ID   GSTP1_NOTMI             Reviewed;         210 AA.
AC   P47954;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 113.
DE   RecName: Full=Glutathione S-transferase P {ECO:0000305};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P09211};
DE   AltName: Full=GST class-pi;
GN   Name=GSTP1;
OS   Nothocricetulus migratorius (Gray dwarf hamster) (Cricetulus migratorius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Nothocricetulus.
OX   NCBI_TaxID=3122392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=8809043; DOI=10.1042/bj3180533;
RA   Swedmark S., Jernstroem B., Jenssen D.;
RT   "Comparison of the mRNA sequences for Pi class glutathione transferases in
RT   different hamster species and the corresponding enzyme activities with
RT   anti-benzo[a]pyrene-7,8-dihydrodiol 9,10-epoxide.";
RL   Biochem. J. 318:533-538(1996).
CC   -!- FUNCTION: Catalyzes conjugation of reduced glutathione to a wide number
CC       of 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. Acts as a negative regulator of ferroptosis by
CC       mediating glutathione conjugation and detoxification of 4-
CC       hydroxynonenal (4-HNE) reactive aldehyde. Negatively regulates CDK5
CC       activity via p25/p35 translocation to prevent neurodegeneration.
CC       {ECO:0000250|UniProtKB:P09211}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RX + glutathione = an S-substituted glutathione + a halide
CC         anion + 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=prostaglandin J2 + glutathione = 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=prostaglandin J2 + glutathione = 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=prostaglandin A2 + glutathione = 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-hydroxynon-2-enal + glutathione = 3-(glutathion-S-yl)-4-
CC         hydroxynonanal; Xref=Rhea:RHEA:85343, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:58968, ChEBI:CHEBI:234318;
CC         Evidence={ECO:0000250|UniProtKB:P09211};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:85344;
CC         Evidence={ECO:0000250|UniProtKB:P09211};
CC   -!- SUBUNIT: Homodimer. Interacts with CDK5 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P09211}.
CC       Mitochondrion {ECO:0000250|UniProtKB:P09211}. Nucleus
CC       {ECO:0000250|UniProtKB:P09211}. Note=The 83 N-terminal amino acids
CC       function as un uncleaved transit peptide, and arginine residues within
CC       it are crucial for mitochondrial localization.
CC       {ECO:0000250|UniProtKB:P09211}.
CC   -!- PTM: Ubiquitinated by SMURF2, leading to its degradation and initiation
CC       of ferroptosis. {ECO:0000250|UniProtKB:P09211}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}.
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DR   EMBL; L46796; AAB39861.1; -; mRNA.
DR   PIR; S71957; S71957.
DR   AlphaFoldDB; P47954; -.
DR   SMR; P47954; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:1901687; P:glutathione derivative biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:TreeGrafter.
DR   GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0110076; P:negative regulation of ferroptosis; ISS:UniProtKB.
DR   GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR   CDD; cd03210; GST_C_Pi; 1.
DR   CDD; cd03076; GST_N_Pi; 1.
DR   FunFam; 1.20.1050.10:FF:000047; Glutathione S-transferase P; 1.
DR   FunFam; 3.40.30.10:FF:000071; Glutathione S-transferase P; 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; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR003082; GST_pi.
DR   InterPro; IPR050213; GST_superfamily.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF255; GLUTATHIONE S-TRANSFERASE P; 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   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Lipid metabolism; Mitochondrion;
KW   Nucleus; Phosphoprotein; Transferase; Ubl conjugation.
FT   CHAIN           1..210
FT                   /note="Glutathione S-transferase P"
FT                   /id="PRO_0000185899"
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   CROSSLNK        55
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   CROSSLNK        121
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   CROSSLNK        191
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
SQ   SEQUENCE   210 AA;  23469 MW;  8CF81AEF04779F61 CRC64;
     MPPYTIVYFP VRGRCEAMRI LLADQGQSWK EEVITGETWG KGSLKSTCLY GQLPKFEDGD
     LTLYQSNAIL RHLGRSLGLY GKDQREAALV DMVNDGVEDL RCKYVTLIYT KYEEGKDDYV
     KALPGHLKPF ETLLSKNQGG KAFIVGDQIS FADYNLLDLL LIHQVLAPGC LDNFPLLSAY
     VARLSARPKI KAFLSSPDHV NRPINGNGKQ
//