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Database: UniProt/SWISS-PROT
Entry: GSTO2_RAT
LinkDB: GSTO2_RAT
Original site: GSTO2_RAT 
ID   GSTO2_RAT               Reviewed;         248 AA.
AC   Q6AXV9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   13-FEB-2019, entry version 114.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
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; BC079295; AAH79295.1; -; mRNA.
DR   RefSeq; NP_001012071.1; NM_001012071.1.
DR   RefSeq; XP_006231652.1; XM_006231590.2.
DR   RefSeq; XP_006231653.1; XM_006231591.2.
DR   RefSeq; XP_006231654.1; XM_006231592.1.
DR   RefSeq; XP_008758721.1; XM_008760499.2.
DR   RefSeq; XP_017444784.1; XM_017589295.1.
DR   UniGene; Rn.206114; -.
DR   ProteinModelPortal; Q6AXV9; -.
DR   SMR; Q6AXV9; -.
DR   STRING; 10116.ENSRNOP00000060669; -.
DR   PaxDb; Q6AXV9; -.
DR   PRIDE; Q6AXV9; -.
DR   Ensembl; ENSRNOT00000017186; ENSRNOP00000017186; ENSRNOG00000012801.
DR   Ensembl; ENSRNOT00000064023; ENSRNOP00000060669; ENSRNOG00000049964.
DR   GeneID; 103690044; -.
DR   GeneID; 309465; -.
DR   KEGG; rno:103690044; -.
DR   KEGG; rno:309465; -.
DR   UCSC; RGD:1310764; rat.
DR   CTD; 119391; -.
DR   RGD; 1310764; Gsto2.
DR   eggNOG; KOG0406; Eukaryota.
DR   eggNOG; ENOG410XSIX; LUCA.
DR   GeneTree; ENSGT00940000162030; -.
DR   HOGENOM; HOG000006560; -.
DR   HOVERGEN; HBG051853; -.
DR   InParanoid; Q6AXV9; -.
DR   KO; K00799; -.
DR   OMA; ADHYSHR; -.
DR   OrthoDB; 1225872at2759; -.
DR   PhylomeDB; Q6AXV9; -.
DR   TreeFam; TF105325; -.
DR   Reactome; R-RNO-156590; Glutathione conjugation.
DR   Reactome; R-RNO-196836; Vitamin C (ascorbate) metabolism.
DR   PRO; PR:Q6AXV9; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000012801; Expressed in 9 organ(s), highest expression level in testis.
DR   ExpressionAtlas; Q6AXV9; baseline and differential.
DR   Genevisible; Q6AXV9; RN.
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: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   2: Evidence at transcript level;
KW   Complete proteome; Oxidoreductase; Reference proteome; Transferase.
FT   CHAIN         1    248       Glutathione S-transferase omega-2.
FT                                /FTId=PRO_0000239142.
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:P78417}.
SQ   SEQUENCE   248 AA;  28679 MW;  2DD551FC7CF1EE47 CRC64;
     MSGDLTRCLG KGSCPPGPVP EGVIRIYSMR FCPYSHRTRL VLKAKSIRHE IININLKNKP
     DWYYTKHPFG QVPVLENSQC QLIYESVIAC EYLDDVFPGR KLFPYDPYER ARQKMLLELF
     CKVPQLSKEC LVALRCGRDC TDLKVALRQE LCNLEEILEY QNTTFFGGDS ISMIDYLVWP
     WFERLDVYGL ADCVNHTPML RLWISSMKQD PAVCALHIDK NIFLGFLNLY FQNNPCAFDF
     GLCGPIVR
//
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