ID   GSTP1_MOUSE             Reviewed;         210 AA.
AC   P19157; Q8BNY4;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 210.
DE   RecName: Full=Glutathione S-transferase P 1 {ECO:0000305};
DE            Short=Gst P1;
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P09211};
DE   AltName: Full=GST YF-YF;
DE   AltName: Full=GST class-pi;
DE   AltName: Full=GST-piB;
DE   AltName: Full=Preadipocyte growth factor;
GN   Name=Gstp1 {ECO:0000312|MGI:MGI:95865}; Synonyms=Gstpib;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RX   PubMed=2388840; DOI=10.1093/nar/18.15.4606;
RA   Hatayama I., Satoh K., Sato K.;
RT   "A cDNA sequence coding a class pi glutathione S-transferase of mouse.";
RL   Nucleic Acids Res. 18:4606-4606(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8135745; DOI=10.1042/bj2980385;
RA   Bammler T.K., Smith C.A.D., Wolf R.C.;
RT   "Isolation and characterization of two mouse PI class glutathione S-
RT   transferase genes.";
RL   Biochem. J. 298:385-390(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ; TISSUE=Liver;
RX   PubMed=7982937; DOI=10.1016/s0021-9258(18)43807-0;
RA   Xu X., Stambrook P.J.;
RT   "Two murine GSTpi genes are arranged in tandem and are differentially
RT   expressed.";
RL   J. Biol. Chem. 269:30268-30273(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kawada T., Aoki N., Kamei Y., Sugimoto E.;
RT   "Molecular cloning of mouse preadipocyte growth factor.";
RL   Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   PROTEIN SEQUENCE OF 2-12; 56-71; 122-141 AND 192-209, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-210.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   CHARACTERIZATION, AND MASS SPECTROMETRY.
RC   STRAIN=CD-1; TISSUE=Liver;
RX   PubMed=8605288; DOI=10.1021/tx00050a009;
RA   Mitchell A.E., Morin D., Lame M.W., Jones A.D.;
RT   "Purification, mass spectrometric characterization, and covalent
RT   modification of murine glutathione S-transferases.";
RL   Chem. Res. Toxicol. 8:1054-1062(1995).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [10]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-103 AND LYS-116, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOGS.
RX   PubMed=8145243; DOI=10.1006/jmbi.1994.1232;
RA   Garcia-Saez I., Parraga A., Phillips M.F., Mantle T.J., Coll M.;
RT   "Molecular structure at 1.8 A of mouse liver class pi glutathione S-
RT   transferase complexed with S-(p-nitrobenzyl)glutathione and other
RT   inhibitors.";
RL   J. Mol. Biol. 237:298-314(1994).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=9446594; DOI=10.1074/jbc.273.5.2844;
RA   Vega M.C., Walsh S.B., Mantle T.J., Coll M.;
RT   "The three-dimensional structure of Cys-47-modified mouse liver glutathione
RT   S-transferase P1-1. Carboxymethylation dramatically decreases the affinity
RT   for glutathione and is associated with a loss of electron density in the
RT   alphaB-310B region.";
RL   J. Biol. Chem. 273:2844-2850(1998).
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: Ubiquitously expressed.
CC   -!- MASS SPECTROMETRY: Mass=23478.8; Mass_error=2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8605288};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}.
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DR   EMBL; X53451; CAA37529.1; -; mRNA.
DR   EMBL; X76143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U15654; AAA64837.1; -; Genomic_DNA.
DR   EMBL; D30687; BAA06349.1; -; mRNA.
DR   EMBL; BC002048; AAH02048.1; -; mRNA.
DR   EMBL; BC061109; AAH61109.1; -; mRNA.
DR   EMBL; AK079144; BAC37560.1; -; mRNA.
DR   CCDS; CCDS29411.1; -.
DR   PIR; S12709; B55140.
DR   RefSeq; NP_038569.1; NM_013541.1.
DR   PDB; 1BAY; X-ray; 2.00 A; A/B=2-210.
DR   PDB; 1GLP; X-ray; 1.90 A; A/B=2-210.
DR   PDB; 1GLQ; X-ray; 1.80 A; A/B=2-210.
