Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P01350 (GAST_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gastrin

Cleaved into the following 6 chains:

  1. Gastrin-71
    Alternative name(s):
    Gastrin component I
  2. Gastrin-52
    Short name=G52
  3. Big gastrin
    Alternative name(s):
    Gastrin component II
    Gastrin-34
    Short name=G34
  4. Gastrin
    Alternative name(s):
    Gastrin component III
    Gastrin-17
    Short name=G17
  5. Gastrin-14
    Short name=G14
  6. Gastrin-6
    Short name=G6
Gene names
Name:GAST
Synonyms:GAS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length101 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Secreted.

Post-translational modification

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. Ref.13 Ref.14 Ref.15

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. Ref.13 Ref.14 Ref.15

Sequence similarities

Belongs to the gastrin/cholecystokinin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TFP027875EBI-3436637,EBI-714319

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.8
Peptide22 – 9271Gastrin-71
PRO_0000010633
Peptide41 – 9252Gastrin-52
PRO_0000010634
Peptide59 – 9234Big gastrin
PRO_0000010635
Peptide76 – 9217Gastrin Ref.9 Ref.11
PRO_0000010636
Peptide79 – 9214Gastrin-14
PRO_0000010637
Peptide87 – 926Gastrin-6
PRO_0000010638
Propeptide96 – 1016Removed in mature form
PRO_0000010639

Sites

Site40 – 412Cleavage
Site58 – 592Cleavage
Site75 – 762Cleavage
Site95 – 962Cleavage

Amino acid modifications

Modified residue591Pyrrolidone carboxylic acid; in form big gastrin Ref.9
Modified residue761Pyrrolidone carboxylic acid; in form gastrin
Modified residue871Sulfotyrosine; partial Ref.13 Ref.15
Modified residue921Phenylalanine amide
Modified residue961Phosphoserine Ref.12

Natural variations

Natural variant31R → P.
Corresponds to variant rs34309618 [ dbSNP | Ensembl ].
VAR_049127

Experimental info

Mutagenesis861A → 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. Ref.14
Mutagenesis871Y → 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. Ref.14

Sequences

Sequence LengthMass (Da)Tools
P01350 [UniParc].

Last modified October 23, 1986. Version 1.
Checksum: A03C847FCFE7216C

FASTA10111,394
        10         20         30         40         50         60 
MQRLCVYVLI FALALAAFSE ASWKPRSQQP DAPLGTGANR DLELPWLEQQ GPASHHRRQL 

