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Q9N4X8 (GSTPA_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. 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 S-transferase P 10

EC=2.5.1.18
Alternative name(s):
GST 5.4
GST class-pi
GSTP2-2
Gene names
Name:gst-10
ORF Names:Y45G12C.2
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Responsible for approximately one-third of 4-hydroxy-2-nonenal conjugation. Ref.1 Ref.3 Ref.4

Catalytic activity

RX + glutathione = HX + R-S-glutathione. UniProtKB P10299

Subunit structure

Homodimer Potential. UniProtKB P10299

Tissue specificity

Expressed in cells at the mouth and adjacent to the pharyngeal bulbs of the head and also in the tail. Ref.3

Disruption phenotype

Increase in susceptibility to 4-hydroxy-2-nonenal, paraquat and heat shock and a reduced lifespan. Ref.4

Sequence similarities

Belongs to the GST superfamily. Pi family. UniProtKB P10299

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

KM=50 µM for 4-HNE Ref.3

Vmax=10.3 µmol/min/mg enzyme Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 210209Glutathione S-transferase P 10 Ref.1
PRO_0000185912

Regions

Domain2 – 8180GST N-terminal
Domain83 – 200118GST C-terminal
Region52 – 532Glutathione binding By similarity
Region65 – 662Glutathione binding By similarity

Sites

Binding site81Glutathione By similarity
Binding site411Glutathione By similarity
Binding site451Glutathione By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9N4X8 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 31AF3BC1ED43594B

FASTA21024,796
        10         20         30         40         50         60 
MAVPQLYYFT IRGFGEYIRL LFLDNGIKFE DIRFDYEGNE WQEFKKGMLL GQLPCLKVDG 

        70         80         90        100        110        120 
QEIVQTGAIM RHLGRVHGLN GSNEQEATFL DMFFEGVRDV RMKYVRYIYY DEGTREDCVN 

       130        140        150        160        170        180 
KTIPEALVKL EELFKAHSGD FIIGNKISYA DYILFEELDV YHVLDANILD KFPTLKSFWE 

       190        200        210 
RMWKRPNLNA YLEKRKADKV WINAIEKGMN 

« Hide

References

« Hide 'large scale' references
[1]"Invertebrate glutathione transferases conjugating 4-hydroxynonenal: CeGST 5.4 from Caenorhabditis elegans."
Engle M.R., Singh S.P., Nanduri B., Ji X., Zimniak P.
Chem. Biol. Interact. 133:244-248(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-11, FUNCTION.
[2]"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.
[3]"Lifespan and stress resistance of Caenorhabditis elegans are increased by expression of glutathione transferases capable of metabolizing the lipid peroxidation product 4-hydroxynonenal."
Ayyadevara S., Engle M.R., Singh S.P., Dandapat A., Lichti C.F., Benes H., Shmookler Reis R.J., Liebau E., Zimniak P.
Aging Cell 4:257-271(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[4]"Lifespan extension in hypomorphic daf-2 mutants of Caenorhabditis elegans is partially mediated by glutathione transferase CeGSTP2-2."
Ayyadevara S., Dandapat A., Singh S.P., Benes H., Zimniak L., Reis R.J.S., Zimniak P.
Aging Cell 4:299-307(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FO080245 Genomic DNA. Translation: CCD62297.1.
RefSeqNP_503701.1. NM_071300.7.
UniGeneCel.34291.

3D structure databases

ProteinModelPortalQ9N4X8.
SMRQ9N4X8. Positions 5-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9N4X8. 1 interaction.
STRING6239.Y45G12C.2.1.

Proteomic databases

PaxDbQ9N4X8.
PRIDEQ9N4X8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaY45G12C.2; Y45G12C.2; Y45G12C.2.
GeneID178725.
KEGGcel:CELE_Y45G12C.2.
UCSCY45G12C.2.1. c. elegans.

Organism-specific databases

CTD178725.
WormBaseY45G12C.2; CE21937; WBGene00001758; gst-10.

Phylogenomic databases

eggNOGNOG266414.
HOGENOMHOG000115733.
InParanoidQ9N4X8.
KOK00799.
OMAADKVWIN.
OrthoDBEOG79CZ0K.
PhylomeDBQ9N4X8.

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.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio902290.

Entry information

Entry nameGSTPA_CAEEL
AccessionPrimary (citable) accession number: Q9N4X8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 89 of the entry and version 3 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