DR   PDB; 1GSY; X-ray; 2.44 A; A/B=2-210.
DR   PDB; 1GTI; X-ray; 3.00 A; A/B/C/D/E/F=2-210.
DR   PDB; 2GLR; X-ray; 2.20 A; A/B=2-210.
DR   PDB; 2OA7; X-ray; 2.20 A; A/B=2-210.
DR   PDB; 2OAC; X-ray; 2.20 A; A/B=2-210.
DR   PDB; 2OAD; X-ray; 2.50 A; A/B=2-210.
DR   PDB; 3O76; X-ray; 1.77 A; A/B=2-210.
DR   PDB; 8C5D; X-ray; 1.28 A; A/B=1-210.
DR   PDBsum; 1BAY; -.
DR   PDBsum; 1GLP; -.
DR   PDBsum; 1GLQ; -.
DR   PDBsum; 1GSY; -.
DR   PDBsum; 1GTI; -.
DR   PDBsum; 2GLR; -.
DR   PDBsum; 2OA7; -.
DR   PDBsum; 2OAC; -.
DR   PDBsum; 2OAD; -.
DR   PDBsum; 3O76; -.
DR   PDBsum; 8C5D; -.
DR   AlphaFoldDB; P19157; -.
DR   SMR; P19157; -.
DR   BioGRID; 200101; 13.
DR   IntAct; P19157; 5.
DR   MINT; P19157; -.
DR   STRING; 10090.ENSMUSP00000129565; -.
DR   iPTMnet; P19157; -.
DR   PhosphoSitePlus; P19157; -.
DR   SwissPalm; P19157; -.
DR   REPRODUCTION-2DPAGE; P19157; -.
DR   EPD; P19157; -.
DR   jPOST; P19157; -.
DR   MaxQB; P19157; -.
DR   PaxDb; 10090-ENSMUSP00000129565; -.
DR   PeptideAtlas; P19157; -.
DR   ProteomicsDB; 271107; -.
DR   Pumba; P19157; -.
DR   TopDownProteomics; P19157; -.
DR   DNASU; 14870; -.
DR   Ensembl; ENSMUST00000169613.4; ENSMUSP00000129565.2; ENSMUSG00000060803.7.
DR   GeneID; 14870; -.
DR   KEGG; mmu:14870; -.
DR   UCSC; uc008fyf.1; mouse.
DR   AGR; MGI:95865; -.
DR   CTD; 2950; -.
DR   MGI; MGI:95865; Gstp1.
DR   VEuPathDB; HostDB:ENSMUSG00000060803; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000162460; -.
DR   HOGENOM; CLU_039475_2_1_1; -.
DR   InParanoid; P19157; -.
DR   OMA; IKPKMIF; -.
DR   OrthoDB; 5302341at2759; -.
DR   PhylomeDB; P19157; -.
DR   TreeFam; TF105321; -.
DR   BRENDA; 2.5.1.18; 3474.
DR   Reactome; R-MMU-156590; Glutathione conjugation.
DR   Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-9753281; Paracetamol ADME.
DR   BioGRID-ORCS; 14870; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Gstp1; mouse.
DR   EvolutionaryTrace; P19157; -.
DR   PRO; PR:P19157; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P19157; Protein.
DR   Bgee; ENSMUSG00000060803; Expressed in hepatobiliary system and 99 other cell types or tissues.
DR   ExpressionAtlas; P19157; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR   GO; GO:0032991; C:protein-containing complex; IDA:BHF-UCL.
DR   GO; GO:0097057; C:TRAF2-GSTP1 complex; ISO:MGI.
DR   GO; GO:0035731; F:dinitrosyl-iron complex binding; ISO:MGI.
DR   GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR   GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:MGI.
DR   GO; GO:0008432; F:JUN kinase binding; IPI:BHF-UCL.
DR   GO; GO:0019207; F:kinase regulator activity; IMP:BHF-UCL.
DR   GO; GO:0097159; F:organic cyclic compound binding; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0035730; F:S-nitrosoglutathione binding; ISO:MGI.
DR   GO; GO:0015643; F:toxic substance binding; ISO:MGI.
DR   GO; GO:0031100; P:animal organ regeneration; ISS:BHF-UCL.