        70         80         90        100 
GPQGPPHLVA DPSKKQGPWL EEEEEAYGWM DFGRRSAEDE N 

« Hide

References

« Hide 'large scale' references
[1]"Expression of human gastrin gene in normal and gastrinoma tissues."
Kariya Y., Kato K., Hayashizaki Y., Himeno S., Tarui S., Matsubara K.
Gene 50:345-352(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structural analysis of the gene encoding human gastrin: the large intron contains an Alu sequence."
Ito R., Sato K., Helmer T., Jay G., Agarwal K.L.
Proc. Natl. Acad. Sci. U.S.A. 81:4662-4666(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Molecular cloning of the human gastrin gene."
Kato K., Hayashizaki Y., Takahashi Y., Himeno S., Matsubara K.
Nucleic Acids Res. 11:8197-8203(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Molecular cloning of human gastrin cDNA: evidence for evolution of gastrin by gene duplication."
Boel E., Vuust J., Norris F., Norris K., Wind A., Rehfeld J.F., Marcker K.A.
Proc. Natl. Acad. Sci. U.S.A. 80:2866-2869(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Structure of a human gastrin gene."
Wiborg O., Berglund L., Boel E., Norris F., Norris K., Rehfeld J.F., Marcker K.A., Vuust J.
Proc. Natl. Acad. Sci. U.S.A. 81:1067-1069(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Molecular cloning of human gastrin precursor cDNA."
Kato K., Himeno S., Takahashi Y., Wakabayashi T., Tarui S., Matsubara K.
Gene 26:53-57(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"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].
[8]"Identification of gastrin component I as gastrin-71. The largest possible bioactive progastrin product."
Rehfeld J.F., Johnsen A.H.
Eur. J. Biochem. 223:765-773(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-101, CHARACTERIZATION OF GASTRIN 71.
Tissue: Gastric mucosa.
[9]"Structures of human gastrins I and II."
Bentley P.H., Kenner G.W., Sheppard R.C.
Nature 209:583-585(1966) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 76-92.
[10]"Purification and structural determination of urinary NH2-terminal big gastrin fragments."
Higashimoto Y., Himeno S., Shinomura Y., Nagao K., Tamura T., Tarui S.
Biochem. Biophys. Res. Commun. 160:1364-1370(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 59-68.
[11]"Aminoacid constitution of two gastrins isolated from Zollinger-Ellison tumour tissue."
Gregory R.A., Tracy H.J., Agarwal K.L., Grossman M.I.
Gut 10:603-608(1969) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 76-92.
[12]"The human gastrin precursor. Characterization of phosphorylated forms and fragments."
Varro A., Desmond H., Pauwels S., Gregory H., Young J., Dockray G.J.
Biochem. J. 256:951-957(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-96.
[13]"Post-poly(Glu) cleavage and degradation modified by O-sulfated tyrosine: a novel post-translational processing mechanism."
Rehfeld J.F., Hansen C.P., Johnsen A.H.
EMBO J. 14:389-396(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY, SULFATION AT TYR-87.
[14]"Tyrosine O-sulfation promotes proteolytic processing of progastrin."
Bundgaard J.R., Vuust J., Rehfeld J.F.
EMBO J. 14:3073-3079(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION, MUTAGENESIS OF ALA-86 AND TYR-87, PROTEOLYTIC PROCESSING.
[15]"Metabolism and acid secretory effect of sulfated and nonsulfated gastrin-6 in humans."
Palnaes Hansen C., Stadil F., Rehfeld J.F.
Am. J. Physiol. 279:G903-G909(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, SULFATION AT TYR-87.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRGMHUB. A93997.
RefSeqNP_000796.1. NM_000805.4.
UniGeneHs.2681.

3D structure databases

ProteinModelPortalP01350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108796. 1 interaction.
DIPDIP-403N.
IntActP01350. 2 interactions.
MINTMINT-7212817.
STRING9606.ENSP00000331358.

PTM databases

PhosphoSiteP01350.

Polymorphism databases

DMDM120952.

Proteomic databases

PaxDbP01350.
PRIDEP01350.

Protocols and materials databases

DNASU2520.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329402; ENSP00000331358; ENSG00000184502.
ENST00000561776; ENSP00000455919; ENSG00000260334.
GeneID2520.
KEGGhsa:2520.
UCSCuc002hxl.3. human.

Organism-specific databases

CTD2520.
GeneCardsGC17P039868.
HGNCHGNC:4164. GAST.
HPACAB000038.
MIM137250. gene.
neXtProtNX_P01350.
PharmGKBPA28577.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39909.
HOGENOMHOG000073533.
HOVERGENHBG097593.
InParanoidP01350.
KOK13768.
OMAKPRSQLQ.
OrthoDBEOG72ZCH9.
PhylomeDBP01350.
TreeFamTF336994.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP01350.
CleanExHS_GAST.
GenevestigatorP01350.

Family and domain databases

InterProIPR001651. Gastrin.
IPR013152. Gastrin/cholecystokinin_CS.
[Graphical view]
PfamPF00918. Gastrin. 1 hit.
[Graphical view]
SMARTSM00029. GASTRIN. 1 hit.
[Graphical view]
PROSITEPS00259. GASTRIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGastrin.
GenomeRNAi2520.
NextBio9923.
PMAP-CutDBP01350.
PROP01350.
SOURCESearch...

Entry information

Entry nameGAST_HUMAN
AccessionPrimary (citable) accession number: P01350
Secondary accession number(s): P78463, P78464
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 23, 1986
Last modified: April 16, 2014
This is version 138 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

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