| IED ID | IndEnz0018000469 |
| Enzyme Type ID | peroxidase000469 |
| Protein Name |
Glutathione S-transferase P EC 2.5.1.18 Chain 7 GST 7-7 GST class-pi |
| Gene Name | Gstp1 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MPPYTIVYFPVRGRCEATRMLLADQGQSWKEEVVTIDVWLQGSLKSTCLYGQLPKFEDGDLTLYQSNAILRHLGRSLGLYGKDQKEAALVDMVNDGVEDLRCKYGTLIYTNYENGKDDYVKALPGHLKPFETLLSQNQGGKAFIVGNQISFADYNLLDLLLVHQVLAPGCLDNFPLLSAYVARLSARPKIKAFLSSPDHLNRPINGNGKQ |
| Enzyme Length | 210 |
| Uniprot Accession Number | P04906 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 8; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:P09211; BINDING 14; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:P09211; BINDING 39; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:P09211; BINDING 45; /note=Glutathione; /evidence=ECO:0000250|UniProtKB:P09211 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P09211};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438; Evidence={ECO:0000250|UniProtKB:P09211}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(R)-glutathione; Xref=Rhea:RHEA:50804, ChEBI:CHEBI:57925, ChEBI:CHEBI:133396, ChEBI:CHEBI:133771; Evidence={ECO:0000250|UniProtKB:P09211};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805; Evidence={ECO:0000250|UniProtKB:P09211}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin J2 = prostaglandin J2-S-(S)-glutathione; Xref=Rhea:RHEA:50808, ChEBI:CHEBI:57925, ChEBI:CHEBI:133396, ChEBI:CHEBI:133772; Evidence={ECO:0000250|UniProtKB:P09211};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50809; Evidence={ECO:0000250|UniProtKB:P09211}; CATALYTIC ACTIVITY: Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(S)-glutathione; Xref=Rhea:RHEA:50800, ChEBI:CHEBI:57925, ChEBI:CHEBI:133370, ChEBI:CHEBI:133769; Evidence={ECO:0000250|UniProtKB:P09211};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50801; Evidence={ECO:0000250|UniProtKB:P09211}; CATALYTIC ACTIVITY: Reaction=11(S)-hydroxy-14(S),15(S)-epoxy-(5Z,8Z,12E)-eicosatrienoate + glutathione = (11S,15S)-dihydroxy-14(R)-S-glutathionyl-(5Z,8Z,12E)-eicosatrienoate; Xref=Rhea:RHEA:50260, ChEBI:CHEBI:57925, ChEBI:CHEBI:132200, ChEBI:CHEBI:132201; Evidence={ECO:0000250|UniProtKB:P09211};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50261; Evidence={ECO:0000250|UniProtKB:P09211}; |
| DNA Binding | |
| EC Number | 2.5.1.18 |
| Enzyme Function | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration. {ECO:0000250|UniProtKB:P09211}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Binding site (4); Chain (1); Domain (2); Initiator methionine (1); Modified residue (5); Region (2); Sequence conflict (1) |
| Keywords | Acetylation;Cytoplasm;Direct protein sequencing;Lipid metabolism;Mitochondrion;Nucleus;Phosphoprotein;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization. {ECO:0000250}. |
| Modified Residue | MOD_RES 4; /note=Phosphotyrosine; by EGFR; /evidence=ECO:0000250|UniProtKB:P09211; MOD_RES 62; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P09211; MOD_RES 103; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P19157; MOD_RES 116; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:P19157; MOD_RES 128; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P09211 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10793289; 11018474; 12011483; 12016164; 15809768; 15863507; 15867277; 15942958; 16242832; 16317157; 16396496; 16407263; 16645134; 16728343; 16728344; 17596925; 17681700; 17786572; 18081878; 18349876; 1908848; 19790251; 20013880; 20091025; 20423715; 21092749; 21213404; 21668448; 22038365; 2206462; 22272023; 22576464; 23741294; 23960717; 23981577; 24205794; 24312188; 24321768; 24412522; 24474500; 25164943; 25419570; 25974399; 29501922; 3421895; 7499462; 9505896; 9834927; |
| Motif | |
| Gene Encoded By | |
| Mass | 23,439 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:16437; RHEA:16438; RHEA:50804; RHEA:50805; RHEA:50808; RHEA:50809; RHEA:50800; RHEA:50801; RHEA:50260; RHEA:50261 |
| Cross Reference Brenda |