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P34345 (GSTO1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 transferase omega-1

EC=2.5.1.18
Alternative name(s):
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:gsto-1
ORF Names:C29E4.7
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exhibits glutathione-dependent thiol transferase activity. Has dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) By similarity. Protects against environmental stress and oxidative stress. Ref.1

Catalytic activity

RX + glutathione = HX + R-S-glutathione. Ref.1

2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate. Ref.1

Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O. Ref.1

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expressed in the intestinal cells. Ref.1

Miscellaneous

Worms lacking gsto-1 exhibit increased sensitivity to heat shock and oxidative stress induced by several prooxidants and arsenite.

Sequence similarities

Belongs to the GST superfamily. Omega family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 250250Glutathione transferase omega-1
PRO_0000185889

Regions

Domain21 – 10181GST N-terminal
Domain106 – 234129GST C-terminal
Region85 – 862Glutathione binding By similarity

Sites

Active site331Nucleophile By similarity
Binding site601Glutathione By similarity

Sequences

Sequence LengthMass (Da)Tools
P34345 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 4EB0E85351217C55

FASTA25028,478
        10         20         30         40         50         60 
MVLTGVTSKA IRKGDAEPPL SKGSFRVYNM RFCPWAERAM LYVAAKGIEA EVVNLNVTDK 

        70         80         90        100        110        120 
LEWYWTKHYQ GKAPAVEHNG KVVIESGFIP EYLDDAFPET RILPTDPYEK VQQKLLADRL 

       130        140        150        160        170        180 
TAVAHAVPLL FAVMRDRTLK DEKQRKVFEV LKQAENLLAN DFYAGSQPGY PDYLSFPFFE 

       190        200        210        220        230        240 
KIWWSASLDG VVDLPTIEFP GEEEYPKLTK WFQKMISSDV VQSVTQSLEH GAAFMNAYAT 

       250 
HQELNYDLGL 

« Hide

References

« Hide 'large scale' references
[1]"Oxidative stress in Caenorhabditis elegans: protective effects of the Omega class glutathione transferase (GSTO-1)."
Burmeister C., Luersen K., Heinick A., Hussein A., Domagalski M., Walter R.D., Liebau E.
FASEB J. 22:343-354(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
[2]"2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans."
Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L. expand/collapse author list , Gardner A., Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J., Wohldman P.
Nature 368:32-38(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FO080706 Genomic DNA. Translation: CCD66006.1.
PIRS44768.
RefSeqNP_498728.1. NM_066327.1.
UniGeneCel.10781.

3D structure databases

ProteinModelPortalP34345.
SMRP34345. Positions 8-228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid47837. 1 interaction.
DIPDIP-24588N.
MINTMINT-1080999.
STRING6239.C29E4.7.

Proteomic databases

PaxDbP34345.
PRIDEP34345.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC29E4.7; C29E4.7; C29E4.7.
GeneID183000.
KEGGcel:CELE_C29E4.7.

Organism-specific databases

CTD183000.
WormBaseC29E4.7; CE00089; WBGene00016204; gsto-1.

Phylogenomic databases

eggNOGNOG288793.
HOGENOMHOG000006560.
InParanoidP34345.
KOK00799.
OMAPEYLDDA.
OrthoDBEOG71CFNG.
PhylomeDBP34345.

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.
PF02798. GST_N. 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

NextBio919570.

Entry information

Entry nameGSTO1_CAEEL
AccessionPrimary (citable) accession number: P34345
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase