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 27-MAR-2024, entry version 188. 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. Negatively regulates 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 GlyGen; P04906; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P04906; -. DR PhosphoSitePlus; P04906; -. DR SwissPalm; P04906; -. DR jPOST; P04906; -. DR PaxDb; 10116-ENSRNOP00000024601; -. DR Ensembl; ENSRNOT00000024601.5; ENSRNOP00000024601.4; ENSRNOG00000018237.5. DR GeneID; 24426; -. DR KEGG; rno:24426; -. DR UCSC; RGD:2758; rat. DR AGR; RGD:2758; -. 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; 5302341at2759; -. 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 cell types or tissues. DR ExpressionAtlas; P04906; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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:0043124; P:negative regulation of canonical NF-kappaB signal transduction; ISS:BHF-UCL. 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: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: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: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 CDD; cd03210; GST_C_Pi; 1. DR CDD; cd03076; GST_N_Pi; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. 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 PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1. DR PANTHER; PTHR11571:SF266; GLUTATHIONE S-TRANSFERASE P 1-RELATED; 1. DR Pfam; PF14497; GST_C_3; 1. DR Pfam; PF02798; GST_N; 1. DR PRINTS; PR01268; GSTRNSFRASEP. DR SFLD; SFLDG01205; AMPS.1; 1. DR SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. DR World-2DPAGE; 0004:P04906; -. DR Genevisible; P04906; RN. 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 //