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Gastrin [Cleaved into: Gastrin-71 (Gastrin component I); Gastrin-52 (G52); Big gastrin (Gastrin component II) (Gastrin-34) (G34); Gastrin (Gastrin component III) (Gastrin-17) (G17); Gastrin-14 (G14); Gastrin-6 (G6)]

 GAST_HUMAN              Reviewed;         101 AA.
P01350; P78463; P78464;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-OCT-1986, sequence version 1.
18-JUL-2018, entry version 168.
RecName: Full=Gastrin;
Contains:
RecName: Full=Gastrin-71;
AltName: Full=Gastrin component I;
Contains:
RecName: Full=Gastrin-52;
Short=G52;
Contains:
RecName: Full=Big gastrin;
AltName: Full=Gastrin component II;
AltName: Full=Gastrin-34;
Short=G34;
Contains:
RecName: Full=Gastrin;
AltName: Full=Gastrin component III;
AltName: Full=Gastrin-17;
Short=G17;
Contains:
RecName: Full=Gastrin-14;
Short=G14;
Contains:
RecName: Full=Gastrin-6;
Short=G6;
Flags: Precursor;
Name=GAST; Synonyms=GAS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3034736; DOI=10.1016/0378-1119(86)90338-0;
Kariya Y., Kato K., Hayashizaki Y., Himeno S., Tarui S., Matsubara K.;
"Expression of human gastrin gene in normal and gastrinoma tissues.";
Gene 50:345-352(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6087340; DOI=10.1073/pnas.81.15.4662;
Ito R., Sato K., Helmer T., Jay G., Agarwal K.L.;
"Structural analysis of the gene encoding human gastrin: the large
intron contains an Alu sequence.";
Proc. Natl. Acad. Sci. U.S.A. 81:4662-4666(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6324077; DOI=10.1093/nar/11.23.8197;
Kato K., Hayashizaki Y., Takahashi Y., Himeno S., Matsubara K.;
"Molecular cloning of the human gastrin gene.";
Nucleic Acids Res. 11:8197-8203(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6574456; DOI=10.1073/pnas.80.10.2866;
Boel E., Vuust J., Norris F., Norris K., Wind A., Rehfeld J.F.,
Marcker K.A.;
"Molecular cloning of human gastrin cDNA: evidence for evolution of
gastrin by gene duplication.";
Proc. Natl. Acad. Sci. U.S.A. 80:2866-2869(1983).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6322186; DOI=10.1073/pnas.81.4.1067;
Wiborg O., Berglund L., Boel E., Norris F., Norris K., Rehfeld J.F.,
Marcker K.A., Vuust J.;
"Structure of a human gastrin gene.";
Proc. Natl. Acad. Sci. U.S.A. 81:1067-1069(1984).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6689486; DOI=10.1016/0378-1119(83)90035-5;
Kato K., Himeno S., Takahashi Y., Wakabayashi T., Tarui S.,
Matsubara K.;
"Molecular cloning of human gastrin precursor cDNA.";
Gene 26:53-57(1983).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 22-101, AND CHARACTERIZATION OF GASTRIN 71.
TISSUE=Gastric mucosa;
PubMed=8055952; DOI=10.1111/j.1432-1033.1994.tb19051.x;
Rehfeld J.F., Johnsen A.H.;
"Identification of gastrin component I as gastrin-71. The largest
possible bioactive progastrin product.";
Eur. J. Biochem. 223:765-773(1994).
[9]
PROTEIN SEQUENCE OF 76-92, PYROGLUTAMATE FORMATION AT GLN-76, AND
AMIDATION AT PHE-92.
PubMed=5921183; DOI=10.1038/209583b0;
Bentley P.H., Kenner G.W., Sheppard R.C.;
"Structures of human gastrins I and II.";
Nature 209:583-585(1966).
[10]
PROTEIN SEQUENCE OF 59-68, AND PYROGLUTAMATE FORMATION AT GLN-59.
PubMed=2730647; DOI=10.1016/S0006-291X(89)80154-8;
Higashimoto Y., Himeno S., Shinomura Y., Nagao K., Tamura T.,
Tarui S.;
"Purification and structural determination of urinary NH2-terminal big
gastrin fragments.";
Biochem. Biophys. Res. Commun. 160:1364-1370(1989).
[11]
PROTEIN SEQUENCE OF 76-92.
