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 03-AUG-2022, entry version 129.
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 PaxDb; Q6AXV9; -.
DR PRIDE; Q6AXV9; -.
DR GeneID; 309465; -.
DR KEGG; rno:309465; -.
DR UCSC; RGD:1310764; rat.
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 OMA; ESMVICE; -.
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 testis and 19 other tissues.
DR ExpressionAtlas; Q6AXV9; baseline.
DR Genevisible; Q6AXV9; RN.
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 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 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
