
Short name:
G17
Gastrin-14
Short name:
G14
Gastrin-6
Short name:
G6
Gene namesi
Name:GAST
Synonyms:GAS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000184502.3
HGNCiHGNC:4164 GAST
MIMi137250 gene
neXtProtiNX_P01350

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi86A → D: Small increase in ratio of gastrin-17 versus gastrin-34 production. No change in ratio of gastrin-17 versus gastrin-34 production; when associated with F-87. 1 Publication1
Mutagenesisi87Y → F: Small decrease in ratio of gastrin-17 versus gastrin-34 production. No change in ratio of gastrin-17 versus gastrin-34 production; when associated with D-86. 1 Publication1

Organism-specific databases

DisGeNETi2520
OpenTargetsiENSG00000184502
PharmGKBiPA28577

Polymorphism and mutation databases

BioMutaiGAST
DMDMi120952

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
PeptideiPRO_000001063322 – 92Gastrin-71Add BLAST71
PeptideiPRO_000001063441 – 92Gastrin-52Add BLAST52
PeptideiPRO_000001063559 – 92Big gastrinAdd BLAST34
PeptideiPRO_000001063676 – 92GastrinAdd BLAST17
PeptideiPRO_000001063779 – 92Gastrin-14Add BLAST14
PeptideiPRO_000001063887 – 92Gastrin-66
PropeptideiPRO_000001063996 – 101Removed in mature form6

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei59Pyrrolidone carboxylic acid; in form big gastrin1 Publication1
Modified residuei76Pyrrolidone carboxylic acid; in form gastrin1 Publication1
Modified residuei87Sulfotyrosine; partial2 Publications1
Modified residuei92Phenylalanine amide1 Publication1
Modified residuei96Phosphoserine1 Publication1

Post-translational modificationi

Two different processing pathways probably exist in antral G-cells. In the dominant pathway progastrin is cleaved at three sites resulting in two major bioactive gastrins, gastrin-34 and gastrin-17. In the putative alternative pathway, progastrin may be processed only at the most C-terminal dibasic site resulting in the synthesis of gastrin-71.
Sulfation enhances proteolytic processing, and blocks peptide degradation. Levels of sulfation differ between proteolytically-cleaved gastrins. Thus, gastrin-6 is almost 73% sulfated, whereas the larger gastrins are less than 50% sulfated. Sulfation levels are also tissue-specific.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei40 – 41Cleavage2
Sitei58 – 59Cleavage2
Sitei75 – 76Cleavage2
Sitei95 – 96Cleavage2

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Phosphoprotein, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

PaxDbiP01350
PeptideAtlasiP01350
PRIDEiP01350
ProteomicsDBi51377

PTM databases

iPTMnetiP01350
PhosphoSitePlusiP01350

Miscellaneous databases

PMAP-CutDBiP01350

Expressioni

Gene expression databases

BgeeiENSG00000184502
CleanExiHS_GAST
ExpressionAtlasiP01350 baseline and differential
GenevisibleiP01350 HS

Organism-specific databases

HPAiCAB000038

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TFP027875EBI-3436637,EBI-714319

GO - Molecular functioni

Protein-protein interaction databases

BioGridi108796, 11 interactors
DIPiDIP-403N
IntActiP01350, 17 interactors
MINTiP01350
STRINGi9606.ENSP00000331358

Structurei

3D structure databases

ProteinModelPortaliP01350
SMRiP01350
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the gastrin/cholecystokinin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J1ZA Eukaryota
ENOG4111D7Y LUCA
GeneTreeiENSGT00390000014792
HOGENOMiHOG000073533
HOVERGENiHBG097593
InParanoidiP01350
KOiK13768
OMAiKKQGPWM
OrthoDBiEOG091G147Z
PhylomeDBiP01350
TreeFamiTF336994

Family and domain databases

InterProiView protein in InterPro
IPR039236 GAST
IPR001651 Gastrin
IPR013152 Gastrin/cholecystokinin_CS
PANTHERiPTHR19309 PTHR19309, 1 hit
PfamiView protein in Pfam
PF00918 Gastrin, 1 hit
PROSITEiView protein in PROSITE
PS00259 GASTRIN, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01350-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRLCVYVLI FALALAAFSE ASWKPRSQQP DAPLGTGANR DLELPWLEQQ
60 70 80 90 100
GPASHHRRQL GPQGPPHLVA DPSKKQGPWL EEEEEAYGWM DFGRRSAEDE

N
Length:101
Mass (Da):11,394
Last modified:October 23, 1986 - v1
Checksum:iA03C847FCFE7216C
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0491273R → P. Corresponds to variant dbSNP:rs34309618Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00183 Genomic DNA Translation: CAA25005.1
X00183 Genomic DNA Translation: CAA25006.1
X00183 Genomic DNA Translation: CAA25007.1
V00511 mRNA Translation: CAA23769.1
M15958 Genomic DNA Translation: AAA52520.1
K01254 Genomic DNA Translation: AAB59533.1
BC069724 mRNA Translation: AAH69724.1
BC069762 mRNA Translation: AAH69762.1
CCDSiCCDS11404.1
PIRiA93997 GMHUB
RefSeqiNP_000796.1, NM_000805.4
UniGeneiHs.2681

Genome annotation databases

EnsembliENST00000329402; ENSP00000331358; ENSG00000184502
GeneIDi2520
KEGGihsa:2520
UCSCiuc002hxl.3 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiGAST_HUMAN
AccessioniPrimary (citable) accession number: P01350
Secondary accession number(s): P78463, P78464
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 23, 1986
Last modified: July 18, 2018
This is version 168 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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