Gastrin-71
     (Gastrin component I)
Gastrin-52
     (G52)
Big gastrin
     (Gastrin-34)
     (G34)
     (Gastrin component II)
Gastrin
     (Gastrin-17)
     (G17)
     (Gastrin component III)
Gastrin-14
     (G14)
Gastrin-6
     (G6)

Gene name

	Name:	GAST
	Synonyms:	GAS

From

Homo sapiens (Human)

[TaxID: 9606]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(86)90338-0; PubMed=3034736 [NCBI, ExPASy, EBI, Israel, Japan] Kariya Y., Kato K., Hayashizaki Y., Himeno S., Tarui S., Matsubara K.; "Expression of human gastrin gene in normal and gastrinoma tissues."; Gene 50:345-352(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=6087340 [NCBI, ExPASy, EBI, Israel, Japan] Ito R., Sato K., Helmer T., Jay G., Agarwal K.L.; "Structural analysis of the gene encoding human gastrin: the large intron contains an Alu sequence."; Proc. Natl. Acad. Sci. U.S.A. 81:4662-4666(1984).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1093/nar/11.23.8197; PubMed=6324077 [NCBI, ExPASy, EBI, Israel, Japan] Kato K., Hayashizaki Y., Takahashi Y., Himeno S., Matsubara K.; "Molecular cloning of the human gastrin gene."; Nucleic Acids Res. 11:8197-8203(1983).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=6574456 [NCBI, ExPASy, EBI, Israel, Japan] Boel E., Vuust J., Norris F., Norris K., Wind A., Rehfeld J.F., Marcker K.A.; "Molecular cloning of human gastrin cDNA: evidence for evolution of gastrin by gene duplication."; Proc. Natl. Acad. Sci. U.S.A. 80:2866-2869(1983).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=6322186 [NCBI, ExPASy, EBI, Israel, Japan] Wiborg O., Berglund L., Boel E., Norris F., Norris K., Rehfeld J.F., Marcker K.A., Vuust J.; "Structure of a human gastrin gene."; Proc. Natl. Acad. Sci. U.S.A. 81:1067-1069(1984).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(83)90035-5; PubMed=6689486 [NCBI, ExPASy, EBI, Israel, Japan] Kato K., Himeno S., Takahashi Y., Wakabayashi T., Tarui S., Matsubara K.; "Molecular cloning of human gastrin precursor cDNA."; Gene 26:53-57(1983).
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[8]	PROTEIN SEQUENCE OF 22-101, AND CHARACTERIZATION OF GASTRIN 71. TISSUE=Gastric mucosa; PubMed=8055952 [NCBI, ExPASy, EBI, Israel, Japan] Rehfeld J.F., Johnsen A.H.; "Identification of gastrin component I as gastrin-71. The largest possible bioactive progastrin product."; Eur. J. Biochem. 223:765-773(1994).
[9]	PROTEIN SEQUENCE OF 76-92. PubMed=5921183 [NCBI, ExPASy, EBI, Israel, Japan] Bentley P.H., Kenner G.W., Sheppard R.C.; "Structures of human gastrins I and II."; Nature 209:583-585(1966).
[10]	PROTEIN SEQUENCE OF 59-68. DOI=10.1016/S0006-291X(89)80154-8; PubMed=2730647 [NCBI, ExPASy, EBI, Israel, Japan] Higashimoto Y., Himeno S., Shinomura Y., Nagao K., Tamura T., Tarui S.; "Purification and structural determination of urinary NH2-terminal big gastrin fragments."; Biochem. Biophys. Res. Commun. 160:1364-1370(1989).
[11]	PROTEIN SEQUENCE OF 76-92. PubMed=5822140 [NCBI, ExPASy, EBI, Israel, Japan] Gregory R.A., Tracy H.J., Agarwal K.L., Grossman M.I.; "Aminoacid constitution of two gastrins isolated from Zollinger-Ellison tumour tissue."; Gut 10:603-608(1969).
[12]	PROTEOLYTIC PROCESSING, MASS SPECTROMETRY, AND SULFATION AT TYR-87. PubMed=7530658 [NCBI, ExPASy, EBI, Israel, Japan] Rehfeld J.F., Hansen C.P., Johnsen A.H.; "Post-poly(Glu) cleavage and degradation modified by O-sulfated tyrosine: a novel post-translational processing mechanism."; EMBO J. 14:389-396(1995).
[13]	SULFATION, MUTAGENESIS OF ALA-86 AND TYR-87, AND PROTEOLYTIC PROCESSING. PubMed=7621822 [NCBI, ExPASy, EBI, Israel, Japan] Bundgaard J.R., Vuust J., Rehfeld J.F.; "Tyrosine O-sulfation promotes proteolytic processing of progastrin."; EMBO J. 14:3073-3079(1995).
[14]	PROTEOLYTIC PROCESSING, AND SULFATION AT TYR-87. PubMed=11052986 [NCBI, ExPASy, EBI, Israel, Japan] Palnaes Hansen C., Stadil F., Rehfeld J.F.; "Metabolism and acid secretory effect of sulfated and nonsulfated gastrin-6 in humans."; Am. J. Physiol. 279:G903-G909(2000).