DR   GO; GO:0071460; P:cellular response to cell-matrix adhesion; ISS:BHF-UCL.
DR   GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:BHF-UCL.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:BHF-UCL.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISS:BHF-UCL.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:BHF-UCL.
DR   GO; GO:0035726; P:common myeloid progenitor cell proliferation; IMP:BHF-UCL.
DR   GO; GO:1901687; P:glutathione derivative biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; IDA:MGI.
DR   GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0043651; P:linoleic acid metabolic process; ISO:MGI.
DR   GO; GO:0002674; P:negative regulation of acute inflammatory response; NAS:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; TAS:BHF-UCL.
DR   GO; GO:0009890; P:negative regulation of biosynthetic process; ISO:MGI.
DR   GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IDA:BHF-UCL.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IDA:BHF-UCL.
DR   GO; GO:0043508; P:negative regulation of JUN kinase activity; IDA:BHF-UCL.
DR   GO; GO:0070664; P:negative regulation of leukocyte proliferation; IMP:BHF-UCL.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:BHF-UCL.
DR   GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IDA:BHF-UCL.
DR   GO; GO:2000429; P:negative regulation of neutrophil aggregation; NAS:BHF-UCL.
DR   GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:2000469; P:negative regulation of peroxidase activity; IDA:BHF-UCL.
DR   GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; ISO:MGI.
DR   GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IDA:BHF-UCL.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
DR   GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0014003; P:oligodendrocyte development; ISS:BHF-UCL.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:BHF-UCL.
DR   GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR   GO; GO:0032872; P:regulation of stress-activated MAPK cascade; IDA:BHF-UCL.
DR   GO; GO:0043200; P:response to amino acid; ISS:BHF-UCL.
DR   GO; GO:0032355; P:response to estradiol; ISS:BHF-UCL.
DR   GO; GO:0045471; P:response to ethanol; ISS:BHF-UCL.
DR   GO; GO:0033591; P:response to L-ascorbic acid; ISS:BHF-UCL.
DR   GO; GO:0031667; P:response to nutrient levels; ISS:BHF-UCL.
DR   GO; GO:0000302; P:response to reactive oxygen species; IDA:BHF-UCL.
DR   GO; GO:0009636; P:response to toxic substance; ISS:BHF-UCL.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
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   SWISS-2DPAGE; P19157; -.
DR   Genevisible; P19157; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Lipid metabolism; Mitochondrion; Nucleus; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.6"
FT   CHAIN           2..210
FT                   /note="Glutathione S-transferase P 1"
FT                   /id="PRO_0000185903"
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:0000305|PubMed:8145243"
FT   BINDING         14
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:8145243"
FT   BINDING         39
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:8145243"
FT   BINDING         45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:8145243"
FT   BINDING         52..53
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:8145243"
FT   BINDING         65..66
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:8145243"
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:0007744|PubMed:23806337"
FT   MOD_RES         116
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         128
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   HELIX           16..24
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   HELIX           36..40
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:1GLQ"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:1GTI"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   STRAND          61..65
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   HELIX           66..77
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   HELIX           84..110
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   HELIX           112..135
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   STRAND          144..148
FT                   /evidence="ECO:0007829|PDB:1GLQ"
FT   HELIX           151..166
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   TURN            168..173
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   HELIX           175..186
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   HELIX           188..195
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   HELIX           197..200
FT                   /evidence="ECO:0007829|PDB:3O76"
FT   STRAND          204..208
FT                   /evidence="ECO:0007829|PDB:3O76"
SQ   SEQUENCE   210 AA;  23609 MW;  DAC7762F4E34FF27 CRC64;
     MPPYTIVYFP VRGRCEAMRM LLADQGQSWK EEVVTIDTWM QGLLKPTCLY GQLPKFEDGD
     LTLYQSNAIL RHLGRSLGLY GKNQREAAQM DMVNDGVEDL RGKYVTLIYT NYENGKNDYV
     KALPGHLKPF ETLLSQNQGG KAFIVGDQIS FADYNLLDLL LIHQVLAPGC LDNFPLLSAY
     VARLSARPKI KAFLSSPEHV NRPINGNGKQ
//