ID   GSTP1_PIG               Reviewed;         207 AA.
AC   P80031;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   24-JAN-2024, entry version 140.
DE   RecName: Full=Glutathione S-transferase P {ECO:0000305};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P09211};
DE   AltName: Full=GST P1-1;
DE   AltName: Full=GST class-pi;
GN   Name=GSTP1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Lung;
RX   PubMed=2013291; DOI=10.1111/j.1432-1033.1991.tb15867.x;
RA   Dirr H.W., Mann K., Huber R., Ladenstein R., Reinemer P.;
RT   "Class pi glutathione S-transferase from pig lung. Purification,
RT   biochemical characterization, primary structure and crystallization.";
RL   Eur. J. Biochem. 196:693-698(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-15.
RC   TISSUE=Lens;
RX   PubMed=2039535; DOI=10.1016/0006-291x(91)90376-i;
RA   Nishinaka T., Fujioka M., Nanjo H., Nishikawa J., Mizoguchi T., Terada T.,
RA   Nishihara T.;
RT   "Pig lens glutathione S-transferase belongs to class Pi enzyme.";
RL   Biochem. Biophys. Res. Commun. 176:966-971(1991).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE
RP   SULFONATE, AND SUBUNIT.
RX   PubMed=2065650; DOI=10.1002/j.1460-2075.1991.tb07729.x;
RA   Reinemer P., Dirr H.W., Ladenstein R., Schaeffer J., Gallay O., Huber R.;
RT   "The three-dimensional structure of class pi glutathione S-transferase in
RT   complex with glutathione sulfonate at 2.3-A resolution.";
RL   EMBO J. 10:1997-2005(1991).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, AND
RP   SUBUNIT.
RX   PubMed=7932743; DOI=10.1006/jmbi.1994.1631;
RA   Dirr H.W., Reinemer P., Huber R.;
RT   "Refined crystal structure of porcine class Pi glutathione S-transferase
RT   (pGST P1-1) at 2.1-A resolution.";
RL   J. Mol. Biol. 243:72-92(1994).
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   -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000305}.
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DR   PIR; S13780; S13780.
DR   PDB; 2GSR; X-ray; 2.11 A; A/B=1-206.
DR   PDBsum; 2GSR; -.
DR   AlphaFoldDB; P80031; -.
DR   SMR; P80031; -.
DR   STRING; 9823.ENSSSCP00000013714; -.
DR   PaxDb; 9823-ENSSSCP00000013714; -.
DR   PeptideAtlas; P80031; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   InParanoid; P80031; -.
DR   BRENDA; 2.5.1.18; 6170.
DR   SABIO-RK; P80031; -.
DR   EvolutionaryTrace; P80031; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
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:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR   GO; GO:1901687; P:glutathione derivative biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0051122; P:hepoxilin biosynthetic process; 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   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; 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; 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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Lipid metabolism; Mitochondrion; Nucleus; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..207
FT                   /note="Glutathione S-transferase P"
FT                   /id="PRO_0000185905"
FT   DOMAIN          1..78
FT                   /note="GST N-terminal"
FT   DOMAIN          80..201
FT                   /note="GST C-terminal"
FT   BINDING         7
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:7932743"
FT   BINDING         13
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:7932743"
FT   BINDING         38
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:7932743"
FT   BINDING         42
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:7932743"
FT   BINDING         49..50
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:7932743"
FT   BINDING         62..63
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000269|PubMed:7932743"
FT   MOD_RES         3
FT                   /note="Phosphotyrosine; by EGFR"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   MOD_RES         59
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   MOD_RES         100
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19157"
FT   MOD_RES         113
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19157"
FT   MOD_RES         125
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09211"
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   TURN            12..14
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   HELIX           15..23
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   STRAND          29..32
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   HELIX           38..41
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   STRAND          52..55
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   HELIX           63..74
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   HELIX           81..107
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   HELIX           109..132
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   HELIX           135..137
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   STRAND          141..145
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   HELIX           148..163
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   HELIX           167..170
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   HELIX           172..182
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   HELIX           185..192
FT                   /evidence="ECO:0007829|PDB:2GSR"
FT   HELIX           194..197
FT                   /evidence="ECO:0007829|PDB:2GSR"
SQ   SEQUENCE   207 AA;  23497 MW;  2B638B60504BF4A0 CRC64;
     PPYTITYFPV RGRCEAMRML LADQDQSWKE EVVTMETWPP LKPSCLFRQL PKFQDGDLTL
     YQSNAILRHL GRSFGLYGKD QKEAALVDMV NDGVEDLRCK YATLIYTNYE AGKEKYVKEL
     PEHLKPFETL LSQNQGGQAF VVGSQISFAD YNLLDLLRIH QVLNPSCLDA FPLLSAYVAR
     LSARPKIKAF LASPEHVNRP INGNGKN
//