Q8JFZ2 (GSTP1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

gstp1

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	212 AA.
Sequence status	Complete.
Protein existence	Evidence 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 motochondrial 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 component	Cytoplasm Mitochondrion Nucleus
Molecular function	Transferase
Gene Ontology (GO)
Biological_process	glutathione metabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutathione transferase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 212	212	Glutathione S-transferase P 1		PRO_0000185910
Regions
	Domain	2 – 83	82	GST N-terminal
	Domain	85 – 206	122	GST C-terminal
	Region	54 – 55	2	Glutathione binding By similarity
	Region	67 – 68	2	Glutathione binding By similarity
Sites
	Binding site	8	1	Glutathione By similarity
	Binding site	14	1	Glutathione By similarity
	Binding site	39	1	Glutathione By similarity
	Binding site	47	1	Glutathione By similarity
Experimental info
	Mutagenesis	111	1	F → Y: Reduction in activity and altered substrate specificity; inactive towards 4-nitroquinoline-1-oxide, active towards ethacrynic acid and tPBO. Ref.1
	Mutagenesis	208	1	P → G or H: Reduction in activity. Ref.1
	Sequence conflict	203	1	K → R in AAH68854. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8JFZ2 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: E5BF0166C08CC5BA	FASTA	212	24,428
	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

References

	« Hide 'large scale' referencesShow '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.
RefSeq	NP_001082252.1. NM_001088783.1.
UniGene	Xl.54920.
3D structure databases
ProteinModelPortal	Q8JFZ2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	398321.
KEGG	xla:398321.
Organism-specific databases
CTD	2950.
Xenbase	XB-GENE-5846294. gstp1.
Phylogenomic databases
HOVERGEN	HBG108324.
KO	K00799.
Family and domain databases
Gene3D	1.20.1050.10. 1 hit. 3.40.30.10. 1 hit.
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR003082. GST_pi. IPR012336. Thioredoxin-like_fold. [Graphical view]
Pfam	PF00043. GST_C. 1 hit. PF02798. GST_N. 1 hit. [Graphical view]
PRINTS	PR01268. GSTRNSFRASEP.
SUPFAM	SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSTP1_XENLA

Accession

Primary (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:	March 6, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program