PubMed=5822140; DOI=10.1136/gut.10.8.603;
Gregory R.A., Tracy H.J., Agarwal K.L., Grossman M.I.;
"Aminoacid constitution of two gastrins isolated from Zollinger-
Ellison tumour tissue.";
Gut 10:603-608(1969).
[12]
PHOSPHORYLATION AT SER-96.
PubMed=3223964; DOI=10.1042/bj2560951;
Varro A., Desmond H., Pauwels S., Gregory H., Young J., Dockray G.J.;
"The human gastrin precursor. Characterization of phosphorylated forms
and fragments.";
Biochem. J. 256:951-957(1988).
[13]
PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY, AND
SULFATION AT TYR-87.
PubMed=7530658;
Rehfeld J.F., Hansen C.P., Johnsen A.H.;
"Post-poly(Glu) cleavage and degradation modified by O-sulfated
tyrosine: a novel post-translational processing mechanism.";
EMBO J. 14:389-396(1995).
[14]
SULFATION, MUTAGENESIS OF ALA-86 AND TYR-87, AND PROTEOLYTIC
PROCESSING.
PubMed=7621822;
Bundgaard J.R., Vuust J., Rehfeld J.F.;
"Tyrosine O-sulfation promotes proteolytic processing of progastrin.";
EMBO J. 14:3073-3079(1995).
[15]
PROTEOLYTIC PROCESSING, AND SULFATION AT TYR-87.
PubMed=11052986;
Palnaes Hansen C., Stadil F., Rehfeld J.F.;
"Metabolism and acid secretory effect of sulfated and nonsulfated
gastrin-6 in humans.";
Am. J. Physiol. 279:G903-G909(2000).
-!- 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.
-!- INTERACTION:
P02787:TF; NbExp=5; IntAct=EBI-3436637, EBI-714319;
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: Two different processing pathways probably exist in antral G-
cells. In the dominant pathway progastrin is cleaved at three
sites resulting in two major bioactive gastrins, gastrin-34 and
gastrin-17. In the putative alternative pathway, progastrin may be
processed only at the most C-terminal dibasic site resulting in
the synthesis of gastrin-71.
-!- PTM: Sulfation enhances proteolytic processing, and blocks peptide
degradation. Levels of sulfation differ between proteolytically-
cleaved gastrins. Thus, gastrin-6 is almost 73% sulfated, whereas
the larger gastrins are less than 50% sulfated. Sulfation levels
are also tissue-specific. {ECO:0000269|PubMed:11052986,
ECO:0000269|PubMed:7530658, ECO:0000269|PubMed:7621822}.
-!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Gastrin entry;
URL="https://en.wikipedia.org/wiki/Gastrin";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GASTID44214ch17q21.html";
-----------------------------------------------------------------------
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EMBL; X00183; CAA25005.1; -; Genomic_DNA.
EMBL; X00183; CAA25006.1; -; Genomic_DNA.
EMBL; X00183; CAA25007.1; -; Genomic_DNA.
EMBL; V00511; CAA23769.1; -; mRNA.
EMBL; M15958; AAA52520.1; -; Genomic_DNA.
EMBL; K01254; AAB59533.1; -; Genomic_DNA.
EMBL; BC069724; AAH69724.1; -; mRNA.
EMBL; BC069762; AAH69762.1; -; mRNA.
CCDS; CCDS11404.1; -.
PIR; A93997; GMHUB.
RefSeq; NP_000796.1; NM_000805.4.
UniGene; Hs.2681; -.
PDB; 5WRJ; X-ray; 2.31 A; F/H/J/L=81-92.
PDBsum; 5WRJ; -.
ProteinModelPortal; P01350; -.
SMR; P01350; -.
BioGrid; 108796; 11.
DIP; DIP-403N; -.
IntAct; P01350; 17.
MINT; P01350; -.
STRING; 9606.ENSP00000331358; -.
iPTMnet; P01350; -.
PhosphoSitePlus; P01350; -.
BioMuta; GAST; -.
DMDM; 120952; -.
PaxDb; P01350; -.
PeptideAtlas; P01350; -.
PRIDE; P01350; -.
ProteomicsDB; 51377; -.
DNASU; 2520; -.
Ensembl; ENST00000329402; ENSP00000331358; ENSG00000184502.
GeneID; 2520; -.
KEGG; hsa:2520; -.
