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   03-AUG-2022, entry version 150.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gastric antrum;
RX   PubMed=3453895; DOI=10.1210/mend-1-4-306;
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   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 sequence
RT   of the mRNA.";
RL   Peptides 3:693-696(1982).
RN   [3]
RP   PROTEOLYTIC PROCESSING, PHOSPHORYLATION AT SER-96, SULFATION AT TYR-87 AND
RP   TYR-103, AND AMIDATION AT PHE-92.
RX   PubMed=1701434; DOI=10.1016/s0021-9258(18)45762-6;
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 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 on Tyr-87 enhances proteolytic processing, and blocks
CC       peptide degradation. Levels of sulfation differ between
CC       proteolytically-cleaved gastrins and between tissues (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC       {ECO:0000305}.
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DR   EMBL; M38653; AAA41919.1; -; mRNA.
DR   EMBL; M25459; AAA41195.1; -; mRNA.
DR   PIR; A40910; A40910.
DR   RefSeq; NP_036981.1; NM_012849.1.
DR   RefSeq; XP_017452526.1; XM_017597037.1.
DR   AlphaFoldDB; P04563; -.
DR   STRING; 10116.ENSRNOP00000019863; -.
DR   iPTMnet; P04563; -.
DR   PhosphoSitePlus; P04563; -.
DR   PaxDb; P04563; -.
DR   Ensembl; ENSRNOT00000019863; ENSRNOP00000019863; ENSRNOG00000014740.
DR   GeneID; 25320; -.
DR   KEGG; rno:25320; -.
DR   UCSC; RGD:2662; rat.
DR   CTD; 2520; -.
DR   RGD; 2662; Gast.
DR   eggNOG; ENOG502SA9S; Eukaryota.
DR   GeneTree; ENSGT00390000014792; -.
DR   HOGENOM; CLU_2249245_0_0_1; -.
DR   InParanoid; P04563; -.
DR   OMA; KPRSQLQ; -.
DR   OrthoDB; 1589970at2759; -.
DR   PhylomeDB; P04563; -.
DR   TreeFam; TF336994; -.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
DR   PRO; PR:P04563; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000014740; Expressed in stomach and 10 other tissues.
DR   Genevisible; P04563; RN.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; IDA:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR   GO; GO:0032094; P:response to food; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IDA:RGD.
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; Hormone; Phosphoprotein;
KW   Reference proteome; Secreted; Signal; Sulfation.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000305"
FT   PROPEP          22..58
FT                   /id="PRO_0000010648"
FT   PEPTIDE         59..92
FT                   /note="Big gastrin"
FT                   /id="PRO_0000010649"
FT   PEPTIDE         76..92
FT                   /note="Gastrin"
FT                   /id="PRO_0000010650"
FT   PROPEP          96..104
FT                   /id="PRO_0000010651"
FT   REGION          23..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         87
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:1701434"
FT   MOD_RES         92
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:1701434"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:1701434"
FT   MOD_RES         103
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:1701434"
SQ   SEQUENCE   104 AA;  11832 MW;  973FD06276BF1E21 CRC64;
     MPRLCVCMLV LVLALATFSE ASWKPRSQLQ DASSGPRTNG ALEQHQLEKL GPASHHRRQL
     GPQGPQHFIA DLSKKQRPPM EEEEEAYGWM DFGRRSAEEE DQYN