GSTP1_RAT
ID GSTP1_RAT Reviewed; 210 AA.
AC P04906;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Glutathione S-transferase P {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P09211};
DE AltName: Full=Chain 7;
DE AltName: Full=GST 7-7;
DE AltName: Full=GST class-pi;
GN Name=Gstp1 {ECO:0000312|RGD:2758};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2995915; DOI=10.1093/nar/13.17.6049;
RA Suguoka Y., Kano T., Okuda A., Sakai M., Kitagawa T., Muramatsu M.;
RT "Cloning and the nucleotide sequence of rat glutathione S-transferase P
RT cDNA.";
RL Nucleic Acids Res. 13:6049-6057(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=3029128; DOI=10.1016/s0021-9258(18)61435-8;
RA Okuda A., Sakai M., Muramatsu M.;
RT "The structure of the rat glutathione S-transferase P gene and related
RT pseudogenes.";
RL J. Biol. Chem. 262:3858-3863(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-27.
RX PubMed=3359441;
RA Rushmore T.H., Harris L., Nagai M., Sharma R.N., Hayes M.A., Cameron R.G.,
RA Murray R.K., Farber E.;
RT "Purification and characterization of P-52 (glutathione S-transferase-P or
RT 7-7) from normal liver and putative preneoplastic liver nodules.";
RL Cancer Res. 48:2805-2812(1988).
RN [5]
RP PROTEIN SEQUENCE OF 2-12; 56-71; 122-141 AND 192-209, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 2-11.
RX PubMed=3864155; DOI=10.1073/pnas.82.21.7202;
RA Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M.,
RA Joernvall H.;
RT "Identification of three classes of cytosolic glutathione transferase
RT common to several mammalian species: correlation between structural data
RT and enzymatic properties.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Involved in the
CC formation of glutathione conjugates of both prostaglandin A2 (PGA2) and
CC prostaglandin J2 (PGJ2). Participates in the formation of novel
CC hepoxilin regioisomers. Regulates negatively CDK5 activity via p25/p35
CC translocation to prevent neurodegeneration.
CC {ECO:0000250|UniProtKB:P09211}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000250|UniProtKB:P09211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000250|UniProtKB:P09211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133771;
CC Evidence={ECO:0000250|UniProtKB:P09211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805;
CC Evidence={ECO:0000250|UniProtKB:P09211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(S)-
CC glutathione; Xref=Rhea:RHEA:50808, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133396, ChEBI:CHEBI:133772;
CC Evidence={ECO:0000250|UniProtKB:P09211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50809;
CC Evidence={ECO:0000250|UniProtKB:P09211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(S)-
CC glutathione; Xref=Rhea:RHEA:50800, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133370, ChEBI:CHEBI:133769;
CC Evidence={ECO:0000250|UniProtKB:P09211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50801;
CC Evidence={ECO:0000250|UniProtKB:P09211};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate +
CC glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)-
CC eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:132200, ChEBI:CHEBI:132201;
CC Evidence={ECO:0000250|UniProtKB:P09211};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261;
CC Evidence={ECO:0000250|UniProtKB:P09211};
CC -!- SUBUNIT: Homodimer. Interacts with CDK5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion
CC {ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino
CC acids function as un uncleaved transit peptide, and arginine residues
CC within it are crucial for mitochondrial localization. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Present in kidney, lung, testis and placenta, very
CC low levels in liver.
CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X02904; CAA26664.1; -; mRNA.
DR EMBL; L29427; AAB59718.1; -; Genomic_DNA.
DR EMBL; BC058439; AAH58439.1; -; mRNA.
DR EMBL; BC058440; AAH58440.1; -; mRNA.
DR PIR; A26546; XURTGP.
DR PIR; S59902; S59902.
DR RefSeq; NP_036709.1; NM_012577.2.
DR AlphaFoldDB; P04906; -.
DR SMR; P04906; -.