UCSC; uc002hxl.3; human.
CTD; 2520; -.
DisGeNET; 2520; -.
EuPathDB; HostDB:ENSG00000184502.3; -.
GeneCards; GAST; -.
HGNC; HGNC:4164; GAST.
HPA; CAB000038; -.
MIM; 137250; gene.
neXtProt; NX_P01350; -.
OpenTargets; ENSG00000184502; -.
PharmGKB; PA28577; -.
eggNOG; ENOG410J1ZA; Eukaryota.
eggNOG; ENOG4111D7Y; LUCA.
GeneTree; ENSGT00390000014792; -.
HOGENOM; HOG000073533; -.
HOVERGEN; HBG097593; -.
InParanoid; P01350; -.
KO; K13768; -.
OMA; KKQGPWM; -.
OrthoDB; EOG091G147Z; -.
PhylomeDB; P01350; -.
TreeFam; TF336994; -.
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
SIGNOR; P01350; -.
ChiTaRS; GAST; human.
GeneWiki; Gastrin; -.
GenomeRNAi; 2520; -.
PMAP-CutDB; P01350; -.
PRO; PR:P01350; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000184502; -.
CleanEx; HS_GAST; -.
ExpressionAtlas; P01350; baseline and differential.
Genevisible; P01350; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005179; F:hormone activity; IBA:GO_Central.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0032094; P:response to food; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; NAS:ProtInc.
InterPro; IPR039236; GAST.
InterPro; IPR001651; Gastrin.
InterPro; IPR013152; Gastrin/cholecystokinin_CS.
PANTHER; PTHR19309; PTHR19309; 1.
Pfam; PF00918; Gastrin; 1.
PROSITE; PS00259; GASTRIN; 1.
1: Evidence at protein level;
3D-structure; Amidation; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Hormone; Phosphoprotein;
Polymorphism; Pyrrolidone carboxylic acid; Reference proteome;
Secreted; Signal; Sulfation.
SIGNAL 1 21 {ECO:0000269|PubMed:8055952}.
PEPTIDE 22 92 Gastrin-71.
/FTId=PRO_0000010633.
PEPTIDE 41 92 Gastrin-52.
/FTId=PRO_0000010634.
PEPTIDE 59 92 Big gastrin.
/FTId=PRO_0000010635.
PEPTIDE 76 92 Gastrin.
/FTId=PRO_0000010636.
PEPTIDE 79 92 Gastrin-14.
/FTId=PRO_0000010637.
PEPTIDE 87 92 Gastrin-6.
/FTId=PRO_0000010638.
PROPEP 96 101 Removed in mature form.
/FTId=PRO_0000010639.
SITE 40 41 Cleavage.
SITE 58 59 Cleavage.
SITE 75 76 Cleavage.
SITE 95 96 Cleavage.
MOD_RES 59 59 Pyrrolidone carboxylic acid; in form big
gastrin. {ECO:0000269|PubMed:2730647}.
MOD_RES 76 76 Pyrrolidone carboxylic acid; in form
gastrin. {ECO:0000269|PubMed:5921183}.
MOD_RES 87 87 Sulfotyrosine; partial.
{ECO:0000269|PubMed:11052986,
ECO:0000269|PubMed:7530658}.
MOD_RES 92 92 Phenylalanine amide.
{ECO:0000269|PubMed:5921183}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000269|PubMed:3223964}.
VARIANT 3 3 R -> P (in dbSNP:rs34309618).
/FTId=VAR_049127.
MUTAGEN 86 86 A->D: Small increase in ratio of gastrin-
17 versus gastrin-34 production. No
change in ratio of gastrin-17 versus
gastrin-34 production; when associated
with F-87. {ECO:0000269|PubMed:7621822}.
MUTAGEN 87 87 Y->F: Small decrease in ratio of gastrin-
17 versus gastrin-34 production. No
change in ratio of gastrin-17 versus
gastrin-34 production; when associated
with D-86. {ECO:0000269|PubMed:7621822}.
SEQUENCE 101 AA; 11394 MW; A03C847FCFE7216C CRC64;
MQRLCVYVLI FALALAAFSE ASWKPRSQQP DAPLGTGANR DLELPWLEQQ GPASHHRRQL
GPQGPPHLVA DPSKKQGPWL EEEEEAYGWM DFGRRSAEDE N


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