ID   GSTO1_PIG               Reviewed;         241 AA.
AC   Q9N1F5;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, 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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-31; 58-83; 101-110;
RP   115-147; 149-160; 162-190; 201-228 AND 235-241, SUBUNIT, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=11485575; DOI=10.1042/0264-6021:3580257;
RA   Rouimi P., Anglade P., Benzekri A., Costet P., Debrauwer L., Pineau T.,
RA   Tulliez J.;
RT   "Purification and characterization of a glutathione S-transferase Omega in
RT   pig: evidence for two distinct organ-specific transcripts.";
RL   Biochem. J. 358:257-262(2001).
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:0000269|PubMed:11485575}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11485575}.
CC   -!- TISSUE SPECIFICITY: Most abundant in the liver and skeletal muscle;
CC       also expressed in heart, diaphragm, colon, thymus, kidney, lung,
CC       ovaries, spleen, intestine and pancreas. {ECO:0000269|PubMed:11485575}.
CC   -!- MASS SPECTROMETRY: Mass=27328; Mass_error=3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11485575};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000305}.
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DR   EMBL; AF188838; AAF71994.2; -; mRNA.
DR   RefSeq; NP_999215.1; NM_214050.2.
DR   AlphaFoldDB; Q9N1F5; -.
DR   SMR; Q9N1F5; -.
DR   STRING; 9823.ENSSSCP00000011305; -.
DR   PaxDb; 9823-ENSSSCP00000011305; -.
DR   PeptideAtlas; Q9N1F5; -.
DR   Ensembl; ENSSSCT00000011607.4; ENSSSCP00000011305.2; ENSSSCG00000022351.3.
DR   Ensembl; ENSSSCT00005012023.1; ENSSSCP00005007045.1; ENSSSCG00005007916.1.
DR   Ensembl; ENSSSCT00015047497.1; ENSSSCP00015018811.1; ENSSSCG00015035687.1.
DR   Ensembl; ENSSSCT00025094544.1; ENSSSCP00025041522.1; ENSSSCG00025068774.1.
DR   Ensembl; ENSSSCT00030014022.1; ENSSSCP00030006281.1; ENSSSCG00030010226.1.
DR   Ensembl; ENSSSCT00035026899.1; ENSSSCP00035010267.1; ENSSSCG00035020670.1.
DR   Ensembl; ENSSSCT00040039734.1; ENSSSCP00040016647.1; ENSSSCG00040029505.1.
DR   Ensembl; ENSSSCT00045030324.1; ENSSSCP00045021014.1; ENSSSCG00045017747.1.
DR   Ensembl; ENSSSCT00050076822.1; ENSSSCP00050033094.1; ENSSSCG00050056308.1.
DR   Ensembl; ENSSSCT00060079326.1; ENSSSCP00060034315.1; ENSSSCG00060058178.1.
DR   Ensembl; ENSSSCT00065017932.1; ENSSSCP00065007312.1; ENSSSCG00065013486.1.
DR   Ensembl; ENSSSCT00070020016.1; ENSSSCP00070016635.1; ENSSSCG00070010275.1.
DR   GeneID; 397117; -.
DR   KEGG; ssc:397117; -.
DR   CTD; 9446; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   GeneTree; ENSGT00940000155351; -.
DR   HOGENOM; CLU_011226_9_2_1; -.
DR   InParanoid; Q9N1F5; -.
DR   OMA; ADHYSHR; -.
DR   OrthoDB; 103277at2759; -.
DR   TreeFam; TF105325; -.
DR   BRENDA; 2.5.1.18; 6170.
DR   Reactome; R-SSC-156581; Methylation.
DR   Reactome; R-SSC-156590; Glutathione conjugation.
DR   Reactome; R-SSC-196836; Vitamin C (ascorbate) metabolism.
DR   Proteomes; UP000008227; Chromosome 14.
DR   Proteomes; UP000314985; Chromosome 14.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   Bgee; ENSSSCG00000022351; Expressed in liver and 43 other cell types or tissues.
DR   ExpressionAtlas; Q9N1F5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; ISS:UniProtKB.
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:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB.
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; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR005442; GST_omega.
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; 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; Q9N1F5; SS.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Oxidoreductase;
KW   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_0000185886"
FT   DOMAIN          22..101
FT                   /note="GST N-terminal"
FT   DOMAIN          106..225
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         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"
FT   CONFLICT        139
FT                   /note="C -> Y (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        158
FT                   /note="T -> Q (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   241 AA;  27419 MW;  AA50EE81C70433A6 CRC64;
     MSGGSARSLG KGSAPPGPVP EGLIRVYSMR FCPFAQRTLL VLNAKGIRHQ VININLKNKP
     EWFFQKNPSG LVPVLENSQG QLIYESAITC EYLDEAYPGK KLLPDDPYEK ACQKMVFELS
     SKVPPLLIRF IRRENEADCS GLKEELRKEF SKLEEVLTKK KTTYFGGSSL SMIDYLIWPW
     FERLEALELN ECIDHTPKLK LWMAAMMKDP AVSALHIEPR DLRAFNDLYL QNSPEACDYG
     L
//