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Glutathione S-transferase omega-2 (GSTO-2) (EC 2.5.1.18) (Glutathione S-transferase omega 2-2) (GSTO 2-2) (Glutathione-dependent dehydroascorbate reductase) (EC 1.8.5.1) (Monomethylarsonic acid reductase) (MMA(V) reductase) (EC 1.20.4.2)

 GSTO2_HUMAN             Reviewed;         243 AA.
Q9H4Y5; A8K771; B4DJW6; E7ESD6; Q49TW5; Q5GM70; Q5JU15; Q86WP3;
19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
28-FEB-2018, entry version 151.
RecName: Full=Glutathione S-transferase omega-2;
Short=GSTO-2;
EC=2.5.1.18 {ECO:0000269|PubMed:15970797, ECO:0000269|PubMed:22522127};
AltName: Full=Glutathione S-transferase omega 2-2;
Short=GSTO 2-2;
AltName: Full=Glutathione-dependent dehydroascorbate reductase;
EC=1.8.5.1 {ECO:0000269|PubMed:15970797, ECO:0000269|PubMed:22522127};
AltName: Full=Monomethylarsonic acid reductase;
Short=MMA(V) reductase;
EC=1.20.4.2 {ECO:0000269|PubMed:15970797};
Name=GSTO2;
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).
Wang L., Xie Y., Mao Y.;
"Cloning and characterization of human GSTO-2 gene.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Xu J., Xie Y., Mao Y.;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Skeletal muscle, and Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain, and Pancreatic carcinoma;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-243 (ISOFORM 1), VARIANT ASP-142, AND
TISSUE SPECIFICITY.
TISSUE=Testis;
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).
[8]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
PubMed=15970797; DOI=10.1097/01.fpc.0000165725.81559.e3;
Schmuck E.M., Board P.G., Whitbread A.K., Tetlow N., Cavanaugh J.A.,
Blackburn A.C., Masoumi A.;
"Characterization of the monomethylarsonate reductase and
dehydroascorbate reductase activities of Omega class glutathione
transferase variants: implications for arsenic metabolism and the age-
at-onset of Alzheimer's and Parkinson's diseases.";
Pharmacogenet. Genomics 15:493-501(2005).
[9]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-239 ALONE AND IN COMPLEX
WITH GLUTATHIONE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-34.
PubMed=22522127; DOI=10.1016/j.jmb.2012.04.014;
Zhou H., Brock J., Liu D., Board P.G., Oakley A.J.;
"Structural insights into the dehydroascorbate reductase activity of
human omega-class glutathione transferases.";
J. Mol. Biol. 420:190-203(2012).
-!- FUNCTION: Exhibits glutathione-dependent thiol transferase
activity. Has high dehydroascorbate reductase activity and may
contribute to the recycling of ascorbic acid. Participates in the
biotransformation of inorganic arsenic and reduces
monomethylarsonic acid (MMA). {ECO:0000269|PubMed:15970797}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000269|PubMed:15970797, ECO:0000269|PubMed:22522127}.
-!- CATALYTIC ACTIVITY: 2 glutathione + dehydroascorbate = glutathione
disulfide + ascorbate. {ECO:0000269|PubMed:15970797,
ECO:0000269|PubMed:22522127}.
-!- CATALYTIC ACTIVITY: Methylarsonate + 2 glutathione =
methylarsonite + glutathione disulfide + H(2)O.
{ECO:0000269|PubMed:15970797}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.5. {ECO:0000269|PubMed:15970797};
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-10194609, EBI-10194609;
Q9H6H2:MUM1; NbExp=3; IntAct=EBI-10194609, EBI-10307610;
P05549:TFAP2A; NbExp=3; IntAct=EBI-10194609, EBI-347351;
P05549-5:TFAP2A; NbExp=5; IntAct=EBI-10194609, EBI-12194905;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9H4Y5-1; Sequence=Displayed;
Name=2;
IsoId=Q9H4Y5-2; Sequence=VSP_042567;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9H4Y5-3; Sequence=VSP_045267;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in a range of tissues, including the
liver, kidney, skeletal muscle and prostate. Strongest expression
in the testis. {ECO:0000269|PubMed:12618591}.
