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P48757

- GAST_MOUSE

UniProt

P48757 - GAST_MOUSE

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Protein
Gastrin
Gene
Gast, Gas
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. protein binding Source: MGI
Complete GO annotation...

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiREACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_207651. G alpha (q) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Gastrin
Cleaved into the following 3 chains:
Gastrin-71
Short name:
G71
Alternative name(s):
Gastrin-34
Short name:
G34
Gene namesi
Name:Gast
Synonyms:Gas
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:104768. Gast.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Peptidei22 – 9271Gastrin-71
PRO_0000010640Add
BLAST
Peptidei59 – 9234Big gastrin
PRO_0000010641Add
BLAST
Peptidei76 – 9217Gastrin
PRO_0000010642Add
BLAST
Propeptidei96 – 1016 By similarity
PRO_0000010643

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591Pyrrolidone carboxylic acid By similarity
Modified residuei76 – 761Pyrrolidone carboxylic acid By similarity
Modified residuei87 – 871Sulfotyrosine By similarity
Modified residuei92 – 921Phenylalanine amide
Modified residuei96 – 961Phosphoserine By similarity

Post-translational modificationi

Sulfation enhances proteolytic processing, and blocks peptide degradation. Levels of sulfation differ between proteolytically-cleaved gastrins and between tissues By similarity.

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Phosphoprotein, Pyrrolidone carboxylic acid, Sulfation

PTM databases

PhosphoSiteiP48757.

Expressioni

Tissue specificityi

Abundantly expressed in the stomach and duodenum. Low levels in brain, ovary and pancreas.1 Publication

Gene expression databases

CleanExiMM_GAST.
GenevestigatoriP48757.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG39909.
GeneTreeiENSGT00390000014792.
HOGENOMiHOG000073533.
HOVERGENiHBG097593.
InParanoidiP48757.
KOiK13768.
OMAiKQRPRME.
OrthoDBiEOG72ZCH9.
TreeFamiTF336994.

Family and domain databases

InterProiIPR001651. Gastrin.
IPR013152. Gastrin/cholecystokinin_CS.
[Graphical view]
PfamiPF00918. Gastrin. 1 hit.
[Graphical view]
SMARTiSM00029. GASTRIN. 1 hit.
[Graphical view]
PROSITEiPS00259. GASTRIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P48757-1 [UniParc]FASTAAdd to Basket

« Hide

MPRLCVYMLV LVLALATFSE ASWKPRSQLQ DASSGPGTNE DLEQRQFNKL    50
GSASHHRRQL GPQGPQHFIA DLSKKQRPRM EEEEEAYGWM DFGRRSAEED 100
Q 101
Length:101
Mass (Da):11,590
Last modified:October 3, 2012 - v2
Checksum:i41DE15814DBFB68E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451R → G in AAB06947. 1 Publication
Sequence conflicti62 – 621P → L in AAB97872. 1 Publication
Sequence conflicti62 – 621P → L in AAB06947. 1 Publication
Sequence conflicti62 – 621P → L in CAA64385. 1 Publication
Sequence conflicti62 – 621P → L in CAA64386. 1 Publication
Sequence conflicti76 – 761Q → E in AAB97872. 1 Publication
Sequence conflicti76 – 761Q → E in AAB06947. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U34293 Genomic DNA. Translation: AAB97872.1.
U58136 Genomic DNA. Translation: AAB06947.1.
X94760 Genomic DNA. Translation: CAA64386.1.
X94758 mRNA. Translation: CAA64385.1.
AK008062 mRNA. Translation: BAB25437.1.
AK008159 mRNA. Translation: BAB25501.1.
AK008313 mRNA. Translation: BAB25596.1.
AK008420 mRNA. Translation: BAB25658.1.
AK008494 mRNA. Translation: BAB25699.1.
AK008649 mRNA. Translation: BAB25807.1.
AL590968 Genomic DNA. Translation: CAM23027.1.
CCDSiCCDS25418.1.
PIRiS68861.
RefSeqiNP_034387.3. NM_010257.3.
UniGeneiMm.4767.

Genome annotation databases

EnsembliENSMUST00000017309; ENSMUSP00000017309; ENSMUSG00000017165.
GeneIDi14459.
KEGGimmu:14459.
UCSCiuc007lkw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U34293 Genomic DNA. Translation: AAB97872.1 .
U58136 Genomic DNA. Translation: AAB06947.1 .
X94760 Genomic DNA. Translation: CAA64386.1 .
X94758 mRNA. Translation: CAA64385.1 .
AK008062 mRNA. Translation: BAB25437.1 .
AK008159 mRNA. Translation: BAB25501.1 .
AK008313 mRNA. Translation: BAB25596.1 .
AK008420 mRNA. Translation: BAB25658.1 .
AK008494 mRNA. Translation: BAB25699.1 .
AK008649 mRNA. Translation: BAB25807.1 .
AL590968 Genomic DNA. Translation: CAM23027.1 .
CCDSi CCDS25418.1.
PIRi S68861.
RefSeqi NP_034387.3. NM_010257.3.
UniGenei Mm.4767.

3D structure databases

ModBasei Search...

PTM databases

PhosphoSitei P48757.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000017309 ; ENSMUSP00000017309 ; ENSMUSG00000017165 .
GeneIDi 14459.
KEGGi mmu:14459.
UCSCi uc007lkw.2. mouse.

Organism-specific databases

CTDi 2520.
MGIi MGI:104768. Gast.

Phylogenomic databases

eggNOGi NOG39909.
GeneTreei ENSGT00390000014792.
HOGENOMi HOG000073533.
HOVERGENi HBG097593.
InParanoidi P48757.
KOi K13768.
OMAi KQRPRME.
OrthoDBi EOG72ZCH9.
TreeFami TF336994.

Enzyme and pathway databases

Reactomei REACT_188573. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_207651. G alpha (q) signalling events.

Miscellaneous databases

NextBioi 286088.
PROi P48757.
SOURCEi Search...

Gene expression databases

CleanExi MM_GAST.
Genevestigatori P48757.

Family and domain databases

InterProi IPR001651. Gastrin.
IPR013152. Gastrin/cholecystokinin_CS.
[Graphical view ]
Pfami PF00918. Gastrin. 1 hit.
[Graphical view ]
SMARTi SM00029. GASTRIN. 1 hit.
[Graphical view ]
PROSITEi PS00259. GASTRIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequencing of the murine gastrin gene."
    Koh T.J., Wang T.C.
    Biochem. Biophys. Res. Commun. 216:34-41(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  2. "Sequences responsible for transcription termination of the mouse gastrin gene."
    Noh M.J., Kim S.J., Kang Y.K., Yoo O.J.
    Biochem. Mol. Biol. Int. 35:1205-1213(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/c.
  3. "Molecular structure and genetic mapping of the mouse gastrin gene."
    Friis-Hansen L., Rourke I.J., Bundgaard J.R., Rehfeld J.F., Samuelson L.C.
    FEBS Lett. 386:128-132(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
    Strain: 129/SvJ.
    Tissue: Stomach.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Small intestine and Stomach.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiGAST_MOUSE
AccessioniPrimary (citable) accession number: P48757
Secondary accession number(s): P70334, Q64295, Q9CPR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 3, 2012
Last modified: September 3, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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