GenomeNet

Database: UniProt/SWISS-PROT
Entry: GSTO2_MOUSE
LinkDB: GSTO2_MOUSE
Original site: GSTO2_MOUSE 
ID   GSTO2_MOUSE             Reviewed;         248 AA.
AC   Q8K2Q2;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   13-FEB-2019, entry version 122.
DE   RecName: Full=Glutathione S-transferase omega-2;
DE            Short=GSTO-2;
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:Q9H4Y5};
DE   AltName: Full=Glutathione S-transferase omega 2-2;
DE            Short=GSTO 2-2;
DE   AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE            EC=1.8.5.1 {ECO:0000250|UniProtKB:Q9H4Y5};
DE   AltName: Full=Monomethylarsonic acid reductase;
DE            Short=MMA(V) reductase;
DE            EC=1.20.4.2 {ECO:0000250|UniProtKB:Q9H4Y5};
GN   Name=Gsto2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Exhibits glutathione-dependent thiol transferase
CC       activity. Has high dehydroascorbate reductase activity and may
CC       contribute to the recycling of ascorbic acid. Participates in the
CC       biotransformation of inorganic arsenic and reduces
CC       monomethylarsonic acid (MMA). {ECO:0000250|UniProtKB:Q9H4Y5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000250|UniProtKB:Q9H4Y5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + L-dehydroascorbate = glutathione
CC         disulfide + L-ascorbate; Xref=Rhea:RHEA:24424,
CC         ChEBI:CHEBI:38290, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC         ChEBI:CHEBI:58539; EC=1.8.5.1;
CC         Evidence={ECO:0000250|UniProtKB:Q9H4Y5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H(+) + methylarsonate = glutathione
CC         disulfide + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17826,
CC         ChEBI:CHEBI:33409, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297;
CC         EC=1.20.4.2; Evidence={ECO:0000250|UniProtKB:Q9H4Y5};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000305}.
DR   EMBL; AK077086; BAC36604.1; -; mRNA.
DR   EMBL; BC030371; AAH30371.1; -; mRNA.
DR   CCDS; CCDS29894.1; -.
DR   RefSeq; NP_080895.2; NM_026619.2.
DR   RefSeq; NP_084327.1; NM_030051.1.
DR   UniGene; Mm.63791; -.
DR   ProteinModelPortal; Q8K2Q2; -.
DR   SMR; Q8K2Q2; -.
DR   IntAct; Q8K2Q2; 1.
DR   STRING; 10090.ENSMUSP00000052592; -.
DR   PhosphoSitePlus; Q8K2Q2; -.
DR   jPOST; Q8K2Q2; -.
DR   MaxQB; Q8K2Q2; -.
DR   PaxDb; Q8K2Q2; -.
DR   PRIDE; Q8K2Q2; -.
DR   Ensembl; ENSMUST00000056159; ENSMUSP00000052592; ENSMUSG00000025069.
DR   Ensembl; ENSMUST00000120645; ENSMUSP00000113409; ENSMUSG00000025069.
DR   GeneID; 68214; -.
DR   KEGG; mmu:68214; -.
DR   UCSC; uc008hvr.1; mouse.
DR   CTD; 119391; -.
DR   MGI; MGI:1915464; Gsto2.
DR   eggNOG; KOG0406; Eukaryota.
DR   eggNOG; ENOG410XSIX; LUCA.
DR   GeneTree; ENSGT00940000162030; -.
DR   HOGENOM; HOG000006560; -.
DR   HOVERGEN; HBG051853; -.
DR   InParanoid; Q8K2Q2; -.
DR   KO; K00799; -.
DR   OMA; ADHYSHR; -.
DR   OrthoDB; 1225872at2759; -.
DR   PhylomeDB; Q8K2Q2; -.
DR   TreeFam; TF105325; -.
DR   Reactome; R-MMU-156590; Glutathione conjugation.
DR   Reactome; R-MMU-196836; Vitamin C (ascorbate) metabolism.
DR   PRO; PR:Q8K2Q2; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   Bgee; ENSMUSG00000025069; Expressed in 89 organ(s), highest expression level in testis.
DR   ExpressionAtlas; Q8K2Q2; baseline and differential.
DR   Genevisible; Q8K2Q2; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; ISS:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR   GO; GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; ISS:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR005442; GST_omega.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13417; GST_N_3; 1.
DR   PRINTS; PR01625; GSTRNSFRASEO.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Oxidoreductase; Reference proteome; Transferase.
FT   CHAIN         1    248       Glutathione S-transferase omega-2.
FT                                /FTId=PRO_0000239141.
FT   DOMAIN       22    101       GST N-terminal.
FT   DOMAIN      106    231       GST C-terminal.
FT   REGION       85     86       Glutathione binding.
FT                                {ECO:0000250|UniProtKB:Q9H4Y5}.
FT   ACT_SITE     32     32       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   BINDING      59     59       Glutathione.
FT                                {ECO:0000250|UniProtKB:Q9H4Y5}.
FT   BINDING      72     72       Glutathione; via amide nitrogen and
FT                                carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:Q9H4Y5}.
SQ   SEQUENCE   248 AA;  28599 MW;  ADB9FCFCA9F0FE48 CRC64;
     MSGDLSRCLG KGSCPPGPVP EGVIRIYSMR FCPYSHRARL VLKAKGIRHE VININLKSKP
     DWYYTKHPFG QIPVLENSQC QLVYESVIAC EYLDDVYPGR KLFPYDPYER ARQKMLLELF
     CKVPPLSKEC LIALRCGRDC TDLKVALRQE LCNMEEILEY QNTTFFGGDC ISMIDYLVWP
     WFERLDVYGL ADCVNHTPML RLWIASMKQD PAVCALHTDK SVFLGFLNLY FQNNPCAFDF
     GLCNPIIR
//
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