GAST_MOUSE
ID GAST_MOUSE Reviewed; 101 AA.
AC P48757; P70334; Q64295; Q9CPR2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Gastrin;
DE Contains:
DE RecName: Full=Gastrin-71;
DE Short=G71;
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=7488110; DOI=10.1006/bbrc.1995.2588;
RA Koh T.J., Wang T.C.;
RT "Molecular cloning and sequencing of the murine gastrin gene.";
RL Biochem. Biophys. Res. Commun. 216:34-41(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=7492958;
RA Noh M.J., Kim S.J., Kang Y.K., Yoo O.J.;
RT "Sequences responsible for transcription termination of the mouse gastrin
RT gene.";
RL Biochem. Mol. Biol. Int. 35:1205-1213(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ; TISSUE=Stomach;
RX PubMed=8647266; DOI=10.1016/0014-5793(96)00430-9;
RA Friis-Hansen L., Rourke I.J., Bundgaard J.R., Rehfeld J.F., Samuelson L.C.;
RT "Molecular structure and genetic mapping of the mouse gastrin gene.";
RL FEBS Lett. 386:128-132(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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 -!- TISSUE SPECIFICITY: Abundantly expressed in the stomach and duodenum.
CC Low levels in brain, ovary and pancreas. {ECO:0000269|PubMed:8647266}.
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}.
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DR EMBL; U34293; AAB97872.1; -; Genomic_DNA.
DR EMBL; U58136; AAB06947.1; -; Genomic_DNA.
DR EMBL; X94760; CAA64386.1; -; Genomic_DNA.
DR EMBL; X94758; CAA64385.1; -; mRNA.
DR EMBL; AK008062; BAB25437.1; -; mRNA.
DR EMBL; AK008159; BAB25501.1; -; mRNA.
DR EMBL; AK008313; BAB25596.1; -; mRNA.
DR EMBL; AK008420; BAB25658.1; -; mRNA.
DR EMBL; AK008494; BAB25699.1; -; mRNA.
DR EMBL; AK008649; BAB25807.1; -; mRNA.
DR EMBL; AL590968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25418.1; -.
DR PIR; S68861; S68861.
DR RefSeq; NP_034387.3; NM_010257.4.
DR AlphaFoldDB; P48757; -.
DR STRING; 10090.ENSMUSP00000017309; -.
DR PhosphoSitePlus; P48757; -.
DR PaxDb; P48757; -.
DR PRIDE; P48757; -.
DR ProteomicsDB; 271671; -.
DR Antibodypedia; 3504; 426 antibodies from 35 providers.
DR Ensembl; ENSMUST00000017309; ENSMUSP00000017309; ENSMUSG00000017165.
DR GeneID; 14459; -.
DR KEGG; mmu:14459; -.
DR UCSC; uc007lkw.2; mouse.
DR CTD; 2520; -.
DR MGI; MGI:104768; Gast.
DR VEuPathDB; HostDB:ENSMUSG00000017165; -.
DR eggNOG; ENOG502SA9S; Eukaryota.
DR GeneTree; ENSGT00390000014792; -.
DR HOGENOM; CLU_2249245_0_0_1; -.
DR InParanoid; P48757; -.
DR OMA; KPRSQLQ; -.
DR OrthoDB; 1589970at2759; -.
DR PhylomeDB; P48757; -.
DR TreeFam; TF336994; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
DR BioGRID-ORCS; 14459; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Gast; mouse.
DR PRO; PR:P48757; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P48757; protein.
DR Bgee; ENSMUSG00000017165; Expressed in pyloric antrum and 41 other tissues.
DR Genevisible; P48757; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0032094; P:response to food; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
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 2: Evidence at transcript level;
KW Amidation; Cleavage on pair of basic residues; Hormone; Phosphoprotein;
KW Reference proteome; Secreted; Signal; Sulfation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PEPTIDE 22..92
FT /note="Gastrin-71"
FT /id="PRO_0000010640"
FT PEPTIDE 59..92
FT /note="Big gastrin"
FT /id="PRO_0000010641"
FT PEPTIDE 76..92
FT /note="Gastrin"
FT /id="PRO_0000010642"
FT PROPEP 96..101
FT /evidence="ECO:0000250"
FT /id="PRO_0000010643"
FT REGION 23..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..101
FT /note="Basic and acidic residues"
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|UniProtKB:P01350"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01353"
FT CONFLICT 45
FT /note="R -> G (in Ref. 2; AAB06947)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="P -> L (in Ref. 1; AAB97872, 2; AAB06947 and 3;
FT CAA64385/CAA64386)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="Q -> E (in Ref. 1; AAB97872 and 2; AAB06947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 101 AA; 11590 MW; 41DE15814DBFB68E CRC64;
MPRLCVYMLV LVLALATFSE ASWKPRSQLQ DASSGPGTNE DLEQRQFNKL GSASHHRRQL
GPQGPQHFIA DLSKKQRPRM EEEEEAYGWM DFGRRSAEED Q
