GAST_CANLF
ID GAST_CANLF Reviewed; 104 AA.
AC P01353;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 131.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Gastric mucosa;
RX PubMed=2262079; DOI=10.1159/000200372;
RA Gantz I., Takeuchi T., Yamada T.;
RT "Cloning of canine gastrin cDNA's encoding variant amino acid sequences.";
RL Digestion 46:99-104(1990).
RN [2]
RP PROTEIN SEQUENCE OF 59-92, PYROGLUTAMATE FORMATION AT GLN-59 AND GLN-76,
RP SULFATION AT TYR-87, AND AMIDATION AT PHE-92.
RC TISSUE=Gastric mucosa;
RX PubMed=3763441; DOI=10.1016/0196-9781(86)90045-8;
RA Bonato C., Eng J., Hulmes J.D., Miedel M., Pan Y.-C.E., Yalow R.S.;
RT "Sequences of gastrins purified from a single antrum of dog and of goat.";
RL Peptides 7:689-693(1986).
RN [3]
RP PROTEIN SEQUENCE OF 76-92, AND PHOSPHORYLATION.
RX PubMed=5799207; DOI=10.1007/bf01899905;
RA Agarwal K.L., Kenner G.W., Sheppard R.C.;
RT "Structure and synthesis of canine gastrin.";
RL Experientia 25:346-348(1969).
RN [4]
RP PROTEIN SEQUENCE OF 96-104, AND PHOSPHORYLATION AT SER-96.
RC TISSUE=Gastric mucosa;
RX PubMed=2756156; DOI=10.1016/0167-0115(89)90264-4;
RA Desmond H., Varro A., Young J., Gregory H., Nemeth J., Dockray G.J.;
RT "The constitution and properties of phosphorylated and unphosphorylated C-
RT terminal fragments of progastrin from dog and ferret antrum.";
RL Regul. Pept. 25:223-233(1989).
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 -!- SIMILARITY: Belongs to the gastrin/cholecystokinin family.
CC {ECO:0000305}.
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DR PIR; B61053; GMDG.
DR RefSeq; XP_003435286.1; XM_003435238.3.
DR AlphaFoldDB; P01353; -.
DR STRING; 9615.ENSCAFP00000023420; -.
DR iPTMnet; P01353; -.
DR PaxDb; P01353; -.
DR Ensembl; ENSCAFT00030035728; ENSCAFP00030031159; ENSCAFG00030019442.
DR Ensembl; ENSCAFT00040019141; ENSCAFP00040016613; ENSCAFG00040010324.
DR Ensembl; ENSCAFT00845021253; ENSCAFP00845016712; ENSCAFG00845011939.
DR GeneID; 100685087; -.
DR KEGG; cfa:100685087; -.
DR CTD; 2520; -.
DR VEuPathDB; HostDB:ENSCAFG00845011939; -.
DR eggNOG; ENOG502SA9S; Eukaryota.
DR GeneTree; ENSGT00390000014792; -.
DR HOGENOM; CLU_2249245_0_0_1; -.
DR InParanoid; P01353; -.
DR OMA; KPRSQLQ; -.
DR OrthoDB; 1589970at2759; -.
DR TreeFam; TF336994; -.
DR Reactome; R-CFA-416476; G alpha (q) signalling events.
DR Proteomes; UP000002254; Chromosome 9.
DR Bgee; ENSCAFG00000015924; Expressed in thymus and 5 other tissues.
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 /evidence="ECO:0000269|PubMed:3763441"
FT /id="PRO_0000010613"
FT PEPTIDE 59..92
FT /note="Big gastrin"
FT /id="PRO_0000010614"
FT PEPTIDE 76..92
FT /note="Gastrin"
FT /id="PRO_0000010615"
FT PROPEP 96..104
FT /id="PRO_0000010616"
FT REGION 22..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 59
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:3763441"
FT MOD_RES 76
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:3763441"
FT MOD_RES 87
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:3763441"
FT MOD_RES 92
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:3763441"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:2756156"
FT VARIANT 85
FT /note="A -> T"
FT CONFLICT 83..85
FT /note="EEA -> AEE (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 104 AA; 11519 MW; 73BF72A18DFE78CA CRC64;
MQRLCVYVLI LALALATFSE ASWKPRSRLQ DAPSGPGANR GLEPHGLDQL GPASHHRRQL
GLQGPPQLVA DLSKKQGPWM EEEEAAYGWM DFGRRSAEEG DQRP