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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_HUMAN             Reviewed;         241 AA.
P78417; D3DRA3; F5H7H0; Q5TA03; Q7Z3T2;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 2.
27-SEP-2017, entry version 185.
RecName: Full=Glutathione S-transferase omega-1;
Short=GSTO-1;
EC=2.5.1.18 {ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:11511179, ECO:0000269|PubMed:17226937, ECO:0000269|PubMed:18028863, ECO:0000269|PubMed:21106529};
AltName: Full=Glutathione S-transferase omega 1-1;
Short=GSTO 1-1;
AltName: Full=Glutathione-dependent dehydroascorbate reductase;
EC=1.8.5.1 {ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:11511179};
AltName: Full=Monomethylarsonic acid reductase;
Short=MMA(V) reductase;
EC=1.20.4.2 {ECO:0000269|PubMed:11511179};
AltName: Full=S-(Phenacyl)glutathione reductase;
Short=SPG-R;
Name=GSTO1; Synonyms=GSTTLP28;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
Kodym R., Story M.D.;
"Cloning of the human homolog to a mouse protein, differentially
expressed in lymphoma cells with different susceptibility to radiation
induced apoptosis.";
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (2.0
ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY,
ACTIVE SITE, SUBUNIT, AND TISSUE SPECIFICITY.
TISSUE=Fetus;
PubMed=10783391; DOI=10.1074/jbc.M001706200;
Board P.G., Coggan M., Chelvanayagam G., Easteal S., Jermiin L.S.,
Schulte G.K., Danley D.E., Hoth L.R., Griffor M.C., Kamath A.V.,
Rosner M.H., Chrunyk B.A., Perregaux D.E., Gabel C.A., Geoghegan K.F.,
Pandit J.;
"Identification, characterization, and crystal structure of the Omega
class glutathione transferases.";
J. Biol. Chem. 275:24798-24806(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-140; GLU-155 DEL;
LYS-208 AND VAL-236.
PubMed=12928150; DOI=10.1289/ehp.6420;
Yu L., Kalla K., Guthrie E., Vidrine A., Klimecki W.T.;
"Genetic variation in genes associated with arsenic metabolism:
glutathione S-transferase omega 1-1 and purine nucleoside
phosphorylase polymorphisms in European and indigenous Americans.";
Environ. Health Perspect. 111:1421-1427(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 12-21; 58-65; 133-139 AND 149-156, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Liver;
PubMed=11271497;
DOI=10.1002/1522-2683(200011)21:17<3785::AID-ELPS3785>3.0.CO;2-2;
Hubbard M.J., McHugh N.J.;
"Human ERp29: isolation, primary structural characterisation and two-
dimensional gel mapping.";
Electrophoresis 21:3785-3796(2000).
[9]
PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Liver;
PubMed=11511179; DOI=10.1021/tx010052h;
Zakharyan R.A., Sampayo-Reyes A., Healy S.M., Tsaprailis G.,
Board P.G., Liebler D.C., Aposhian H.V.;
"Human monomethylarsonic acid (MMA(V)) reductase is a member of the
glutathione-S-transferase superfamily.";
Chem. Res. Toxicol. 14:1051-1057(2001).
[10]
FUNCTION, MUTAGENESIS OF CYS-32, BIOPHYSICOCHEMICAL PROPERTIES, AND
CATALYTIC ACTIVITY.
PubMed=17226937; DOI=10.1021/tx600305y;
Board P.G., Anders M.W.;
"Glutathione transferase omega 1 catalyzes the reduction of S-
(phenacyl)glutathiones to acetophenones.";
Chem. Res. Toxicol. 20:149-154(2007).
[11]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18028863; DOI=10.1016/j.ab.2007.09.029;
Board P.G., Coggan M., Cappello J., Zhou H., Oakley A.J., Anders M.W.;
"S-(4-Nitrophenacyl)glutathione is a specific substrate for
glutathione transferase omega 1-1.";
Anal. Biochem. 374:25-30(2008).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-143; LYS-148 AND
LYS-152, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF VARIANT GLU-155 DEL IN
COMPLEX WITH GLUTATHIONE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
CHARACTERIZATION OF VARIANTS ASP-140 AND GLU-155 DEL.
