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Q9Z339 (GSTO1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase omega-1

Short name=GSTO-1
EC=2.5.1.18
Alternative name(s):
Glutathione S-transferase omega 1-1
Short name=GSTO 1-1
Glutathione-dependent dehydroascorbate reductase
EC=1.8.5.1
Monomethylarsonic acid reductase
Short name=MMA(V) reductase
EC=1.20.4.2
S-(Phenacyl)glutathione reductase
Short name=SPG-R
Gene names
Name:Gsto1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

Catalytic activity

RX + glutathione = HX + R-S-glutathione.

2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.

Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O.

Subunit structure

Homodimer.

Subcellular location

Cytoplasmcytosol.

Sequence similarities

Belongs to the GST superfamily. Omega family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence caution

The sequence BAA34217.1 differs from that shown. Reason: Frameshift at position 23.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionOxidoreductase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processL-ascorbic acid biosynthetic process

Inferred from mutant phenotype Ref.1. Source: RGD

L-ascorbic acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to arsenic-containing substance

Inferred from sequence or structural similarity. Source: UniProtKB

xenobiotic catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from direct assay PubMed 11311527. Source: RGD

basement membrane

Inferred from direct assay PubMed 11311527. Source: RGD

cell body

Inferred from direct assay PubMed 11311527. Source: RGD

cytoplasm

Inferred from direct assay PubMed 11311527. Source: RGD

cytosol

Inferred from direct assay Ref.1. Source: RGD

myelin sheath

Inferred from direct assay PubMed 11311527. Source: RGD

nuclear membrane

Inferred from direct assay PubMed 11311527. Source: RGD

   Molecular_functionglutathione dehydrogenase (ascorbate) activity

Inferred from direct assay Ref.1. Source: RGD

glutathione transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

methylarsonate reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

oxidoreductase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 241240Glutathione S-transferase omega-1
PRO_0000185887

Regions

Domain22 – 10180GST N-terminal
Domain106 – 228123GST C-terminal
Region85 – 862Glutathione binding By similarity

Sites

Active site321Nucleophile By similarity
Binding site591Glutathione By similarity
Binding site721Glutathione; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue571N6-acetyllysine By similarity
Modified residue1431N6-acetyllysine By similarity
Modified residue1481N6-acetyllysine By similarity
Modified residue1521N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z339 [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: 31EAC5A7CAF22BC6

FASTA24127,669
        10         20         30         40         50         60 
MSGASARSLG KGSAPPGPVP EGQIRVYSMR FCPFAQRTLM VLKAKGIRHE IININLKNKP 

        70         80         90        100        110        120 
EWFFEKNPFG LVPVLENTQG HLITESVITC EYLDEAYPEK KLFPDDPYEK ACQKMTFELF 

       130        140        150        160        170        180 
SKVPSLVTSF IRAKRKEDHP GIKEELKKEF SKLEEAMANK RTAFFGGNSL SMIDYLIWPW 

       190        200        210        220        230        240 
FQRLEALELN ECIDHTPKLK LWMATMQEDP VASSHFIDAK TYRDYLSLYL QDSPEACDYG 


L 

« Hide

References

[1]"Molecular cloning and functional expression of rat liver glutathione-dependent dehydroascorbate reductase."
Ishikawa T., Casini A.F., Nishikimi M.
J. Biol. Chem. 273:28708-28712(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]Lubec G., Diao W., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 38-43 AND 123-132, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Hippocampus.
[3]"Purification and characterization of glutathione-dependent dehydroascorbate reductase from rat liver."
Maellaro E., Del Bello B., Sugherini L., Santucci A., Comporti M., Casini A.F.
Biochem. J. 301:471-476(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB008807 mRNA. Translation: BAA34217.1. Frameshift.
UniGeneRn.25166.

3D structure databases

ProteinModelPortalQ9Z339.
SMRQ9Z339. Positions 5-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4569802.

PTM databases

PhosphoSiteQ9Z339.

2D gel databases

World-2DPAGE0004:Q9Z339.

Proteomic databases

PaxDbQ9Z339.
PRIDEQ9Z339.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:70952. rat.

Organism-specific databases

RGD70952. Gsto1.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000006560.
HOVERGENHBG051853.
InParanoidQ9Z339.
PhylomeDBQ9Z339.

Gene expression databases

GenevestigatorQ9Z339.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
PRINTSPR01625. GSTRNSFRASEO.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9Z339.

Entry information

Entry nameGSTO1_RAT
AccessionPrimary (citable) accession number: Q9Z339
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 24, 2001
Last modified: April 16, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families