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Q8JFZ2 (GSTP1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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 P 1

EC=2.5.1.18
Alternative name(s):
GST class-pi
Short name=GST-Pi
XlGSTP1-1
Gene names
Name:gstp1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Highly active towards 1-chloro-2,4-dinitrobenzene and organic isothiocyanates, but shows no detectable activity towards 1,2-dichloro-4-nitrobenzene, p-nitrobenzylchloride, trans-4-phenyl-3-buten-2-one (tPBO) and ethacrynic acid. May be associated with cellular proliferation. Ref.1

Catalytic activity

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

Subunit structure

Homodimer By similarity. UniProtKB P83325

Subcellular location

Cytoplasm By similarity. Mitochondrion By similarity. Nucleus By similarity. Note: The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization By similarity.

Tissue specificity

Expressed only in embryos. Not expressed in liver, lung, heart, kidney and ovary. Ref.1

Developmental stage

Detected in embryos at stages 11-15, but not detected in unfertilized eggs. Ref.1

Sequence similarities

Belongs to the GST superfamily. Pi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Molecular functionTransferase
Gene Ontology (GO)
   Biological_processglutathione metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutathione transferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Glutathione S-transferase P 1
PRO_0000185910

Regions

Domain2 – 8382GST N-terminal
Domain85 – 206122GST C-terminal
Region54 – 552Glutathione binding By similarity
Region67 – 682Glutathione binding By similarity

Sites

Binding site81Glutathione By similarity
Binding site141Glutathione By similarity
Binding site391Glutathione By similarity
Binding site471Glutathione By similarity

Experimental info

Mutagenesis1111F → Y: Reduction in activity and altered substrate specificity; inactive towards 4-nitroquinoline-1-oxide, active towards ethacrynic acid and tPBO. Ref.1
Mutagenesis2081P → G or H: Reduction in activity. Ref.1
Sequence conflict2031K → R in AAH68854. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8JFZ2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: E5BF0166C08CC5BA

FASTA21224,428
        10         20         30         40         50         60 
MPGYVLTYFP VRGRAEPIRL LLADQGISWK EDEVQIPDWF SGKDARKKEA VFGQLPQFQD 

        70         80         90        100        110        120 
GDYVLYQSNS ILRYLGNKHG LTGANDEERG HIDMVNDGVE DLRQKYGRLI FFEYETGKDK 

       130        140        150        160        170        180 
YLKELPSQLD FFERILSKNA NGSKFVVGQK ISFADYNLLD ILQCHLDLCS KSLSAYPLLT 

       190        200        210 
AYVERLVARP KISEYLKSDA RNKRPITPKH KK 

« Hide

References

« Hide 'large scale' references
[1]"A novel amphibian Pi-class glutathione transferase isoenzyme from Xenopus laevis: importance of phenylalanine 111 in the H-site."
De Luca A., Favaloro B., Carletti E., Sacchetta P., Di Ilio C.
Biochem. J. 373:539-545(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF PHE-111 AND PRO-208.
Tissue: Liver tumor.
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-212.
Tissue: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ489617 mRNA. Translation: CAD33920.1.
BC068854 mRNA. Translation: AAH68854.1.
RefSeqNP_001082252.1. NM_001088783.1.
UniGeneXl.54920.

3D structure databases

ProteinModelPortalQ8JFZ2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID398321.
KEGGxla:398321.

Organism-specific databases

CTD2950.
XenbaseXB-GENE-5846294. gstp1.

Phylogenomic databases

HOVERGENHBG108324.
KOK00799.

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.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSPR01268. GSTRNSFRASEP.
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSTP1_XENLA
AccessionPrimary (citable) accession number: Q8JFZ2
Secondary accession number(s): Q6NTV0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2002
Last modified: February 19, 2014
This is version 64 of the entry and version 1 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