ID GSTP1_CAPHI Reviewed; 210 AA. AC Q9TTY8; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 100. 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 Capra hircus (Goat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Caprinae; Capra. OX NCBI_TaxID=9925; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Testis; RA Hemchand T., Shaha C.; RT "Complementary DNA sequence (632 b.p.) of goat germ cell glutathione S- RT transferase Pi."; RL Submitted (SEP-1999) 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; AF186248; AAF01323.1; -; mRNA. DR AlphaFoldDB; Q9TTY8; -. DR SMR; Q9TTY8; -. DR STRING; 9925.ENSCHIP00000012372; -. DR Proteomes; UP000291000; Unassembled WGS sequence. DR Proteomes; UP000694566; Unplaced. DR Proteomes; UP000694900; Genome assembly. 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; 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; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 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_0000185897" 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; 23630 MW; BDA49F961FA69DBA CRC64; MASYTIVYFP VQGRCEAMRM LLADQDQSWK EEVVAMQSWL QGPLKASCLY GQLPKFQDGD LTLYQSNAIL RHLGRTLGLY GKDQREAALV DMVNDGVEDL RCKYVSLIYT NYQAGKEDYV KALPQHLKPF ETLLSQNKGG QAFIVGDQIS FADYNLLDLL RIHQVLAPSC LDSFPLLSAY VARLNSRPKL KAFLASPEHV NRPINGNGKQ //