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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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).
Catalytic activity	RX + glutathione = HX + R-S-glutathione. 2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate. Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O.
Tissue specificity	Expressed in a range of tissues, including the liver, kidney, skeletal muscle and prostate. Strongest expression in the testis. Ref.6
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.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Molecular function	Oxidoreductase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	water-soluble vitamin metabolic process Traceable author statement. Source: Reactome xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	glutathione transferase activity Traceable author statement. Source: Reactome
Complete GO annotation...

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 By similarity
Sites
	Active site	32	1	Nucleophile By similarity
	Binding site	59	1	Glutathione By similarity
	Binding site	72	1	Glutathione; via amide nitrogen and carbonyl oxygen By similarity
Natural variations
	Natural variant	130	1	C → Y. Corresponds to variant rs45582439 [ dbSNP | Ensembl ].		VAR_049492
	Natural variant	142	1	N → D. Ref.6 Corresponds to variant rs156697 [ dbSNP | Ensembl ].		VAR_016812
Experimental info
	Sequence conflict	215	1	A → V in AAP47743. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9H4Y5 [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

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].
[2]	Xu J., Xie Y., Mao Y. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skeletal muscle.
[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: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	"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: 12618591] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-243, VARIANT ASP-142, TISSUE SPECIFICITY. Tissue: Testis.
[7]	"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: 15970797] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.
+	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. AL162742 Genomic DNA. Translation: CAC16040.1. BC056918 mRNA. Translation: AAH56918.1. AY191318 mRNA. Translation: AAO23573.1.
IPI	IPI00007512.
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
ProteinModelPortal	Q9H4Y5.
SMR	Q9H4Y5. Positions 5-242.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9H4Y5.
Polymorphism databases
DMDM	34922124.
Proteomic databases
PRIDE	Q9H4Y5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000338595; ENSP00000345023; ENSG00000065621. ENST00000369708; ENSP00000358722; ENSG00000065621. ENST00000401888; ENSP00000386011; ENSG00000065621.
GeneID	119391.
KEGG	hsa:119391.
UCSC	uc001kyb.1. human.
Organism-specific databases
CTD	119391.
GeneCards	GC10P106018.
H-InvDB	HIX0018455.
HGNC	HGNC:23064. GSTO2.
MIM	612314. gene.
neXtProt	NX_Q9H4Y5.
PharmGKB	PA133787053.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10020.
GeneTree	ENSGT00390000005479.
HOGENOM	HBG714248.
HOVERGEN	HBG051853.
InParanoid	Q9H4Y5.
OMA	IACEYLD.
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
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]
Gene3D	G3DSA:1.20.1050.10. GST_C_like. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K00799.
Pfam	PF02798. GST_N. 1 hit. [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
DrugBank	DB00143. Glutathione.
NextBio	80409.
SOURCE	Search...

Entry information

Entry name

GSTO2_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 89 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.