ID GSTO1_RAT Reviewed; 241 AA.
AC Q9Z339;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 24-JAN-2024, entry version 145.
DE RecName: Full=Glutathione S-transferase omega-1;
DE Short=GSTO-1;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P78417};
DE AltName: Full=Glutathione S-transferase omega 1-1;
DE Short=GSTO 1-1;
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE EC=1.8.5.1 {ECO:0000250|UniProtKB:P78417};
DE AltName: Full=Monomethylarsonic acid reductase;
DE Short=MMA(V) reductase;
DE EC=1.20.4.2 {ECO:0000250|UniProtKB:P78417};
DE AltName: Full=S-(Phenacyl)glutathione reductase;
DE Short=SPG-R;
GN Name=Gsto1;
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 [MRNA].
RC TISSUE=Liver;
RX PubMed=9786866; DOI=10.1074/jbc.273.44.28708;
RA Ishikawa T., Casini A.F., Nishikimi M.;
RT "Molecular cloning and functional expression of rat liver glutathione-
RT dependent dehydroascorbate reductase.";
RL J. Biol. Chem. 273:28708-28712(1998).
RN [2]
RP PROTEIN SEQUENCE OF 38-43 AND 123-132, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Diao W., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
CC -!- FUNCTION: Exhibits glutathione-dependent thiol transferase and
CC dehydroascorbate reductase activities. Has S-(phenacyl)glutathione
CC reductase activity. Has also glutathione S-transferase activity.
CC Participates in the biotransformation of inorganic arsenic and reduces
CC monomethylarsonic acid (MMA) and dimethylarsonic acid.
CC {ECO:0000250|UniProtKB:P78417}.
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:P78417};
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:P78417};
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:P78417};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P78417}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34217.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB008807; BAA34217.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q9Z339; -.
DR SMR; Q9Z339; -.
DR IntAct; Q9Z339; 2.
DR STRING; 10116.ENSRNOP00000016851; -.
DR iPTMnet; Q9Z339; -.
DR PhosphoSitePlus; Q9Z339; -.
DR SwissPalm; Q9Z339; -.
DR World-2DPAGE; 0004:Q9Z339; -.
DR jPOST; Q9Z339; -.
DR PaxDb; 10116-ENSRNOP00000016851; -.
DR UCSC; RGD:70952; rat.
DR AGR; RGD:70952; -.
DR RGD; 70952; Gsto1.
DR eggNOG; KOG0406; Eukaryota.
DR InParanoid; Q9Z339; -.
DR PhylomeDB; Q9Z339; -.
DR Reactome; R-RNO-156581; Methylation.
DR Reactome; R-RNO-156590; Glutathione conjugation.
DR Reactome; R-RNO-196836; Vitamin C (ascorbate) metabolism.
DR PRO; PR:Q9Z339; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005604; C:basement membrane; IDA:RGD.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:RGD.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
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:0019853; P:L-ascorbic acid biosynthetic process; IMP:RGD.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0042178; P:xenobiotic catabolic 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; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR005442; GST_omega.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43968; -; 1.
DR PANTHER; PTHR43968:SF5; GLUTATHIONE S-TRANSFERASE OMEGA-1; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR PRINTS; PR01625; GSTRNSFRASEO.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 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.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT CHAIN 2..241
FT /note="Glutathione S-transferase omega-1"
FT /id="PRO_0000185887"
FT DOMAIN 22..101
FT /note="GST N-terminal"
FT DOMAIN 106..228
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:P78417"
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:P78417"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78417"
SQ SEQUENCE 241 AA; 27669 MW; 31EAC5A7CAF22BC6 CRC64;
MSGASARSLG KGSAPPGPVP EGQIRVYSMR FCPFAQRTLM VLKAKGIRHE IININLKNKP
EWFFEKNPFG LVPVLENTQG HLITESVITC EYLDEAYPEK KLFPDDPYEK ACQKMTFELF
SKVPSLVTSF IRAKRKEDHP GIKEELKKEF SKLEEAMANK RTAFFGGNSL SMIDYLIWPW
FQRLEALELN ECIDHTPKLK LWMATMQEDP VASSHFIDAK TYRDYLSLYL QDSPEACDYG
L
//
