ID   GAST_SHEEP              Reviewed;         104 AA.
AC   O02686;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 75.
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   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9522119; DOI=10.3109/10425179709020883;
RA   Moore C., Jie R., Shulkes A., Baldwin G.S.;
RT   "Molecular cloning and sequence of the ovine gastrin gene.";
RL   DNA Seq. 8:39-44(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 76-92.
RX   PubMed=5665711; DOI=10.1038/219614a0;
RA   Agarwal K.L., Beacham J., Bentley P.H., Gregory R.A., Kenner G.W.,
RA   Sheppard R.C., Tracy H.J.;
RT   "Isolation, structure and synthesis of ovine and bovine gastrins.";
RL   Nature 219:614-615(1968).
CC   -!- FUNCTION: Gastrin stimulates the stomach mucosa to produce and secrete
CC       hydrochloric acid and the pancreas to secrete its digestive enzymes. It
CC       also stimulates smooth muscle contraction and increases blood
CC       circulation and water secretion in the stomach and intestine.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Sulfation enhances proteolytic processing, and blocks peptide
CC       degradation. Levels of sulfation differ between proteolytically-cleaved
CC       gastrins and between tissues (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U92801; AAB51307.1; -; Genomic_DNA.
DR   PIR; A01619; GMSH.
DR   AlphaFoldDB; O02686; -.
DR   STRING; 9940.ENSOARP00000018691; -.
DR   eggNOG; ENOG502SA9S; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0032094; P:response to food; ISS:AgBase.
DR   InterPro; IPR039236; GAST.
DR   InterPro; IPR001651; Gastrin/CCK.
DR   InterPro; IPR013152; Gastrin/cholecystokinin_CS.
DR   PANTHER; PTHR19309; PTHR19309; 1.
DR   Pfam; PF00918; Gastrin; 1.
DR   PROSITE; PS00259; GASTRIN; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Hormone; Phosphoprotein; Reference proteome; Secreted; Signal; Sulfation.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..58
FT                   /id="PRO_0000010652"
FT   PEPTIDE         59..92
FT                   /note="Big gastrin"
FT                   /id="PRO_0000010653"
FT   PEPTIDE         76..92
FT                   /note="Gastrin"
FT                   /id="PRO_0000010654"
FT   PROPEP          96..104
FT                   /id="PRO_0000010655"
FT   REGION          26..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         87
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         92
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01353"
SQ   SEQUENCE   104 AA;  11532 MW;  624063D4B5CE5AFD CRC64;
     MQRLCAHALI LVLALAAFCE ASWKPHSQLQ DAPVAPGANK GQEPLRMDRL GPASHPRRQL
     GLQDPPHMVA DLSKKQGPWV EEEEAAYGWM DFGRRSAEEG DQHP