-!- SIMILARITY: Belongs to the GST superfamily. Omega family.
{ECO:0000305}.
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EMBL; AY350731; AAR02452.1; -; mRNA.
EMBL; AY209189; AAP47743.1; -; mRNA.
EMBL; AK291886; BAF84575.1; -; mRNA.
EMBL; AK296266; BAG58978.1; -; mRNA.
EMBL; AL139341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL162742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49600.1; -; Genomic_DNA.
EMBL; BC046194; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC056918; AAH56918.1; -; mRNA.
EMBL; AY191318; AAO23573.1; -; mRNA.
CCDS; CCDS53574.1; -. [Q9H4Y5-2]
CCDS; CCDS53575.1; -. [Q9H4Y5-3]
CCDS; CCDS7556.1; -. [Q9H4Y5-1]
RefSeq; NP_001177942.1; NM_001191013.1. [Q9H4Y5-2]
RefSeq; NP_001177943.1; NM_001191014.1. [Q9H4Y5-3]
RefSeq; NP_001177944.1; NM_001191015.1.
RefSeq; NP_899062.1; NM_183239.1. [Q9H4Y5-1]
RefSeq; XP_011537572.1; XM_011539270.2. [Q9H4Y5-1]
UniGene; Hs.107384; -.
UniGene; Hs.203634; -.
PDB; 3Q18; X-ray; 1.70 A; A/B=1-239.
PDB; 3Q19; X-ray; 1.90 A; A/B=1-239.
PDB; 3QAG; X-ray; 2.00 A; A=1-239.
PDBsum; 3Q18; -.
PDBsum; 3Q19; -.
PDBsum; 3QAG; -.
ProteinModelPortal; Q9H4Y5; -.
SMR; Q9H4Y5; -.
BioGrid; 125638; 16.
IntAct; Q9H4Y5; 10.
STRING; 9606.ENSP00000345023; -.
ChEMBL; CHEMBL2161; -.
DrugBank; DB00143; Glutathione.
iPTMnet; Q9H4Y5; -.
PhosphoSitePlus; Q9H4Y5; -.
BioMuta; GSTO2; -.
DMDM; 34922124; -.
PaxDb; Q9H4Y5; -.
PeptideAtlas; Q9H4Y5; -.
PRIDE; Q9H4Y5; -.
DNASU; 119391; -.
Ensembl; ENST00000338595; ENSP00000345023; ENSG00000065621. [Q9H4Y5-1]
Ensembl; ENST00000369707; ENSP00000358721; ENSG00000065621. [Q9H4Y5-3]
Ensembl; ENST00000450629; ENSP00000390986; ENSG00000065621. [Q9H4Y5-2]
GeneID; 119391; -.
KEGG; hsa:119391; -.
UCSC; uc001kyb.4; human. [Q9H4Y5-1]
CTD; 119391; -.
DisGeNET; 119391; -.
EuPathDB; HostDB:ENSG00000065621.14; -.
GeneCards; GSTO2; -.
HGNC; HGNC:23064; GSTO2.
HPA; HPA048141; -.
MIM; 612314; gene.
neXtProt; NX_Q9H4Y5; -.
OpenTargets; ENSG00000065621; -.
PharmGKB; PA133787053; -.
eggNOG; KOG0406; Eukaryota.
eggNOG; ENOG410XSIX; LUCA.
GeneTree; ENSGT00390000005479; -.
HOGENOM; HOG000006560; -.
HOVERGEN; HBG051853; -.
InParanoid; Q9H4Y5; -.
KO; K00799; -.
OMA; DCVSHTP; -.
OrthoDB; EOG091G0IEA; -.
PhylomeDB; Q9H4Y5; -.
TreeFam; TF105325; -.
BRENDA; 1.8.5.1; 2681.
BRENDA; 2.5.1.18; 2681.
Reactome; R-HSA-156590; Glutathione conjugation.
