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Protein

Glutathione S-transferase omega-2

Gene

Gsto2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) (By similarity).By similarity

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.
Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei32 – 321NucleophileBy similarity
Binding sitei59 – 591GlutathioneBy similarity
Binding sitei72 – 721Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

  1. glutathione dehydrogenase (ascorbate) activity Source: UniProtKB
  2. glutathione transferase activity Source: UniProtKB-EC
  3. methylarsonate reductase activity Source: UniProtKB-EC
  4. oxidoreductase activity Source: UniProtKB

GO - Biological processi

  1. cellular response to arsenic-containing substance Source: UniProtKB
  2. L-ascorbic acid metabolic process Source: UniProtKB
  3. oxidation-reduction process Source: UniProtKB
  4. xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Enzyme and pathway databases

ReactomeiREACT_287684. Vitamin C (ascorbate) metabolism.
REACT_317599. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase omega-2 (EC:2.5.1.18)
Short name:
GSTO-2
Alternative name(s):
Glutathione S-transferase omega 2-2
Short name:
GSTO 2-2
Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1)
Monomethylarsonic acid reductase (EC:1.20.4.2)
Short name:
MMA(V) reductase
Gene namesi
Name:Gsto2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1915464. Gsto2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 248248Glutathione S-transferase omega-2PRO_0000239141Add
BLAST

Proteomic databases

PaxDbiQ8K2Q2.
PRIDEiQ8K2Q2.

PTM databases

PhosphoSiteiQ8K2Q2.

Expressioni

Gene expression databases

BgeeiQ8K2Q2.
CleanExiMM_GSTO2.
ExpressionAtlasiQ8K2Q2. baseline and differential.
GenevestigatoriQ8K2Q2.

Structurei

3D structure databases

ProteinModelPortaliQ8K2Q2.
SMRiQ8K2Q2. Positions 7-239.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 10180GST N-terminalAdd
BLAST
Domaini106 – 231126GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni85 – 862Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Omega family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00390000005479.
HOGENOMiHOG000006560.
HOVERGENiHBG051853.
InParanoidiQ8K2Q2.
KOiK00799.
OMAiVYGIADC.
OrthoDBiEOG71CFNG.
PhylomeDBiQ8K2Q2.
TreeFamiTF105325.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
PRINTSiPR01625. GSTRNSFRASEO.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K2Q2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGDLSRCLG KGSCPPGPVP EGVIRIYSMR FCPYSHRARL VLKAKGIRHE
60 70 80 90 100
VININLKSKP DWYYTKHPFG QIPVLENSQC QLVYESVIAC EYLDDVYPGR
110 120 130 140 150
KLFPYDPYER ARQKMLLELF CKVPPLSKEC LIALRCGRDC TDLKVALRQE
160 170 180 190 200
LCNMEEILEY QNTTFFGGDC ISMIDYLVWP WFERLDVYGL ADCVNHTPML
210 220 230 240
RLWIASMKQD PAVCALHTDK SVFLGFLNLY FQNNPCAFDF GLCNPIIR
Length:248
Mass (Da):28,599
Last modified:October 1, 2002 - v1
Checksum:iADB9FCFCA9F0FE48
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077086 mRNA. Translation: BAC36604.1.
BC030371 mRNA. Translation: AAH30371.1.
CCDSiCCDS29894.1.
RefSeqiNP_080895.2. NM_026619.2.
NP_084327.1. NM_030051.1.
UniGeneiMm.63791.

Genome annotation databases

EnsembliENSMUST00000056159; ENSMUSP00000052592; ENSMUSG00000025069.
ENSMUST00000120645; ENSMUSP00000113409; ENSMUSG00000025069.
GeneIDi68214.
KEGGimmu:68214.
UCSCiuc008hvs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077086 mRNA. Translation: BAC36604.1.
BC030371 mRNA. Translation: AAH30371.1.
CCDSiCCDS29894.1.
RefSeqiNP_080895.2. NM_026619.2.
NP_084327.1. NM_030051.1.
UniGeneiMm.63791.

3D structure databases

ProteinModelPortaliQ8K2Q2.
SMRiQ8K2Q2. Positions 7-239.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ8K2Q2.

Proteomic databases

PaxDbiQ8K2Q2.
PRIDEiQ8K2Q2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000056159; ENSMUSP00000052592; ENSMUSG00000025069.
ENSMUST00000120645; ENSMUSP00000113409; ENSMUSG00000025069.
GeneIDi68214.
KEGGimmu:68214.
UCSCiuc008hvs.1. mouse.

Organism-specific databases

CTDi119391.
MGIiMGI:1915464. Gsto2.

Phylogenomic databases

eggNOGiCOG0625.
GeneTreeiENSGT00390000005479.
HOGENOMiHOG000006560.
HOVERGENiHBG051853.
InParanoidiQ8K2Q2.
KOiK00799.
OMAiVYGIADC.
OrthoDBiEOG71CFNG.
PhylomeDBiQ8K2Q2.
TreeFamiTF105325.

Enzyme and pathway databases

ReactomeiREACT_287684. Vitamin C (ascorbate) metabolism.
REACT_317599. Glutathione conjugation.

Miscellaneous databases

NextBioi326722.
PROiQ8K2Q2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K2Q2.
CleanExiMM_GSTO2.
ExpressionAtlasiQ8K2Q2. baseline and differential.
GenevestigatoriQ8K2Q2.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
PRINTSiPR01625. GSTRNSFRASEO.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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: Testis.
  2. "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: FVB/N-3.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiGSTO2_MOUSE
AccessioniPrimary (citable) accession number: Q8K2Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: October 1, 2002
Last modified: April 1, 2015
This is version 94 of the entry and version 1 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.