ID   GAST_PIG                Reviewed;         104 AA.
AC   P01351;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 110.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6951161; DOI=10.1073/pnas.79.4.1049;
RA   Yoo O.J., Powell C.T., Agarwal K.L.;
RT   "Molecular cloning and nucleotide sequence of full-length of cDNA coding
RT   for porcine gastrin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:1049-1053(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 56-82.
RX   PubMed=6930858; DOI=10.1111/j.1749-6632.1980.tb47272.x;
RA   Agarwal K.L., Noyes B.E.;
RT   "Studies on gastrin mRNA structure using an oligonucleotide probe.";
RL   Ann. N. Y. Acad. Sci. 343:433-442(1980).
RN   [3]
RP   PROTEIN SEQUENCE OF 76-92.
RX   PubMed=14248711; DOI=10.1038/204931a0;
RA   Gregory H., Hardy P.M., Jones D.S., Kenner G.W., Sheppard R.C.;
RT   "The antral hormone gastrin. Structure of gastrin.";
RL   Nature 204:931-933(1964).
RN   [4]
RP   SYNTHESIS.
RX   PubMed=14248712; DOI=10.1038/204933a0;
RA   Anderson J.C., Barton M.A., Gregory R.A., Hardy P.M., Kenner G.W.,
RA   McLeod J.K., Preston J., Sheppard R.C., Morley J.S.;
RT   "Synthesis of gastrin.";
RL   Nature 204:933-934(1964).
RN   [5]
RP   PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY, AND SULFATION
RP   AT TYR-87.
RX   PubMed=7530658; DOI=10.1002/j.1460-2075.1995.tb07013.x;
RA   Rehfeld J.F., Hansen C.P., Johnsen A.H.;
RT   "Post-poly(Glu) cleavage and degradation modified by O-sulfated tyrosine: a
RT   novel post-translational processing mechanism.";
RL   EMBO J. 14:389-396(1995).
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. Thus, gastrin-6 is almost 73% sulfated, whereas the larger
CC       gastrins are less than 50% sulfated. Sulfation levels are also tissue-
CC       specific. {ECO:0000269|PubMed:7530658}.
CC   -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC       {ECO:0000305}.
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DR   EMBL; V01303; CAA24610.1; -; mRNA.
DR   EMBL; M25036; AAA31111.1; -; mRNA.
DR   PIR; A93903; GMPGB.
DR   RefSeq; NP_001004036.1; NM_001004036.2.
DR   AlphaFoldDB; P01351; -.
DR   STRING; 9823.ENSSSCP00000022312; -.
DR   PaxDb; P01351; -.
DR   GeneID; 445524; -.
DR   KEGG; ssc:445524; -.
DR   CTD; 2520; -.
DR   eggNOG; ENOG502SA9S; Eukaryota.
DR   InParanoid; P01351; -.
DR   OrthoDB; 1589970at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0032094; P:response to food; IBA:GO_Central.
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; Pyrrolidone carboxylic acid; Reference proteome;
KW   Secreted; Signal; Sulfation.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..58
FT                   /id="PRO_0000010644"
FT   PEPTIDE         59..92
FT                   /note="Big gastrin"
FT                   /id="PRO_0000010645"
FT   PEPTIDE         76..92
FT                   /note="Gastrin"
FT                   /id="PRO_0000010646"
FT   PROPEP          96..104
FT                   /id="PRO_0000010647"
FT   REGION          27..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         59
FT                   /note="Pyrrolidone carboxylic acid; in form big gastrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01350"
FT   MOD_RES         76
FT                   /note="Pyrrolidone carboxylic acid; in form gastrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01350"
FT   MOD_RES         87
FT                   /note="Sulfotyrosine; partial"
FT                   /evidence="ECO:0000269|PubMed:7530658"
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;  11558 MW;  B0BD1D7E05304B79 CRC64;
     MQRLCAYVLI HVLALAACSE ASWKPGFQLQ DASSGPGANR GKEPHELDRL GPASHHRRQL
     GLQGPPHLVA DLAKKQGPWM EEEEEAYGWM DFGRRSAEEG DQRP