Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8K2Q2 (GSTO2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 80. 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
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-2
Short name=GSTO-2
EC=2.5.1.18
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
Short name=MMA(V) reductase
EC=1.20.4.2
Gene names
Name:Gsto2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.

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

Sequence similarities

Belongs to the GST superfamily. Omega family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 248248Glutathione S-transferase omega-2
PRO_0000239141

Regions

Domain22 – 10180GST N-terminal
Domain106 – 231126GST 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

Sequences

Sequence LengthMass (Da)Tools
Q8K2Q2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: ADB9FCFCA9F0FE48

FASTA24828,599
        10         20         30         40         50         60 
MSGDLSRCLG KGSCPPGPVP EGVIRIYSMR FCPYSHRARL VLKAKGIRHE VININLKSKP 

        70         80         90        100        110        120 
DWYYTKHPFG QIPVLENSQC QLVYESVIAC EYLDDVYPGR KLFPYDPYER ARQKMLLELF 

       130        140        150        160        170        180 
CKVPPLSKEC LIALRCGRDC TDLKVALRQE LCNMEEILEY QNTTFFGGDC ISMIDYLVWP 

       190        200        210        220        230        240 
WFERLDVYGL ADCVNHTPML RLWIASMKQD PAVCALHTDK SVFLGFLNLY FQNNPCAFDF 


GLCNPIIR

« Hide

References

[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. 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: 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK077086 mRNA. Translation: BAC36604.1.
BC030371 mRNA. Translation: AAH30371.1.
IPIIPI00459308.
RefSeqNP_080895.2. NM_026619.2.
NP_084327.1. NM_030051.1.
UniGeneMm.63791.

3D structure databases

ProteinModelPortalQ8K2Q2.
SMRQ8K2Q2. Positions 7-239.
ModBaseSearch...

PTM databases

PhosphoSiteQ8K2Q2.

Proteomic databases

PaxDbQ8K2Q2.
PRIDEQ8K2Q2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000056159; ENSMUSP00000052592; ENSMUSG00000025069.
ENSMUST00000120645; ENSMUSP00000113409; ENSMUSG00000025069.
GeneID68214.
KEGGmmu:68214.
UCSCuc008hvs.1. mouse.

Organism-specific databases

CTD119391.
MGIMGI:1915464. Gsto2.

Phylogenomic databases

eggNOGCOG0625.
GeneTreeENSGT00390000005479.
HOGENOMHOG000006560.
HOVERGENHBG051853.
InParanoidQ8K2Q2.
KOK00799.
OMAVYGIADC.
OrthoDBEOG43TZW5.

Gene expression databases

ArrayExpressQ8K2Q2.
BgeeQ8K2Q2.
CleanExMM_GSTO2.
GenevestigatorQ8K2Q2.
GermOnlineENSMUSG00000025069. Mus musculus.

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.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PRINTSPR01625. GSTRNSFRASEO.
SUPFAMSSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio326722.
SOURCESearch...

Entry information

Entry nameGSTO2_MOUSE
AccessionPrimary (citable) accession number: Q8K2Q2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: October 1, 2002
Last modified: May 29, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents