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Glutathione S-transferase omega-1 (GSTO-1) (EC 2.5.1.18) (Glutathione S-transferase omega 1-1) (GSTO 1-1) (Glutathione-dependent dehydroascorbate reductase) (EC 1.8.5.1) (Monomethylarsonic acid reductase) (MMA(V) reductase) (EC 1.20.4.2) (S-(Phenacyl)glutathione reductase) (SPG-R)

 GSTO1_PIG               Reviewed;         241 AA.
Q9N1F5;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
31-JAN-2002, sequence version 2.
23-MAY-2018, entry version 119.
RecName: Full=Glutathione S-transferase omega-1;
Short=GSTO-1;
EC=2.5.1.18 {ECO:0000250|UniProtKB:P78417};
AltName: Full=Glutathione S-transferase omega 1-1;
Short=GSTO 1-1;
AltName: Full=Glutathione-dependent dehydroascorbate reductase;
EC=1.8.5.1 {ECO:0000250|UniProtKB:P78417};
AltName: Full=Monomethylarsonic acid reductase;
Short=MMA(V) reductase;
EC=1.20.4.2 {ECO:0000250|UniProtKB:P78417};
AltName: Full=S-(Phenacyl)glutathione reductase;
Short=SPG-R;
Name=GSTO1;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-31; 58-83; 101-110;
115-147; 149-160; 162-190; 201-228 AND 235-241, SUBUNIT, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
TISSUE=Liver;
PubMed=11485575; DOI=10.1042/0264-6021:3580257;
Rouimi P., Anglade P., Benzekri A., Costet P., Debrauwer L.,
Pineau T., Tulliez J.;
"Purification and characterization of a glutathione S-transferase
Omega in pig: evidence for two distinct organ-specific transcripts.";
Biochem. J. 358:257-262(2001).
-!- FUNCTION: Exhibits glutathione-dependent thiol transferase and
dehydroascorbate reductase activities. Has S-(phenacyl)glutathione
reductase activity. Has also glutathione S-transferase activity.
Participates in the biotransformation of inorganic arsenic and
reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.
{ECO:0000250|UniProtKB:P78417}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000250|UniProtKB:P78417}.
-!- CATALYTIC ACTIVITY: 2 glutathione + dehydroascorbate = glutathione
disulfide + ascorbate. {ECO:0000250|UniProtKB:P78417}.
-!- CATALYTIC ACTIVITY: Methylarsonate + 2 glutathione =
methylarsonite + glutathione disulfide + H(2)O.
{ECO:0000250|UniProtKB:P78417}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11485575}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:11485575}.
-!- TISSUE SPECIFICITY: Most abundant in the liver and skeletal
muscle; also expressed in heart, diaphragm, colon, thymus, kidney,
lung, ovaries, spleen, intestine and pancreas.
{ECO:0000269|PubMed:11485575}.
-!- MASS SPECTROMETRY: Mass=27328; Mass_error=3; Method=Electrospray;
Range=2-241; Evidence={ECO:0000269|PubMed:11485575};
-!- SIMILARITY: Belongs to the GST superfamily. Omega family.
{ECO:0000305}.
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EMBL; AF188838; AAF71994.2; -; mRNA.
RefSeq; NP_999215.1; NM_214050.2.
UniGene; Ssc.58505; -.
ProteinModelPortal; Q9N1F5; -.
SMR; Q9N1F5; -.
STRING; 9823.ENSSSCP00000011305; -.
PaxDb; Q9N1F5; -.
PeptideAtlas; Q9N1F5; -.
PRIDE; Q9N1F5; -.
Ensembl; ENSSSCT00000011607; ENSSSCP00000011305; ENSSSCG00000022351.
GeneID; 397117; -.
KEGG; ssc:397117; -.
CTD; 9446; -.
eggNOG; KOG0406; Eukaryota.
eggNOG; ENOG410XSIX; LUCA.
GeneTree; ENSGT00390000005479; -.
HOGENOM; HOG000006560; -.
HOVERGEN; HBG051853; -.
InParanoid; Q9N1F5; -.
KO; K00799; -.
OMA; ADHYSHR; -.
OrthoDB; EOG091G0IEA; -.
TreeFam; TF105325; -.
BRENDA; 2.5.1.18; 6170.
Reactome; R-SSC-156581; Methylation.
Reactome; R-SSC-156590; Glutathione conjugation.
Reactome; R-SSC-196836; Vitamin C (ascorbate) metabolism.
Proteomes; UP000008227; Chromosome 14.
Bgee; ENSSSCG00000022351; -.
Genevisible; Q9N1F5; SS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; ISS:UniProtKB.
GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC.
GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
GO; GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB.
GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
GO; GO:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB.
GO; GO:0009407; P:toxin catabolic process; IBA:GO_Central.
GO; GO:0042178; P:xenobiotic catabolic process; ISS:UniProtKB.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR005442; GST_omega.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF14497; GST_C_3; 1.
Pfam; PF13417; GST_N_3; 1.
PRINTS; PR01625; GSTRNSFRASEO.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
Oxidoreductase; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P78417}.
CHAIN 2 241 Glutathione S-transferase omega-1.
/FTId=PRO_0000185886.
DOMAIN 22 101 GST N-terminal.
DOMAIN 106 225 GST C-terminal.
REGION 85 86 Glutathione binding.
{ECO:0000250|UniProtKB:P78417}.
ACT_SITE 32 32 Nucleophile.
{ECO:0000250|UniProtKB:P78417}.
BINDING 59 59 Glutathione.
{ECO:0000250|UniProtKB:P78417}.
BINDING 72 72 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P78417}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P78417}.
MOD_RES 57 57 N6-acetyllysine.
{ECO:0000250|UniProtKB:P78417}.
MOD_RES 143 143 N6-acetyllysine.
{ECO:0000250|UniProtKB:P78417}.
MOD_RES 148 148 N6-acetyllysine.
{ECO:0000250|UniProtKB:P78417}.
MOD_RES 152 152 N6-acetyllysine.
{ECO:0000250|UniProtKB:P78417}.
CONFLICT 139 139 C -> Y (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 158 158 T -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
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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