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   24-JAN-2024, entry version 134.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Exhibits glutathione-dependent thiol transferase activity.
CC       Has high dehydroascorbate reductase activity and may contribute to the
CC       recycling of ascorbic acid. Participates in the biotransformation of
CC       inorganic arsenic and reduces monomethylarsonic acid (MMA).
CC       {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 disulfide +
CC         L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC         Evidence={ECO:0000250|UniProtKB:Q9H4Y5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H(+) + methylarsonate = glutathione disulfide
CC         + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17826, ChEBI:CHEBI:33409,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.20.4.2;
CC         Evidence={ECO:0000250|UniProtKB:Q9H4Y5};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000305}.
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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   AlphaFoldDB; Q6AXV9; -.
DR   SMR; Q6AXV9; -.
DR   STRING; 10116.ENSRNOP00000017186; -.
DR   PhosphoSitePlus; Q6AXV9; -.
DR   PaxDb; 10116-ENSRNOP00000017186; -.
DR   Ensembl; ENSRNOT00060033012; ENSRNOP00060027006; ENSRNOG00060019077.
DR   GeneID; 309465; -.
DR   KEGG; rno:309465; -.
DR   UCSC; RGD:1310764; rat.
DR   AGR; RGD:1310764; -.
DR   CTD; 119391; -.
DR   RGD; 1310764; Gsto2.
DR   VEuPathDB; HostDB:ENSRNOG00000069697; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_9_2_1; -.
DR   InParanoid; Q6AXV9; -.
DR   OrthoDB; 103277at2759; -.
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 testis and 19 other cell types or tissues.
DR   ExpressionAtlas; Q6AXV9; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; ISS:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR   CDD; cd03184; GST_C_Omega; 1.
DR   CDD; cd03055; GST_N_Omega; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   PANTHER; PTHR43968; -; 1.
DR   PANTHER; PTHR43968:SF4; GLUTATHIONE S-TRANSFERASE OMEGA-2; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   PRINTS; PR01625; GSTRNSFRASEO.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   Genevisible; Q6AXV9; RN.
PE   2: Evidence at transcript level;
KW   Oxidoreductase; Reference proteome; Transferase.
FT   CHAIN           1..248
FT                   /note="Glutathione S-transferase omega-2"
FT                   /id="PRO_0000239142"
FT   DOMAIN          22..101
FT                   /note="GST N-terminal"
FT   DOMAIN          106..231
FT                   /note="GST C-terminal"
FT   ACT_SITE        32
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   BINDING         59
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4Y5"
FT   BINDING         72
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P78417"
FT   BINDING         85..86
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4Y5"
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
//