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Glutathione S-transferase P (EC 2.5.1.18) (Chain 7) (GST 7-7) (GST class-pi)

 GSTP1_RAT               Reviewed;         210 AA.
P04906;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 154.
RecName: Full=Glutathione S-transferase P;
EC=2.5.1.18;
AltName: Full=Chain 7;
AltName: Full=GST 7-7;
AltName: Full=GST class-pi;
Name=Gstp1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2995915; DOI=10.1093/nar/13.17.6049;
Suguoka Y., Kano T., Okuda A., Sakai M., Kitagawa T., Muramatsu M.;
"Cloning and the nucleotide sequence of rat glutathione S-transferase
P cDNA.";
Nucleic Acids Res. 13:6049-6057(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=3029128;
Okuda A., Sakai M., Muramatsu M.;
"The structure of the rat glutathione S-transferase P gene and related
pseudogenes.";
J. Biol. Chem. 262:3858-3863(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 2-27.
PubMed=3359441;
Rushmore T.H., Harris L., Nagai M., Sharma R.N., Hayes M.A.,
Cameron R.G., Murray R.K., Farber E.;
"Purification and characterization of P-52 (glutathione S-transferase-
P or 7-7) from normal liver and putative preneoplastic liver
nodules.";
Cancer Res. 48:2805-2812(1988).
[5]
PROTEIN SEQUENCE OF 2-12; 56-71; 122-141 AND 192-209, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 2-11.
PubMed=3864155; DOI=10.1073/pnas.82.21.7202;
Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K.,
Warholm M., Joernvall H.;
"Identification of three classes of cytosolic glutathione transferase
common to several mammalian species: correlation between structural
data and enzymatic properties.";
Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985).
-!- 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBUNIT: Homodimer. Interacts with CDK5 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion
{ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino
acids function as un uncleaved transit peptide, and arginine
residues within it are crucial for mitochondrial localization.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Present in kidney, lung, testis and placenta,
very low levels in liver.
-!- SIMILARITY: Belongs to the GST superfamily. Pi family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X02904; CAA26664.1; -; mRNA.
EMBL; L29427; AAB59718.1; -; Genomic_DNA.
EMBL; BC058439; AAH58439.1; -; mRNA.
EMBL; BC058440; AAH58440.1; -; mRNA.
PIR; A26546; XURTGP.
PIR; S59902; S59902.
RefSeq; NP_036709.1; NM_012577.2.
UniGene; Rn.87063; -.
ProteinModelPortal; P04906; -.
SMR; P04906; -.
BioGrid; 246591; 1.
IntAct; P04906; 1.
STRING; 10116.ENSRNOP00000024601; -.
iPTMnet; P04906; -.
PhosphoSitePlus; P04906; -.
World-2DPAGE; 0004:P04906; -.
PaxDb; P04906; -.
PRIDE; P04906; -.
Ensembl; ENSRNOT00000024601; ENSRNOP00000024601; ENSRNOG00000018237.
GeneID; 24426; -.
KEGG; rno:24426; -.
UCSC; RGD:2758; rat.
CTD; 2950; -.
RGD; 2758; Gstp1.
eggNOG; KOG1695; Eukaryota.
eggNOG; ENOG4111VAU; LUCA.
GeneTree; ENSGT00550000074559; -.
HOGENOM; HOG000115733; -.
HOVERGEN; HBG108324; -.
InParanoid; P04906; -.
KO; K00799; -.
OMA; LRCKYAT; -.
OrthoDB; EOG091G0K2E; -.
PhylomeDB; P04906; -.
TreeFam; TF105321; -.
Reactome; R-RNO-156590; Glutathione conjugation.
Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PMAP-CutDB; P04906; -.
PRO; PR:P04906; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000018237; -.
ExpressionAtlas; P04906; baseline and differential.
Genevisible; P04906; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005622; C:intracellular; ISS:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043234; C:protein complex; ISS:BHF-UCL.
GO; GO:0097057; C:TRAF2-GSTP1 complex; IEA:Ensembl.
GO; GO:0035731; F:dinitrosyl-iron complex binding; IEA:Ensembl.
GO; GO:0008144; F:drug binding; IDA:RGD.
