ID GSTP1_PONAB Reviewed; 210 AA. AC Q5R8R5; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 114. 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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Heart; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. 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. {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR859686; CAH91845.1; -; mRNA. DR RefSeq; NP_001127471.1; NM_001133999.1. DR AlphaFoldDB; Q5R8R5; -. DR SMR; Q5R8R5; -. DR STRING; 9601.ENSPPYP00000003460; -. DR Ensembl; ENSPPYT00000003583.3; ENSPPYP00000003460.3; ENSPPYG00000002985.3. DR GeneID; 100174544; -. DR KEGG; pon:100174544; -. DR CTD; 2950; -. DR eggNOG; KOG1695; Eukaryota. DR GeneTree; ENSGT00940000162460; -. DR HOGENOM; CLU_860419_0_0_1; -. DR InParanoid; Q5R8R5; -. DR OMA; IKPKMIF; -. DR OrthoDB; 5302341at2759; -. DR Proteomes; UP000001595; Chromosome 11. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0097057; C:TRAF2-GSTP1 complex; IEA:Ensembl. DR GO; GO:0035731; F:dinitrosyl-iron complex binding; IEA:Ensembl. DR GO; GO:0005504; F:fatty acid binding; IEA:Ensembl. DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:Ensembl. DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB. DR GO; GO:0035730; F:S-nitrosoglutathione binding; IEA:Ensembl. DR GO; GO:1901687; P:glutathione derivative biosynthetic process; ISS:UniProtKB. DR GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl. DR GO; GO:0051122; P:hepoxilin biosynthetic process; ISS:UniProtKB. DR GO; GO:0043651; P:linoleic acid metabolic process; IEA:Ensembl. DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IEA:Ensembl. DR GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IEA:Ensembl. DR GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; IEA:Ensembl. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl. DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB. DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl. 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:SF141; GLUTATHIONE S-TRANSFERASE P; 1. DR Pfam; PF00043; GST_C; 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 2: Evidence at transcript level; KW Acetylation; Cytoplasm; Lipid metabolism; Mitochondrion; Nucleus; KW Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1..210 FT /note="Glutathione S-transferase P" FT /id="PRO_0000185906" 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" SQ SEQUENCE 210 AA; 23390 MW; 56337AEA78462CEB CRC64; MPPYTVVYFP VRGRCAALRM LLADQGQSWK EEVVSMETWQ EGSLKASCLY GQLPKFQDGD LTLYQSNTIL RHLGRTLGLY GKDQREAALV DMVNDGVEDL RCKYLSLIYT NYEAGKDDYV KALPGQLKPF ETLLSQNQGG KTFIVGDQIS FADYNLLDLL LIHEVLAPGC LDAFPLLSAY VARLSARPKL KAFLASPEHV NLPINGNGKQ //