Q9H4Y5 (GSTO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase omega-2
Short name=GSTO-2
EC=2.5.1.18

Alternative name(s):
Glutathione S-transferase omega 2-2
Short name=GSTO 2-2
Glutathione-dependent dehydroascorbate reductase
EC=1.8.5.1
Monomethylarsonic acid reductase
Short name=MMA(V) reductase
EC=1.20.4.2

Gene names

Name:

GSTO2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	243 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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). Ref.8
Catalytic activity	RX + glutathione = HX + R-S-glutathione. Ref.8 Ref.9 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate. Ref.8 Ref.9 Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O. Ref.8 Ref.9
Tissue specificity	Expressed in a range of tissues, including the liver, kidney, skeletal muscle and prostate. Strongest expression in the testis. Ref.7
Sequence similarities	Belongs to the GST superfamily. Omega family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.
Biophysicochemical properties	pH dependence: Optimum pH is 7.5. Ref.8

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Oxidoreductase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-ascorbic acid metabolic process Inferred from direct assay Ref.8. Source: UniProtKB cellular response to arsenic-containing substance Inferred from direct assay Ref.8. Source: UniProtKB xenobiotic metabolic process Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	glutathione dehydrogenase (ascorbate) activity Inferred from direct assay Ref.8. Source: UniProtKB glutathione transferase activity Inferred from electronic annotation. Source: EC methylarsonate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H4Y5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9H4Y5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     123-156: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9H4Y5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 243

243

Glutathione S-transferase omega-2

PRO_0000185888

Regions

Domain

22 – 101

80

GST N-terminal

Domain

106 – 231

126

GST C-terminal

Region

85 – 86

2

Glutathione binding

Sites

Active site

32

1

Nucleophile

Binding site

59

1

Glutathione

Binding site

72

1

Glutathione; via amide nitrogen and carbonyl oxygen

Natural variations

Alternative sequence

1 – 28

28

Missing in isoform 3.

VSP_045267

Alternative sequence

123 – 156

34

Missing in isoform 2.

VSP_042567

Natural variant

130

1

C → Y.
Corresponds to variant rs45582439 [ dbSNP | Ensembl ].

VAR_049492

Natural variant

142

1

N → D. Ref.7
Corresponds to variant rs156697 [ dbSNP | Ensembl ].

VAR_016812

Experimental info

Mutagenesis

34

1

Y → A: Abolishes DHAR activity. Ref.9

Sequence conflict

215

1

A → V in AAP47743. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

243

Helix Strand Turn

Details...