GO; GO:0043295; F:glutathione binding; IDA:RGD.
GO; GO:0004602; F:glutathione peroxidase activity; IEA:Ensembl.
GO; GO:0004364; F:glutathione transferase activity; IDA:RGD.
GO; GO:0008432; F:JUN kinase binding; ISS:BHF-UCL.
GO; GO:0019207; F:kinase regulator activity; ISS:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0035730; F:S-nitrosoglutathione binding; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
GO; GO:0071460; P:cellular response to cell-matrix adhesion; IEP:RGD.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:BHF-UCL.
GO; GO:0035726; P:common myeloid progenitor cell proliferation; ISS:BHF-UCL.
GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
GO; GO:0043651; P:linoleic acid metabolic process; IEA:Ensembl.
GO; GO:0009890; P:negative regulation of biosynthetic process; ISS:BHF-UCL.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:BHF-UCL.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:BHF-UCL.
GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISS:BHF-UCL.
GO; GO:0043508; P:negative regulation of JUN kinase activity; ISS:BHF-UCL.
GO; GO:0070664; P:negative regulation of leukocyte proliferation; ISS:BHF-UCL.
GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; ISS:BHF-UCL.
GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; ISS:BHF-UCL.
GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:RGD.
GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; IMP:RGD.
GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISS:BHF-UCL.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:BHF-UCL.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; IMP:RGD.
GO; GO:0014003; P:oligodendrocyte development; IEP:RGD.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:BHF-UCL.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
GO; GO:0032872; P:regulation of stress-activated MAPK cascade; ISS:BHF-UCL.
GO; GO:0043200; P:response to amino acid; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0033591; P:response to L-ascorbic acid; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0000302; P:response to reactive oxygen species; ISS:BHF-UCL.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:0006805; P:xenobiotic metabolic process; IDA:RGD.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR003082; GST_pi.
InterPro; IPR012336; Thioredoxin-like_fold.
Pfam; PF14497; GST_C_3; 1.
Pfam; PF02798; GST_N; 1.
PRINTS; PR01268; GSTRNSFRASEP.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3359441,
ECO:0000269|PubMed:3864155,
ECO:0000269|Ref.5}.
CHAIN 2 210 Glutathione S-transferase P.
/FTId=PRO_0000185907.
DOMAIN 2 81 GST N-terminal.
DOMAIN 83 204 GST C-terminal.
REGION 52 53 Glutathione binding.
{ECO:0000250|UniProtKB:P09211}.
REGION 65 66 Glutathione binding.
{ECO:0000250|UniProtKB:P09211}.
BINDING 8 8 Glutathione.
{ECO:0000250|UniProtKB:P09211}.
BINDING 14 14 Glutathione.
{ECO:0000250|UniProtKB:P09211}.
BINDING 39 39 Glutathione.
{ECO:0000250|UniProtKB:P09211}.
BINDING 45 45 Glutathione.
{ECO:0000250|UniProtKB:P09211}.
MOD_RES 4 4 Phosphotyrosine; by EGFR.
{ECO:0000250|UniProtKB:P09211}.
MOD_RES 62 62 Phosphothreonine.
{ECO:0000250|UniProtKB:P09211}.
MOD_RES 103 103 N6-succinyllysine.
{ECO:0000250|UniProtKB:P19157}.
MOD_RES 116 116 N6-succinyllysine.
{ECO:0000250|UniProtKB:P19157}.
MOD_RES 128 128 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09211}.
CONFLICT 15 15 C -> Y (in Ref. 4; AA sequence).
{ECO:0000305}.
SEQUENCE 210 AA; 23439 MW; 9B71785D1FC28FDB CRC64;
MPPYTIVYFP VRGRCEATRM LLADQGQSWK EEVVTIDVWL QGSLKSTCLY GQLPKFEDGD
LTLYQSNAIL RHLGRSLGLY GKDQKEAALV DMVNDGVEDL RCKYGTLIYT NYENGKDDYV
KALPGHLKPF ETLLSQNQGG KAFIVGNQIS FADYNLLDLL LVHQVLAPGC LDNFPLLSAY
VARLSARPKI KAFLSSPDHL NRPINGNGKQ


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