PubMed=21106529; DOI=10.1074/jbc.M110.197822;
Zhou H., Brock J., Casarotto M.G., Oakley A.J., Board P.G.;
"Novel folding and stability defects cause a deficiency of human
glutathione transferase omega 1.";
J. Biol. Chem. 286:4271-4279(2011).
[18]
VARIANTS ASP-140 AND GLU-155 DEL.
PubMed=12618591; DOI=10.1097/00008571-200303000-00003;
Whitbread A.K., Tetlow N., Eyre H.J., Sutherland G.R., Board P.G.;
"Characterization of the human Omega class glutathione transferase
genes and associated polymorphisms.";
Pharmacogenetics 13:131-144(2003).
-!- 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:0000269|PubMed:10783391, ECO:0000269|PubMed:11511179,
ECO:0000269|PubMed:17226937, ECO:0000269|PubMed:18028863,
ECO:0000269|PubMed:21106529}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000269|PubMed:10783391, ECO:0000269|PubMed:11511179,
ECO:0000269|PubMed:17226937, ECO:0000269|PubMed:18028863,
ECO:0000269|PubMed:21106529}.
-!- CATALYTIC ACTIVITY: 2 glutathione + dehydroascorbate = glutathione
disulfide + ascorbate. {ECO:0000269|PubMed:10783391,
ECO:0000269|PubMed:11511179}.
-!- CATALYTIC ACTIVITY: Methylarsonate + 2 glutathione =
methylarsonite + glutathione disulfide + H(2)O.
{ECO:0000269|PubMed:11511179}.
-!- ENZYME REGULATION: Monomethylarsonic acid reductase activity is
competitively inhibited by 1-chloro 2,4-dinitrobenzene (CDNB) and
by deoxycholate.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8. {ECO:0000269|PubMed:11511179,
ECO:0000269|PubMed:17226937};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10783391,
ECO:0000269|PubMed:21106529}.
-!- INTERACTION:
P04792:HSPB1; NbExp=2; IntAct=EBI-712083, EBI-352682;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:11511179}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P78417-1; Sequence=Displayed;
Name=2;
IsoId=P78417-2; Sequence=VSP_045820;
Name=3;
IsoId=P78417-3; Sequence=VSP_045819;
-!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in liver,
pancreas, skeletal muscle, spleen, thymus, colon, blood leukocyte
and heart. Lowest expression in brain, placenta and lung.
{ECO:0000269|PubMed:10783391}.
-!- SIMILARITY: Belongs to the GST superfamily. Omega family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAD97673.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U90313; AAB70109.1; -; mRNA.
EMBL; AF212303; AAF73376.1; -; mRNA.
EMBL; AY817669; AAV68046.1; -; Genomic_DNA.
EMBL; BX537431; CAD97673.1; ALT_INIT; mRNA.
EMBL; AL139341; CAI17224.1; -; Genomic_DNA.
EMBL; CH471066; EAW49601.1; -; Genomic_DNA.
EMBL; CH471066; EAW49602.1; -; Genomic_DNA.
EMBL; CH471066; EAW49603.1; -; Genomic_DNA.
EMBL; BC000127; AAH00127.1; -; mRNA.
CCDS; CCDS53572.1; -. [P78417-2]
CCDS; CCDS53573.1; -. [P78417-3]
CCDS; CCDS7555.1; -. [P78417-1]
RefSeq; NP_001177931.1; NM_001191002.1. [P78417-2]
RefSeq; NP_001177932.1; NM_001191003.1. [P78417-3]
RefSeq; NP_004823.1; NM_004832.2. [P78417-1]
UniGene; Hs.190028; -.
PDB; 1EEM; X-ray; 2.00 A; A=1-241.
PDB; 3LFL; X-ray; 2.10 A; A/B/C=1-241.
PDB; 3VLN; X-ray; 1.70 A; A=1-241.
PDB; 4IS0; X-ray; 1.72 A; A=1-241.
PDB; 4YQM; X-ray; 2.38 A; A/B/C=1-241.
PDB; 4YQU; X-ray; 1.94 A; A/B=1-241.
