[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=6951161 [NCBI, ExPASy, EBI, Israel, Japan] Yoo O.J., Powell C.T., Agarwal K.L.; "Molecular cloning and nucleotide sequence of full-length of cDNA coding for porcine gastrin."; Proc. Natl. Acad. Sci. U.S.A. 79:1049-1053(1982).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 56-82. PubMed=6930858 [NCBI, ExPASy, EBI, Israel, Japan] Agarwal K.L., Noyes B.E.; "Studies on gastrin mRNA structure using an oligonucleotide probe."; Ann. N. Y. Acad. Sci. 343:433-442(1980).
[3]	PROTEIN SEQUENCE OF 76-92. PubMed=14248711 [NCBI, ExPASy, EBI, Israel, Japan] Gregory H., Hardy P.M., Jones D.S., Kenner G.W., Sheppard R.C.; "The antral hormone gastrin. Structure of gastrin."; Nature 204:931-933(1964).
[4]	SYNTHESIS. PubMed=14248712 [NCBI, ExPASy, EBI, Israel, Japan] Anderson J.C., Barton M.A., Gregory R.A., Hardy P.M., Kenner G.W., McLeod J.K., Preston J., Sheppard R.C., Morley J.S.; "Synthesis of gastrin."; Nature 204:933-934(1964).
[5]	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).

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: 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.

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

V01303; CAA24610.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M25036; AAA31111.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A93903; GMPGB.

NP_001004036.1; -.

3D structure databases

ModBase

P01351.

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.

PS00259; GASTRIN; 1.

Genome annotation databases

GeneID

445524; -.

KEGG

ssc:445524; -.

Phylogenomic databases

HOVERGEN

P01351; -.

Other

UniRef

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`	`Potential.`
`PROPEP`	`22 58`	`37`		`PRO_0000010644`
`PEPTIDE`	`59 92`	`34`	`Big gastrin.`	`PRO_0000010645`
`PEPTIDE`	`76 92`	`17`	`Gastrin.`	`PRO_0000010646`
`PROPEP`	`96 104`	`9`		`PRO_0000010647`
`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 (By similarity).`
`MOD_RES`	`96 96`		`Phosphoserine (By similarity).`

Sequence information

Length: 104 AA [This is the length of the unprocessed precursor]

Molecular weight: 11558 Da [This is the MW of the unprocessed precursor]

CRC64: B0BD1D7E05304B79 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQRLCAYVLI HVLALAACSE ASWKPGFQLQ DASSGPGANR GKEPHELDRL GPASHHRRQL 

        70         80         90        100 
GLQGPPHLVA DLAKKQGPWM EEEEEAYGWM DFGRRSAEEG DQRP

P01351 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