GSTP1_CRIMI
ID GSTP1_CRIMI Reviewed; 210 AA.
AC P47954;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 101.
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 Cricetulus migratorius (Gray dwarf hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10032;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=8809043; DOI=10.1042/bj3180533;
RA Swedmark S., Jernstroem B., Jenssen D.;
RT "Comparison of the mRNA sequences for Pi class glutathione transferases in
RT different hamster species and the corresponding enzyme activities with
RT anti-benzo[a]pyrene-7,8-dihydrodiol 9,10-epoxide.";
RL Biochem. J. 318:533-538(1996).
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 EMBL; L46796; AAB39861.1; -; mRNA.
DR PIR; S71957; S71957.
DR AlphaFoldDB; P47954; -.
DR SMR; P47954; -.
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; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Lipid metabolism; Mitochondrion; Nucleus;
KW Phosphoprotein; Transferase.
FT CHAIN 1..210
FT /note="Glutathione S-transferase P"
FT /id="PRO_0000185899"
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; 23469 MW; 8CF81AEF04779F61 CRC64;
MPPYTIVYFP VRGRCEAMRI LLADQGQSWK EEVITGETWG KGSLKSTCLY GQLPKFEDGD
LTLYQSNAIL RHLGRSLGLY GKDQREAALV DMVNDGVEDL RCKYVTLIYT KYEEGKDDYV
KALPGHLKPF ETLLSKNQGG KAFIVGDQIS FADYNLLDLL LIHQVLAPGC LDNFPLLSAY
VARLSARPKI KAFLSSPDHV NRPINGNGKQ