PDB; 4YQV; X-ray; 2.06 A; A/B/C=1-241.
PDBsum; 1EEM; -.
PDBsum; 3LFL; -.
PDBsum; 3VLN; -.
PDBsum; 4IS0; -.
PDBsum; 4YQM; -.
PDBsum; 4YQU; -.
PDBsum; 4YQV; -.
ProteinModelPortal; P78417; -.
SMR; P78417; -.
BioGrid; 114836; 37.
IntAct; P78417; 9.
MINT; MINT-1384709; -.
STRING; 9606.ENSP00000358727; -.
BindingDB; P78417; -.
ChEMBL; CHEMBL3174; -.
DrugBank; DB00143; Glutathione.
DrugBank; DB00163; Vitamin E.
iPTMnet; P78417; -.
PhosphoSitePlus; P78417; -.
SwissPalm; P78417; -.
BioMuta; GSTO1; -.
DMDM; 6016173; -.
OGP; P78417; -.
UCD-2DPAGE; P78417; -.
EPD; P78417; -.
PaxDb; P78417; -.
PeptideAtlas; P78417; -.
PRIDE; P78417; -.
TopDownProteomics; P78417-1; -. [P78417-1]
Ensembl; ENST00000369710; ENSP00000358724; ENSG00000148834. [P78417-2]
Ensembl; ENST00000369713; ENSP00000358727; ENSG00000148834. [P78417-1]
Ensembl; ENST00000539281; ENSP00000441488; ENSG00000148834. [P78417-3]
GeneID; 9446; -.
KEGG; hsa:9446; -.
UCSC; uc021pxr.2; human. [P78417-1]
CTD; 9446; -.
DisGeNET; 9446; -.
EuPathDB; HostDB:ENSG00000148834.12; -.
GeneCards; GSTO1; -.
HGNC; HGNC:13312; GSTO1.
HPA; HPA037603; -.
HPA; HPA037604; -.
MIM; 605482; gene.
neXtProt; NX_P78417; -.
OpenTargets; ENSG00000148834; -.
PharmGKB; PA133787054; -.
eggNOG; KOG0406; Eukaryota.
eggNOG; ENOG410XSIX; LUCA.
GeneTree; ENSGT00390000005479; -.
HOGENOM; HOG000006560; -.
HOVERGEN; HBG051853; -.
InParanoid; P78417; -.
KO; K00799; -.
OMA; ADHYSHR; -.
OrthoDB; EOG091G0IEA; -.
PhylomeDB; P78417; -.
TreeFam; TF105325; -.
BioCyc; MetaCyc:HS07564-MONOMER; -.
BRENDA; 1.20.4.2; 2681.
BRENDA; 1.8.5.1; 2681.
BRENDA; 2.5.1.18; 2681.
Reactome; R-HSA-156581; Methylation.
Reactome; R-HSA-156590; Glutathione conjugation.
Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
ChiTaRS; GSTO1; human.
EvolutionaryTrace; P78417; -.
GeneWiki; GSTO1; -.
GenomeRNAi; 9446; -.
PRO; PR:P78417; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000148834; -.
CleanEx; HS_GSTO1; -.
ExpressionAtlas; P78417; baseline and differential.
Genevisible; P78417; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:UniProtKB.
GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
GO; GO:0050610; F:methylarsonate reductase activity; TAS:Reactome.
GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
GO; GO:0071243; P:cellular response to arsenic-containing substance; IDA:UniProtKB.
GO; GO:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0019852; P:L-ascorbic acid metabolic process; IDA:UniProtKB.
GO; GO:0032259; P:methylation; TAS:Reactome.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0014810; P:positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; IC:BHF-UCL.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IC:BHF-UCL.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0009407; P:toxin catabolic process; IBA:GO_Central.
GO; GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR005442; GST_omega.
InterPro; IPR012336; Thioredoxin-like_fold.
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;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Oxidoreductase; Phosphoprotein;
Polymorphism; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 241 Glutathione S-transferase omega-1.
/FTId=PRO_0000185884.
DOMAIN 22 101 GST N-terminal.
DOMAIN 106 230 GST C-terminal.
