GSTP1_PIG
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 03-AUG-2022, entry version 134.
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. 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 -!- 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 PaxDb; P80031; -.
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 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:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
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 Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01268; GSTRNSFRASEP.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
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 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
