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Protein

Gastrin

Gene

Gast

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 - Biological processi

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

Keywords - Molecular functioni

Hormone

Enzyme and pathway databases

ReactomeiREACT_337888. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_347934. 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 Componenti: 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 – 2121Sequence AnalysisAdd
BLAST
Peptidei22 – 9271Gastrin-71PRO_0000010640Add
BLAST
Peptidei59 – 9234Big gastrinPRO_0000010641Add
BLAST
Peptidei76 – 9217GastrinPRO_0000010642Add
BLAST
Propeptidei96 – 1016By similarityPRO_0000010643

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591Pyrrolidone carboxylic acidBy similarity
Modified residuei76 – 761Pyrrolidone carboxylic acidBy similarity
Modified residuei87 – 871SulfotyrosineBy similarity
Modified residuei92 – 921Phenylalanine amide
Modified residuei96 – 961PhosphoserineBy 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).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.
ExpressionAtlasiP48757. differential.
GenevestigatoriP48757.

Family & Domainsi

Sequence similaritiesi

Belongs to the gastrin/cholecystokinin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG39909.
GeneTreeiENSGT00390000014792.
HOGENOMiHOG000073533.
HOVERGENiHBG097593.
InParanoidiP48757.
KOiK13768.
OMAiKPRSQLQ.
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

        10         20         30         40         50
MPRLCVYMLV LVLALATFSE ASWKPRSQLQ DASSGPGTNE DLEQRQFNKL
60 70 80 90 100
GSASHHRRQL GPQGPQHFIA DLSKKQRPRM EEEEEAYGWM DFGRRSAEED

Q
Length:101
Mass (Da):11,590
Last modified:October 2, 2012 - v2
Checksum:i41DE15814DBFB68E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451R → G in AAB06947 (PubMed:7492958).Curated
Sequence conflicti62 – 621P → L in AAB97872 (PubMed:7488110).Curated
Sequence conflicti62 – 621P → L in AAB06947 (PubMed:7492958).Curated
Sequence conflicti62 – 621P → L in CAA64385 (PubMed:8647266).Curated
Sequence conflicti62 – 621P → L in CAA64386 (PubMed:8647266).Curated
Sequence conflicti76 – 761Q → E in AAB97872 (PubMed:7488110).Curated
Sequence conflicti76 – 761Q → E in AAB06947 (PubMed:7492958).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiP48757.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2520.
MGIiMGI:104768. Gast.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_337888. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_347934. G alpha (q) signalling events.

Miscellaneous databases

NextBioi286088.
PROiP48757.
SOURCEiSearch...

Gene expression databases

CleanExiMM_GAST.
ExpressionAtlasiP48757. differential.
GenevestigatoriP48757.

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]
ProtoNetiSearch...

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(1994) [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(1994) [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(1995) [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(2004) [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: January 31, 1996
Last sequence update: October 2, 2012
Last modified: March 31, 2015
This is version 105 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.