P04906 (GSTP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase P
EC=2.5.1.18

Alternative name(s):
Chain 7
GST 7-7
GST class-pi

Gene names

Name:

Gstp1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration By similarity.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer. Interacts with CDK5 By similarity.
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	Present in kidney, lung, testis and placenta, very low levels in liver.
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
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to cell-matrix adhesion Inferred from expression pattern PubMed 10793289. Source: RGD cellular response to epidermal growth factor stimulus Inferred from expression pattern PubMed 1908848. Source: RGD cellular response to glucocorticoid stimulus Inferred from expression pattern PubMed 18349876. Source: RGD cellular response to insulin stimulus Inferred from expression pattern PubMed 1908848. Source: RGD cellular response to lipopolysaccharide Inferred from sequence or structural similarity. Source: BHF-UCL common myeloid progenitor cell proliferation Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of I-kappaB kinase/NF-kappaB cascade Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of JUN kinase activity Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of fibroblast proliferation Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of interleukin-1 beta production Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of leukocyte proliferation Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of monocyte chemotactic protein-1 production Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of necrotic cell death Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of nitric-oxide synthase biosynthetic process Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of stress-activated MAPK cascade Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of tumor necrosis factor production Inferred from sequence or structural similarity. Source: BHF-UCL oligodendrocyte development Inferred from expression pattern PubMed 17681700. Source: RGD organ regeneration Inferred from expression pattern PubMed 7499462. Source: RGD positive regulation of superoxide anion generation Inferred from sequence or structural similarity. Source: BHF-UCL response to L-ascorbic acid Inferred from expression pattern PubMed 9834927. Source: RGD response to amino acid stimulus Inferred from expression pattern PubMed 20013880. Source: RGD response to estradiol stimulus Inferred from expression pattern PubMed 9505896. Source: RGD response to ethanol Inferred from expression pattern PubMed 2206462. Source: RGD response to mercury ion Inferred from expression pattern PubMed 12730625. Source: RGD response to reactive oxygen species Inferred from sequence or structural similarity. Source: BHF-UCL response to toxin Inferred from expression pattern PubMed 19790251. Source: RGD xenobiotic metabolic process Inferred from direct assay PubMed 11018474. Source: RGD
Cellular_component	cytosol Inferred from direct assay PubMed 3421895. Source: RGD mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 15942958. Source: RGD plasma membrane Inferred from direct assay PubMed 18349876. Source: RGD protein complex Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	JUN kinase binding Inferred from sequence or structural similarity. Source: BHF-UCL drug binding Inferred from direct assay PubMed 11018474. Source: RGD glutathione binding Inferred from direct assay PubMed 11018474. Source: RGD glutathione transferase activity Inferred from direct assay PubMed 11018474. Source: RGD kinase regulator activity Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4 Ref.5 Ref.6
	Chain	2 – 210	209	Glutathione S-transferase P		PRO_0000185907
Regions
	Domain	2 – 81	80	GST N-terminal
	Domain	83 – 204	122	GST C-terminal
	Region	52 – 53	2	Glutathione binding By similarity
	Region	65 – 66	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	45	1	Glutathione By similarity
Amino acid modifications
	Modified residue	4	1	Phosphotyrosine; by EGFR By similarity
	Modified residue	109	1	Phosphotyrosine By similarity
	Modified residue	128	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	15	1	C → Y AA sequence Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P04906 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 9B71785D1FC28FDB	FASTA	210	23,439
	10 20 30 40 50 60 MPPYTIVYFP VRGRCEATRM LLADQGQSWK EEVVTIDVWL QGSLKSTCLY GQLPKFEDGD 70 80 90 100 110 120 LTLYQSNAIL RHLGRSLGLY GKDQKEAALV DMVNDGVEDL RCKYGTLIYT NYENGKDDYV 130 140 150 160 170 180 KALPGHLKPF ETLLSQNQGG KAFIVGNQIS FADYNLLDLL LVHQVLAPGC LDNFPLLSAY 190 200 210 VARLSARPKI KAFLSSPDHL NRPINGNGKQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and the nucleotide sequence of rat glutathione S-transferase P cDNA." Suguoka Y., Kano T., Okuda A., Sakai M., Kitagawa T., Muramatsu M. Nucleic Acids Res. 13:6049-6057(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The structure of the rat glutathione S-transferase P gene and related pseudogenes." Okuda A., Sakai M., Muramatsu M. J. Biol. Chem. 262:3858-3863(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sprague-Dawley. Tissue: Liver.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pituitary.
[4]	"Purification and characterization of P-52 (glutathione S-transferase-P or 7-7) from normal liver and putative preneoplastic liver nodules." Rushmore T.H., Harris L., Nagai M., Sharma R.N., Hayes M.A., Cameron R.G., Murray R.K., Farber E. Cancer Res. 48:2805-2812(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-27.
[5]	Lubec G., Afjehi-Sadat L., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-12; 56-71; 122-141 AND 192-209, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord.
[6]	"Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties." Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Joernvall H. Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X02904 mRNA. Translation: CAA26664.1. L29427 Genomic DNA. Translation: AAB59718.1. BC058439 mRNA. Translation: AAH58439.1. BC058440 mRNA. Translation: AAH58440.1.
IPI	IPI00231229.
PIR	XURTGP. A26546. S59902.
RefSeq	NP_036709.1. NM_012577.2.
UniGene	Rn.87063.
3D structure databases
ProteinModelPortal	P04906.
SMR	P04906. Positions 2-210.
ModBase	Search...
Protein-protein interaction databases
IntAct	P04906. 1 interaction.
PTM databases
PhosphoSite	P04906.
2D gel databases
World-2DPAGE	0004:P04906.
Proteomic databases
PaxDb	P04906.
PRIDE	P04906.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000024601; ENSRNOP00000024601; ENSRNOG00000018237.
GeneID	24426.
KEGG	rno:24426.
UCSC	RGD:2758. rat.
Organism-specific databases
CTD	2950.
RGD	2758. Gstp1.
Phylogenomic databases
eggNOG	NOG05174.
GeneTree	ENSGT00550000074559.
HOGENOM	HOG000115733.
HOVERGEN	HBG108324.
InParanoid	P04906.
KO	K00799.
OMA	YEAGKDD.
OrthoDB	EOG48SGTZ.
Gene expression databases
ArrayExpress	P04906.
Genevestigator	P04906.
GermOnline	ENSRNOG00000018237. Rattus norvegicus.
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...
Other
NextBio	603297.
PMAP-CutDB	P04906.

Entry information

Entry name

GSTP1_RAT

Accession

Primary (citable) accession number: P04906

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program