Beta strand

24 – 28

5

Helix

33 – 44

12

Beta strand

49 – 54

6

Beta strand

56 – 58

3

Helix

61 – 65

5

Beta strand

74 – 76

3

Beta strand

82 – 85

4

Helix

86 – 96

11

Helix

107 – 119

13

Turn

120 – 122

3

Helix

123 – 136

14

Helix

141 – 161

21

Beta strand

168 – 170

3

Helix

173 – 183

11

Helix

185 – 188

4

Helix

191 – 194

4

Helix

198 – 208

11

Helix

211 – 216

6

Helix

220 – 231

12

Helix

235 – 238

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 45A959432BCF490A	FASTA	243	28,254
	10 20 30 40 50 60 MSGDATRTLG KGSQPPGPVP EGLIRIYSMR FCPYSHRTRL VLKAKDIRHE VVNINLRNKP 70 80 90 100 110 120 EWYYTKHPFG HIPVLETSQC QLIYESVIAC EYLDDAYPGR KLFPYDPYER ARQKMLLELF 130 140 150 160 170 180 CKVPHLTKEC LVALRCGREC TNLKAALRQE FSNLEEILEY QNTTFFGGTC ISMIDYLLWP 190 200 210 220 230 240 WFERLDVYGI LDCVSHTPAL RLWISAMKWD PTVCALLMDK SIFQGFLNLY FQNNPNAFDF GLC
	Isoform 2 [UniParc]. Checksum: 4FEFB66449685934	FASTA	209	24,399
	10 20 30 40 50 60 MSGDATRTLG KGSQPPGPVP EGLIRIYSMR FCPYSHRTRL VLKAKDIRHE VVNINLRNKP 70 80 90 100 110 120 EWYYTKHPFG HIPVLETSQC QLIYESVIAC EYLDDAYPGR KLFPYDPYER ARQKMLLELF 130 140 150 160 170 180 CKILEYQNTT FFGGTCISMI DYLLWPWFER LDVYGILDCV SHTPALRLWI SAMKWDPTVC 190 200 ALLMDKSIFQ GFLNLYFQNN PNAFDFGLC
	Isoform 3 [UniParc]. Checksum: A04CD756F6EB962F	FASTA	215	25,387
	10 20 30 40 50 60 MRFCPYSHRT RLVLKAKDIR HEVVNINLRN KPEWYYTKHP FGHIPVLETS QCQLIYESVI 70 80 90 100 110 120 ACEYLDDAYP GRKLFPYDPY ERARQKMLLE LFCKVPHLTK ECLVALRCGR ECTNLKAALR 130 140 150 160 170 180 QEFSNLEEIL EYQNTTFFGG TCISMIDYLL WPWFERLDVY GILDCVSHTP ALRLWISAMK 190 200 210 WDPTVCALLM DKSIFQGFLN LYFQNNPNAF DFGLC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of human GSTO-2 gene." Wang L., Xie Y., Mao Y. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	Xu J., Xie Y., Mao Y. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Skeletal muscle and Thalamus.
[4]	"The DNA sequence and comparative analysis of human chromosome 10." 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. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Brain and Pancreatic carcinoma.
[7]	"Characterization of the human Omega class glutathione transferase genes and associated polymorphisms." Whitbread A.K., Tetlow N., Eyre H.J., Sutherland G.R., Board P.G. Pharmacogenetics 13:131-144(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-243 (ISOFORM 1), VARIANT ASP-142, TISSUE SPECIFICITY. Tissue: Testis.
[8]	"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." Schmuck E.M., Board P.G., Whitbread A.K., Tetlow N., Cavanaugh J.A., Blackburn A.C., Masoumi A. Pharmacogenet. Genomics 15:493-501(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.
[9]	"Structural insights into the dehydroascorbate reductase activity of human omega-class glutathione transferases." Zhou H., Brock J., Liu D., Board P.G., Oakley A.J. J. Mol. Biol. 420:190-203(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-239 ALONE AND IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-34.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY350731 mRNA. Translation: AAR02452.1.
AY209189 mRNA. Translation: AAP47743.1.
AK291886 mRNA. Translation: BAF84575.1.
AK296266 mRNA. Translation: BAG58978.1.
AL139341 Genomic DNA. No translation available.
AL162742 Genomic DNA. Translation: CAC16040.1.
AL162742 Genomic DNA. Translation: CAI12107.1.
CH471066 Genomic DNA. Translation: EAW49600.1.
BC046194 mRNA. No translation available.
BC056918 mRNA. Translation: AAH56918.1.
AY191318 mRNA. Translation: AAO23573.1.

IPI

IPI00007512.
IPI00647624.
IPI00908358.

RefSeq

NP_001177942.1. NM_001191013.1.
NP_001177943.1. NM_001191014.1.
NP_001177944.1. NM_001191015.1.
NP_899062.1. NM_183239.1.

UniGene

Hs.203634.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3Q18	X-ray	1.70	A/B	1-239	[»]
3Q19	X-ray	1.90	A/B	1-239	[»]
3QAG	X-ray	2.00	A	1-239	[»]

ProteinModelPortal

Q9H4Y5.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000345023.

PTM databases

PhosphoSite

Q9H4Y5.

Polymorphism databases

DMDM

34922124.

Proteomic databases

PaxDb

Q9H4Y5.

PRIDE

Q9H4Y5.

Protocols and materials databases

DNASU

119391.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338595; ENSP00000345023; ENSG00000065621.
ENST00000369707; ENSP00000358721; ENSG00000065621.
ENST00000369708; ENSP00000358722; ENSG00000065621.
ENST00000450629; ENSP00000390986; ENSG00000065621.

GeneID

119391.

KEGG

hsa:119391.

UCSC

uc001kyb.3. human.

Organism-specific databases

CTD

119391.

GeneCards

GC10P106018.

HGNC

HGNC:23064. GSTO2.

HPA

HPA048141.

MIM

612314. gene.

neXtProt

NX_Q9H4Y5.

PharmGKB

PA133787053.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0625.

HOGENOM

HOG000006560.

HOVERGEN

HBG051853.

InParanoid

Q9H4Y5.

KO

K00799.

OMA

VYGIADC.

OrthoDB

EOG43TZW5.

PhylomeDB

Q9H4Y5.

Enzyme and pathway databases

BRENDA

2.5.1.18. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

Q9H4Y5.

Bgee

Q9H4Y5.

CleanEx

HS_GSTO2.

Genevestigator

Q9H4Y5.

GermOnline

ENSG00000065621. Homo sapiens.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

PRINTS

PR01625. GSTRNSFRASEO.

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2161.

DrugBank

DB00143. Glutathione.

GenomeRNAi

119391.

NextBio

80409.

SOURCE

Search...

Entry information

Entry name

GSTO2_HUMAN

Accession

Primary (citable) accession number: Q9H4Y5
Secondary accession number(s): A8K771 , B4DJW6, E7ESD6, Q49TW5, Q5GM70, Q5JU15, Q86WP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.