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O09131 (GSTO1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase omega-1

Short name=GSTO-1
EC=2.5.1.18
Alternative name(s):
Glutathione S-transferase omega 1-1
Short name=GSTO 1-1
Glutathione-dependent dehydroascorbate reductase
EC=1.8.5.1
Monomethylarsonic acid reductase
Short name=MMA(V) reductase
EC=1.20.4.2
S-(Phenacyl)glutathione reductase
Short name=SPG-R
p28
Gene names
Name:Gsto1
Synonyms:Gstx, Gtsttl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid By similarity.

Catalytic activity

RX + glutathione = HX + R-S-glutathione.

2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.

Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasmcytosol By similarity.

Sequence similarities

Belongs to the GST superfamily. Omega family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionOxidoreductase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-ascorbic acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to arsenic-containing substance

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of ryanodine-sensitive calcium-release channel activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of ryanodine-sensitive calcium-release channel activity

Inferred from electronic annotation. Source: Ensembl

regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

xenobiotic catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione dehydrogenase (ascorbate) activity

Inferred from sequence or structural similarity. Source: UniProtKB

glutathione transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

methylarsonate reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

oxidoreductase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 240239Glutathione S-transferase omega-1
PRO_0000185885

Regions

Domain22 – 10180GST N-terminal
Domain106 – 227122GST C-terminal
Region85 – 862Glutathione binding By similarity

Sites

Active site321Nucleophile By similarity
Binding site591Glutathione By similarity
Binding site721Glutathione; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue571N6-acetyllysine By similarity
Modified residue1521N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O09131 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: 17FEB52DB4BBE506

FASTA24027,498
        10         20         30         40         50         60 
MSGESSRSLG KGSAPPGPVP EGQIRVYSMR FCPFAQRTLM VLKAKGIRHE VININLKNKP 

        70         80         90        100        110        120 
EWFFEKNPLG LVPVLENSQG HLVTESVITC EYLDEAYPEK KLFPDDPYKK ARQKMTLESF 

       130        140        150        160        170        180 
SKVPPLIASF VRSKRKEDSP NLREALENEF KKLEEGMDNY KSFLGGDSPS MVDYLTWPWF 

       190        200        210        220        230        240 
QRLEALELKE CLAHTPKLKL WMAAMQQDPV ASSHKIDAKT YREYLNLYLQ DSPEACDYGL 

« Hide

References

« Hide 'large scale' references
[1]"The cloning and characterization of a new stress response protein. A mammalian member of a family of theta class glutathione s-transferase-like proteins."
Kodym R., Calkins P., Story M.D.
J. Biol. Chem. 274:5131-5137(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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: Amnion.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U80819 mRNA. Translation: AAB70110.1.
AK027922 mRNA. Translation: BAC25667.1.
AK146834 mRNA. Translation: BAE27469.1.
AK168383 mRNA. Translation: BAE40311.1.
BC085165 mRNA. Translation: AAH85165.1.
CCDSCCDS29893.1.
RefSeqNP_034492.1. NM_010362.2.
UniGeneMm.378931.

3D structure databases

ProteinModelPortalO09131.
SMRO09131. Positions 3-240.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO09131. 2 interactions.
MINTMINT-1868625.
STRING10090.ENSMUSP00000026050.

PTM databases

PhosphoSiteO09131.

2D gel databases

REPRODUCTION-2DPAGEIPI00114285.

Proteomic databases

MaxQBO09131.
PaxDbO09131.
PRIDEO09131.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026050; ENSMUSP00000026050; ENSMUSG00000025068.
GeneID14873.
KEGGmmu:14873.
UCSCuc008hvq.1. mouse.

Organism-specific databases

CTD9446.
MGIMGI:1342273. Gsto1.

Phylogenomic databases

eggNOGCOG0625.
GeneTreeENSGT00390000005479.
HOGENOMHOG000006560.
HOVERGENHBG051853.
InParanoidO09131.
KOK00799.
OMAAYANEMP.
OrthoDBEOG71CFNG.
PhylomeDBO09131.
TreeFamTF105325.

Gene expression databases

BgeeO09131.
CleanExMM_GSTO1.
GenevestigatorO09131.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
PRINTSPR01625. GSTRNSFRASEO.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio287145.
PROO09131.
SOURCESearch...

Entry information

Entry nameGSTO1_MOUSE
AccessionPrimary (citable) accession number: O09131
Secondary accession number(s): Q3TH87
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot