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Database: UniProt/SWISS-PROT
Entry: GSTO1_PIG
LinkDB: GSTO1_PIG
Original site: GSTO1_PIG 
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   16-JAN-2019, entry version 123.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   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.,
RA   Pineau T., Tulliez J.;
RT   "Purification and characterization of a glutathione S-transferase
RT   Omega in 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
CC       reduces 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
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:P78417};
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:P78417};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11485575}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:11485575}.
CC   -!- TISSUE SPECIFICITY: Most abundant in the liver and skeletal
CC       muscle; also expressed in heart, diaphragm, colon, thymus, kidney,
CC       lung, ovaries, spleen, intestine and pancreas.
CC       {ECO:0000269|PubMed:11485575}.
CC   -!- MASS SPECTROMETRY: Mass=27328; Mass_error=3; Method=Electrospray;
CC       Range=2-241; Evidence={ECO:0000269|PubMed:11485575};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000305}.
DR   EMBL; AF188838; AAF71994.2; -; mRNA.
DR   RefSeq; NP_999215.1; NM_214050.2.
DR   UniGene; Ssc.58505; -.
DR   ProteinModelPortal; Q9N1F5; -.
DR   SMR; Q9N1F5; -.
DR   STRING; 9823.ENSSSCP00000011305; -.
DR   PaxDb; Q9N1F5; -.
DR   PeptideAtlas; Q9N1F5; -.
DR   PRIDE; Q9N1F5; -.
DR   Ensembl; ENSSSCT00000011607; ENSSSCP00000011305; ENSSSCG00000022351.
DR   GeneID; 397117; -.
DR   KEGG; ssc:397117; -.
DR   CTD; 9446; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   eggNOG; ENOG410XSIX; LUCA.
DR   GeneTree; ENSGT00940000155351; -.
DR   HOGENOM; HOG000006560; -.
DR   HOVERGEN; HBG051853; -.
DR   InParanoid; Q9N1F5; -.
DR   KO; K00799; -.
DR   OMA; EHPLKLY; -.
DR   OrthoDB; 1225872at2759; -.
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   Bgee; ENSSSCG00000022351; Expressed in 5 organ(s), highest expression level in liver.
DR   Genevisible; Q9N1F5; SS.
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:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central.
DR   GO; GO:0042178; P:xenobiotic catabolic 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; IPR004046; GST_C.
DR   InterPro; IPR005442; GST_omega.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF14497; GST_C_3; 1.
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   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Oxidoreductase; Reference proteome; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P78417}.
FT   CHAIN         2    241       Glutathione S-transferase omega-1.
FT                                /FTId=PRO_0000185886.
FT   DOMAIN       22    101       GST N-terminal.
FT   DOMAIN      106    225       GST C-terminal.
FT   REGION       85     86       Glutathione binding.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   ACT_SITE     32     32       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   BINDING      59     59       Glutathione.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   BINDING      72     72       Glutathione; via amide nitrogen and
FT                                carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   MOD_RES      57     57       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   MOD_RES     143    143       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   MOD_RES     148    148       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   MOD_RES     152    152       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P78417}.
FT   CONFLICT    139    139       C -> Y (in Ref. 1; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    158    158       T -> Q (in Ref. 1; AA sequence).
FT                                {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
//
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