ID   GAST_RAT                Reviewed;         104 AA.
AC   P04563;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   04-NOV-2008, entry version 72.
DE   RecName: Full=Gastrin;
DE   Contains:
DE     RecName: Full=Big gastrin;
DE     AltName: Full=Gastrin-34;
DE              Short=G34;
DE   Contains:
DE     RecName: Full=Gastrin;
DE   Flags: Precursor;
GN   Name=Gast; Synonyms=Gas;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gastric antrum;
RX   MEDLINE=88288206; PubMed=3453895;
RA   Fuller P.J., Stone D.L., Brand S.J.;
RT   "Molecular cloning and sequencing of a rat preprogastrin complementary
RT   deoxyribonucleic acid.";
RL   Mol. Endocrinol. 1:306-311(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 56-92.
RX   MEDLINE=83039009; PubMed=6897117; DOI=10.1016/0196-9781(82)90172-3;
RA   Schaffer M.H., Agarwal K.L., Noyes B.E.;
RT   "Rat gastrin's amino acid sequence determined from the nucleotide
RT   sequence of the mRNA.";
RL   Peptides 3:693-696(1982).
RN   [3]
RP   PROTEOLYTIC PROCESSING, PHOSPHORYLATION AT SER-96, SULFATION AT TYR-87
RP   AND TYR-103, AND AMIDATION AT PHE-92.
RX   MEDLINE=91072336; PubMed=1701434;
RA   Varro A., Nemeth J., Bridson J., Lee C., Moore S., Dockray G.J.;
RT   "Processing of the gastrin precursor. Modulation of phosphorylated,
RT   sulfated, and amidated products.";
RL   J. Biol. Chem. 265:21476-21481(1990).
CC   -!- FUNCTION: Gastrin stimulates the stomach mucosa to produce and
CC       secrete hydrochloric acid and the pancreas to secrete its
CC       digestive enzymes. It also stimulates smooth muscle contraction
CC       and increases blood circulation and water secretion in the stomach
CC       and intestine.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Sulfation on Tyr-87 enhances proteolytic processing, and
CC       blocks peptide degradation. Levels of sulfation differ between
CC       proteolytically-cleaved gastrins and between tissues (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M38653; AAA41919.1; -; mRNA.
DR   EMBL; M25459; AAA41195.1; -; mRNA.
DR   PIR; A40910; A40910.
DR   RefSeq; NP_036981.1; -.
DR   UniGene; Rn.9754; -.
DR   Ensembl; ENSRNOG00000014740; Rattus norvegicus.
DR   GeneID; 25320; -.
DR   KEGG; rno:25320; -.
DR   RGD; 2662; Gast.
DR   HOVERGEN; P04563; -.
DR   NextBio; 606161; -.
DR   ArrayExpress; P04563; -.
DR   GermOnline; ENSRNOG00000014740; Rattus norvegicus.
DR   InterPro; IPR001651; Gastrin.
DR   InterPro; IPR013152; Gastrin_CCK_CS.
DR   Pfam; PF00918; Gastrin; 1.
DR   SMART; SM00029; GASTRIN; 1.
DR   PROSITE; PS00259; GASTRIN; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Hormone;
KW   Phosphoprotein; Pyrrolidone carboxylic acid; Secreted; Signal;
KW   Sulfation.
FT   SIGNAL        1     21       Probable.
FT   PROPEP       22     58
FT                                /FTId=PRO_0000010648.
FT   PEPTIDE      59     92       Big gastrin.
FT                                /FTId=PRO_0000010649.
FT   PEPTIDE      76     92       Gastrin.
FT                                /FTId=PRO_0000010650.
FT   PROPEP       96    104
FT                                /FTId=PRO_0000010651.
FT   MOD_RES      59     59       Pyrrolidone carboxylic acid (By
FT                                similarity).
FT   MOD_RES      76     76       Pyrrolidone carboxylic acid (By
FT                                similarity).
FT   MOD_RES      87     87       Sulfotyrosine.
FT   MOD_RES      92     92       Phenylalanine amide.
FT   MOD_RES      96     96       Phosphoserine.
FT   MOD_RES     103    103       Sulfotyrosine.
SQ   SEQUENCE   104 AA;  11832 MW;  973FD06276BF1E21 CRC64;
     MPRLCVCMLV LVLALATFSE ASWKPRSQLQ DASSGPRTNG ALEQHQLEKL GPASHHRRQL
     GPQGPQHFIA DLSKKQRPPM EEEEEAYGWM DFGRRSAEEE DQYN
//