DR BioGRID; 246591; 1.
DR IntAct; P04906; 2.
DR STRING; 10116.ENSRNOP00000024601; -.
DR iPTMnet; P04906; -.
DR PhosphoSitePlus; P04906; -.
DR SwissPalm; P04906; -.
DR World-2DPAGE; 0004:P04906; -.
DR jPOST; P04906; -.
DR PaxDb; P04906; -.
DR PRIDE; P04906; -.
DR Ensembl; ENSRNOT00000024601; ENSRNOP00000024601; ENSRNOG00000018237.
DR GeneID; 24426; -.
DR KEGG; rno:24426; -.
DR UCSC; RGD:2758; rat.
DR CTD; 2950; -.
DR RGD; 2758; Gstp1.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000162460; -.
DR HOGENOM; CLU_039475_2_1_1; -.
DR InParanoid; P04906; -.
DR OMA; IKPKMIF; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P04906; -.
DR TreeFam; TF105321; -.
DR Reactome; R-RNO-156590; Glutathione conjugation.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR PRO; PR:P04906; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018237; Expressed in kidney and 20 other tissues.
DR ExpressionAtlas; P04906; baseline and differential.
DR Genevisible; P04906; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISS:BHF-UCL.
DR GO; GO:0097057; C:TRAF2-GSTP1 complex; ISO:RGD.
DR GO; GO:0035731; F:dinitrosyl-iron complex binding; ISO:RGD.
DR GO; GO:0005504; F:fatty acid binding; ISO:RGD.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISO:RGD.
DR GO; GO:0004364; F:glutathione transferase activity; ISO:RGD.
DR GO; GO:0008432; F:JUN kinase binding; ISS:BHF-UCL.
DR GO; GO:0019207; F:kinase regulator activity; ISS:BHF-UCL.
DR GO; GO:0097159; F:organic cyclic compound binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0035730; F:S-nitrosoglutathione binding; ISO:RGD.
DR GO; GO:0015643; F:toxic substance binding; IPI:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0071460; P:cellular response to cell-matrix adhesion; IEP:RGD.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEP:RGD.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEP:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:BHF-UCL.
DR GO; GO:0035726; P:common myeloid progenitor cell proliferation; ISS:BHF-UCL.
DR GO; GO:1901687; P:glutathione derivative biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:RGD.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043651; P:linoleic acid metabolic process; ISO:RGD.
DR GO; GO:0009890; P:negative regulation of biosynthetic process; ISO:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:BHF-UCL.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:BHF-UCL.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISS:BHF-UCL.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; ISS:BHF-UCL.
DR GO; GO:0070664; P:negative regulation of leukocyte proliferation; ISS:BHF-UCL.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; ISS:BHF-UCL.
DR GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; ISS:BHF-UCL.
DR GO; GO:2000469; P:negative regulation of peroxidase activity; ISO:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:RGD.
DR GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; IMP:RGD.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISS:BHF-UCL.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:BHF-UCL.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0014003; P:oligodendrocyte development; IEP:RGD.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:BHF-UCL.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; ISS:BHF-UCL.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0033591; P:response to L-ascorbic acid; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0000302; P:response to reactive oxygen species; ISS:BHF-UCL.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003082; GST_pi.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01268; GSTRNSFRASEP.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Lipid metabolism;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3359441,
FT ECO:0000269|PubMed:3864155, ECO:0000269|Ref.5"
FT CHAIN 2..210
FT /note="Glutathione S-transferase P"
FT /id="PRO_0000185907"
FT DOMAIN 2..81
FT /note="GST N-terminal"
FT DOMAIN 83..204
FT /note="GST C-terminal"
FT BINDING 8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 14
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 39
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 45
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 52..53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 65..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT MOD_RES 4
FT /note="Phosphotyrosine; by EGFR"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19157"
FT MOD_RES 116
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19157"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT CONFLICT 15
FT /note="C -> Y (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