Reactome; R-HSA-196836; Vitamin C (ascorbate) metabolism.
ChiTaRS; GSTO2; human.
GeneWiki; GSTO2; -.
GenomeRNAi; 119391; -.
PRO; PR:Q9H4Y5; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000065621; -.
CleanEx; HS_GSTO2; -.
Genevisible; Q9H4Y5; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:UniProtKB.
GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC.
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:0019852; P:L-ascorbic acid metabolic process; IDA:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0009407; P:toxin catabolic process; IBA:GO_Central.
GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR005442; GST_omega.
InterPro; IPR036249; Thioredoxin-like_sf.
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; Alternative splicing; Complete proteome; Oxidoreductase;
Polymorphism; Reference proteome; Transferase.
CHAIN 1 243 Glutathione S-transferase omega-2.
/FTId=PRO_0000185888.
DOMAIN 22 101 GST N-terminal.
DOMAIN 106 231 GST C-terminal.
REGION 85 86 Glutathione binding.
{ECO:0000269|PubMed:22522127}.
ACT_SITE 32 32 Nucleophile.
BINDING 59 59 Glutathione.
{ECO:0000269|PubMed:22522127}.
BINDING 72 72 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:22522127}.
VAR_SEQ 1 28 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045267.
VAR_SEQ 123 156 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042567.
VARIANT 130 130 C -> Y (in dbSNP:rs45582439).
/FTId=VAR_049492.
VARIANT 142 142 N -> D (in dbSNP:rs156697).
{ECO:0000269|PubMed:12618591}.
/FTId=VAR_016812.
MUTAGEN 34 34 Y->A: Abolishes DHAR activity.
{ECO:0000269|PubMed:22522127}.
CONFLICT 215 215 A -> V (in Ref. 2; AAP47743).
{ECO:0000305}.
STRAND 24 28 {ECO:0000244|PDB:3Q18}.
HELIX 33 44 {ECO:0000244|PDB:3Q18}.
STRAND 49 54 {ECO:0000244|PDB:3Q18}.
STRAND 56 58 {ECO:0000244|PDB:3Q18}.
HELIX 61 65 {ECO:0000244|PDB:3Q18}.
STRAND 74 76 {ECO:0000244|PDB:3Q18}.
STRAND 82 85 {ECO:0000244|PDB:3QAG}.
HELIX 86 96 {ECO:0000244|PDB:3Q18}.
HELIX 107 119 {ECO:0000244|PDB:3Q18}.
TURN 120 122 {ECO:0000244|PDB:3Q18}.
HELIX 123 136 {ECO:0000244|PDB:3Q18}.
HELIX 141 161 {ECO:0000244|PDB:3Q18}.
STRAND 168 170 {ECO:0000244|PDB:3Q18}.
HELIX 173 183 {ECO:0000244|PDB:3Q18}.
HELIX 185 188 {ECO:0000244|PDB:3Q18}.
HELIX 191 194 {ECO:0000244|PDB:3Q18}.
HELIX 198 208 {ECO:0000244|PDB:3Q18}.
HELIX 211 216 {ECO:0000244|PDB:3Q18}.
HELIX 220 231 {ECO:0000244|PDB:3Q18}.
HELIX 235 238 {ECO:0000244|PDB:3Q18}.
SEQUENCE 243 AA; 28254 MW; 45A959432BCF490A CRC64;
MSGDATRTLG KGSQPPGPVP EGLIRIYSMR FCPYSHRTRL VLKAKDIRHE VVNINLRNKP
EWYYTKHPFG HIPVLETSQC QLIYESVIAC EYLDDAYPGR KLFPYDPYER ARQKMLLELF
CKVPHLTKEC LVALRCGREC TNLKAALRQE FSNLEEILEY QNTTFFGGTC ISMIDYLLWP
WFERLDVYGI LDCVSHTPAL RLWISAMKWD PTVCALLMDK SIFQGFLNLY FQNNPNAFDF
GLC


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Tel 01 43 25 01 50

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GENTAUR GmbH
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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