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Q8JFZ2

- GSTP1_XENLA

UniProt

Q8JFZ2 - GSTP1_XENLA

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Protein

Glutathione S-transferase P 1

Gene
gstp1
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei8 – 81Glutathione By similarity
Binding sitei14 – 141Glutathione By similarity
Binding sitei39 – 391Glutathione By similarity
Binding sitei47 – 471Glutathione By similarity

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB

GO - Biological processi

  1. glutathione metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase P 1 (EC:2.5.1.18)
Alternative name(s):
GST class-pi
Short name:
GST-Pi
XlGSTP1-1
Gene namesi
Name:gstp1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-5846294. gstp1.

Subcellular locationi

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.

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi111 – 1111F → Y: Reduction in activity and altered substrate specificity; inactive towards 4-nitroquinoline-1-oxide, active towards ethacrynic acid and tPBO. 1 Publication
Mutagenesisi208 – 2081P → G or H: Reduction in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Glutathione S-transferase P 1PRO_0000185910Add
BLAST

Expressioni

Tissue specificityi

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

Developmental stagei

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

Interactioni

Subunit structurei

Homodimer By similarity.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8JFZ2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8382GST N-terminalAdd
BLAST
Domaini85 – 206122GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 552Glutathione binding By similarity
Regioni67 – 682Glutathione binding By similarity

Sequence similaritiesi

Belongs to the GST superfamily. Pi family.

Phylogenomic databases

HOVERGENiHBG108324.
KOiK00799.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01268. GSTRNSFRASEP.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8JFZ2-1 [UniParc]FASTAAdd to Basket

« Hide

MPGYVLTYFP VRGRAEPIRL LLADQGISWK EDEVQIPDWF SGKDARKKEA    50
VFGQLPQFQD GDYVLYQSNS ILRYLGNKHG LTGANDEERG HIDMVNDGVE 100
DLRQKYGRLI FFEYETGKDK YLKELPSQLD FFERILSKNA NGSKFVVGQK 150
ISFADYNLLD ILQCHLDLCS KSLSAYPLLT AYVERLVARP KISEYLKSDA 200
RNKRPITPKH KK 212
Length:212
Mass (Da):24,428
Last modified:October 1, 2002 - v1
Checksum:iE5BF0166C08CC5BA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031K → R in AAH68854. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ489617 mRNA. Translation: CAD33920.1.
BC068854 mRNA. Translation: AAH68854.1.
RefSeqiNP_001082252.1. NM_001088783.1.
UniGeneiXl.54920.

Genome annotation databases

GeneIDi398321.
KEGGixla:398321.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ489617 mRNA. Translation: CAD33920.1 .
BC068854 mRNA. Translation: AAH68854.1 .
RefSeqi NP_001082252.1. NM_001088783.1.
UniGenei Xl.54920.

3D structure databases

ProteinModelPortali Q8JFZ2.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 398321.
KEGGi xla:398321.

Organism-specific databases

CTDi 2950.
Xenbasei XB-GENE-5846294. gstp1.

Phylogenomic databases

HOVERGENi HBG108324.
KOi K00799.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view ]
PRINTSi PR01268. GSTRNSFRASEP.
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiGSTP1_XENLA
AccessioniPrimary (citable) accession number: Q8JFZ2
Secondary accession number(s): Q6NTV0
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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