NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 62-95, AMIDATION AT PHE-95, PYROGLUTAMATE FORMATION AT GLN-62 AND GLN-79, AND MASS SPECTROMETRY.
TISSUE=Gastric mucosa;
PubMed=9716385 [NCBI, ExPASy, EBI, Israel, Japan]
Johnsen A.H., Sandin A., Rourke I.J., Bundgaard J.R., Nilsson G., Rehfeld J.F.;
"Unique progastrin processing in equine G-cells suggests marginal tyrosyl sulfotransferase activity.";
Eur. J. Biochem. 255:432-438(1998).

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: Neither gastrin is sulfated.
MASS SPECTROMETRY: Mass=1928; Method=MALDI; Range=63-78; Source=PubMed:9716385;.
MASS SPECTROMETRY: Mass=3814; Method=MALDI; Range=62-95; Source=PubMed:9716385;.
MASS SPECTROMETRY: Mass=3703; Method=MALDI; Range=63-95; Source=PubMed:9716385;.
MASS SPECTROMETRY: Mass=2039; Method=MALDI; Range=80-95; Source=PubMed:9716385;.
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

Y09440; CAA70590.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001075979.1; -.

UniGene

Eca.13044

3D structure databases

ModBase

P55885.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0005179;	Molecular function: hormone activity (inferred from electronic annotation from InterPro).
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.

Genome annotation databases

GeneID

100034214; -.

Phylogenomic databases

HOVERGEN

P55885; -.

Other

ProtoNet

P55885.

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.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`
`PROPEP`	`22 61`	`40`		`PRO_0000010629`
`PEPTIDE`	`62 95`	`34`	`Big gastrin.`	`PRO_0000010630`
`PEPTIDE`	`79 95`	`17`	`Gastrin.`	`PRO_0000010631`
`PROPEP`	`99 107`	`9`		`PRO_0000010632`
`MOD_RES`	`62 62`		`Pyrrolidone carboxylic acid.`
`MOD_RES`	`79 79`		`Pyrrolidone carboxylic acid.`
`MOD_RES`	`95 95`		`Phenylalanine amide.`
`MOD_RES`	`99 99`		`Phosphoserine (By similarity).`

Sequence information

Length: 107 AA [This is the length of the unprocessed precursor]

Molecular weight: 11884 Da [This is the MW of the unprocessed precursor]

CRC64: 104166CAAE5C234F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRRLCVYVLI FALALAAFSE ASWKPCSQLQ DAPSGPGANK GLYPHWPDQL DRLGPASHHR 

        70         80         90        100 
RQLGLQGSPH LVADLSKKQG PWLEKEEAAY GWMDFGRRSA EEGDQSP

P55885 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