REGION 85 86 Glutathione binding.
{ECO:0000269|PubMed:10783391,
ECO:0000269|PubMed:21106529}.
ACT_SITE 32 32 Nucleophile.
{ECO:0000269|PubMed:10783391}.
BINDING 59 59 Glutathione.
{ECO:0000269|PubMed:10783391,
ECO:0000269|PubMed:21106529}.
BINDING 72 72 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:10783391,
ECO:0000269|PubMed:21106529}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 57 57 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 143 143 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 148 148 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 152 152 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 28 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_045819.
VAR_SEQ 123 155 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_045820.
VARIANT 32 32 C -> Y (in dbSNP:rs45529437).
/FTId=VAR_061231.
VARIANT 86 86 S -> C (in dbSNP:rs11509436).
/FTId=VAR_029269.
VARIANT 140 140 A -> D (in allele GSTO1*C; no effect on
protein stability; dbSNP:rs4925).
{ECO:0000269|PubMed:12618591,
ECO:0000269|PubMed:12928150,
ECO:0000269|PubMed:21106529}.
/FTId=VAR_016811.
VARIANT 155 155 Missing (in allele GSTO1*B; decreased
protein stability).
{ECO:0000269|PubMed:12618591,
ECO:0000269|PubMed:12928150,
ECO:0000269|PubMed:21106529}.
/FTId=VAR_016813.
VARIANT 208 208 E -> K (in dbSNP:rs11509438).
{ECO:0000269|PubMed:12928150}.
/FTId=VAR_024484.
VARIANT 236 236 A -> V (in dbSNP:rs11509439).
{ECO:0000269|PubMed:12928150}.
/FTId=VAR_026583.
MUTAGEN 32 32 C->A: Loss of activity.
{ECO:0000269|PubMed:17226937}.
HELIX 4 6 {ECO:0000244|PDB:3VLN}.
STRAND 24 28 {ECO:0000244|PDB:3VLN}.
HELIX 33 45 {ECO:0000244|PDB:3VLN}.
STRAND 49 54 {ECO:0000244|PDB:3VLN}.
STRAND 56 58 {ECO:0000244|PDB:3LFL}.
HELIX 63 66 {ECO:0000244|PDB:3VLN}.
STRAND 74 76 {ECO:0000244|PDB:3VLN}.
STRAND 82 85 {ECO:0000244|PDB:3VLN}.
HELIX 86 96 {ECO:0000244|PDB:3VLN}.
HELIX 107 120 {ECO:0000244|PDB:3VLN}.
HELIX 123 131 {ECO:0000244|PDB:3VLN}.
HELIX 136 160 {ECO:0000244|PDB:3VLN}.
STRAND 162 164 {ECO:0000244|PDB:4IS0}.
STRAND 167 169 {ECO:0000244|PDB:3VLN}.
HELIX 172 184 {ECO:0000244|PDB:3VLN}.
TURN 185 188 {ECO:0000244|PDB:3VLN}.
HELIX 190 192 {ECO:0000244|PDB:3VLN}.
STRAND 193 195 {ECO:0000244|PDB:1EEM}.
HELIX 197 207 {ECO:0000244|PDB:3VLN}.
HELIX 210 215 {ECO:0000244|PDB:3VLN}.
HELIX 219 229 {ECO:0000244|PDB:3VLN}.
TURN 230 232 {ECO:0000244|PDB:3VLN}.
HELIX 236 238 {ECO:0000244|PDB:3VLN}.
SEQUENCE 241 AA; 27566 MW; 9134ABA265F5C87E CRC64;
MSGESARSLG KGSAPPGPVP EGSIRIYSMR FCPFAERTRL VLKAKGIRHE VININLKNKP
EWFFKKNPFG LVPVLENSQG QLIYESAITC EYLDEAYPGK KLLPDDPYEK ACQKMILELF
SKVPSLVGSF IRSQNKEDYA GLKEEFRKEF TKLEEVLTNK KTTFFGGNSI SMIDYLIWPW
FERLEAMKLN ECVDHTPKLK LWMAAMKEDP TVSALLTSEK DWQGFLELYL QNSPEACDYG
L


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