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.
PTM: 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.
PTM: 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.
SIMILARITY: Belongs to the gastrin/cholecystokinin family.
WEB RESOURCE: Name=Wikipedia; Note=Gastrin entry; URL="http://en.wikipedia.org/wiki/Gastrin";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X00183; CAA25005.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X00183; CAA25006.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X00183; CAA25007.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
V00511; CAA23769.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M15958; AAA52520.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
K01254; AAB59533.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069724; AAH69724.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069762; AAH69762.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A93997; GMHUB.

NP_000796.1; -.

3D structure databases

ModBase

P01350.

Protein-protein interaction databases

DIP

DIP:403N; -.

PTM databases

PhosphoSite

P01350; -.

Organism-specific databases

HIX0039214; -.

HGNC:4164; GAST.

CAB000038; -.

137250; gene. [NCBI / EBI]

PharmGKB

PA28577; -.

GeneCards

P01350.

Gene expression databases

ArrayExpress

P01350; -.

CleanEx

HS_GAST; -.

GermOnline

ENSG00000184502; Homo sapiens.

Ontologies

GO:0005179;	Molecular function: hormone activity (traceable author statement from ProtInc).
GO:0007165;	Biological process: signal transduction (non-traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR001651; Gastrin.
IPR013152; Gastrin_CCK_CS.
Graphical view of domain structure.

Pfam

PF00918; Gastrin; 1.
Pfam graphical view of domain structure.

SMART

SM00029; GASTRIN; 1.
SMART graphical view of domain structure.

PROSITE

PS00259; GASTRIN; 1.

BLOCKS

P01350.

Genome annotation databases

Ensembl

ENSG00000184502; Homo sapiens. [Contig view]

GeneID

2520; -.

KEGG

hsa:2520; -.

Phylogenomic databases

HOGENOM

P01350; -.

HOVERGEN

P01350; -.

Other

GAST; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amidation; Cleavage on pair of basic residues; Direct protein sequencing; Hormone; Phosphoprotein; Pyrrolidone carboxylic acid; Secreted; Signal; Sulfation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`
`PEPTIDE`	`22 92`	`71`	`Gastrin-71.`	`PRO_0000010633`
`PEPTIDE`	`41 92`	`52`	`Gastrin-52.`	`PRO_0000010634`
`PEPTIDE`	`59 92`	`34`	`Big gastrin.`	`PRO_0000010635`
`PEPTIDE`	`76 92`	`17`	`Gastrin.`	`PRO_0000010636`
`PEPTIDE`	`79 92`	`14`	`Gastrin-14.`	`PRO_0000010637`
`PEPTIDE`	`87 92`	`6`	`Gastrin-6.`	`PRO_0000010638`
`PROPEP`	`96 101`	`6`	`Removed in mature form.`	`PRO_0000010639`
`SITE`	`40 41`	`2`	`Cleavage.`
`SITE`	`58 59`	`2`	`Cleavage.`
`SITE`	`75 76`	`2`	`Cleavage.`
`SITE`	`95 96`	`2`	`Cleavage.`
`MOD_RES`	`59 59`		`Pyrrolidone carboxylic acid; in form big gastrin.`
`MOD_RES`	`76 76`		`Pyrrolidone carboxylic acid; in form gastrin.`
`MOD_RES`	`87 87`		`Sulfotyrosine; partial.`
`MOD_RES`	`92 92`		`Phenylalanine amide.`
`MOD_RES`	`96 96`		`Phosphoserine (By similarity).`
`MUTAGEN`	`86 86`		`A->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.`
`MUTAGEN`	`87 87`		`Y->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.`

Sequence information

Length: 101 AA [This is the length of the unprocessed precursor]

Molecular weight: 11394 Da [This is the MW of the unprocessed precursor]

CRC64: A03C847FCFE7216C [This is a checksum on the sequence]

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

        70         80         90        100 
GPQGPPHLVA DPSKKQGPWL EEEEEAYGWM DFGRRSAEDE N

P01350 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools