GSTP1_XENLA
ID GSTP1_XENLA Reviewed; 212 AA.
AC Q8JFZ2; Q6NTV0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Glutathione S-transferase P 1 {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P09211};
DE AltName: Full=GST class-pi;
DE Short=GST-Pi;
DE AltName: Full=XlGSTP1-1;
GN Name=gstp1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAD33920.1}
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF PHE-111 AND PRO-208.
RC TISSUE=Liver tumor {ECO:0000269|PubMed:12710888};
RX PubMed=12710888; DOI=10.1042/bj20030261;
RA De Luca A., Favaloro B., Carletti E., Sacchetta P., Di Ilio C.;
RT "A novel amphibian Pi-class glutathione transferase isoenzyme from Xenopus
RT laevis: importance of phenylalanine 111 in the H-site.";
RL Biochem. J. 373:539-545(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH68854.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-212.
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH68854.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Highly active
CC towards 1-chloro-2,4-dinitrobenzene and organic isothiocyanates, but
CC shows no detectable activity towards 1,2-dichloro-4-nitrobenzene, p-
CC nitrobenzylchloride, trans-4-phenyl-3-buten-2-one (tPBO) and ethacrynic
CC acid. May be associated with cellular proliferation.
CC {ECO:0000269|PubMed:12710888, ECO:0000303|PubMed:12710888}.
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:0000269|PubMed:12710888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000305};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P83325}.
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 -!- TISSUE SPECIFICITY: Expressed only in embryos. Not expressed in liver,
CC lung, heart, kidney and ovary. {ECO:0000269|PubMed:12710888}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos at stages 11-15, but not
CC detected in unfertilized eggs. {ECO:0000269|PubMed:12710888}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Pi family. {ECO:0000255}.
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DR EMBL; AJ489617; CAD33920.1; -; mRNA.
DR EMBL; BC068854; AAH68854.1; -; mRNA.
DR RefSeq; NP_001082252.1; NM_001088783.1.
DR AlphaFoldDB; Q8JFZ2; -.
DR SMR; Q8JFZ2; -.
DR GeneID; 398321; -.
DR KEGG; xla:398321; -.
DR CTD; 398321; -.
DR Xenbase; XB-GENE-5846294; gstp1.L.
DR OrthoDB; 1162336at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 398321; Expressed in zone of skin and 12 other tissues.
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; IDA:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
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 Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01268; GSTRNSFRASEP.
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 Cytoplasm; Mitochondrion; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..212
FT /note="Glutathione S-transferase P 1"
FT /id="PRO_0000185910"
FT DOMAIN 2..83
FT /note="GST N-terminal"
FT DOMAIN 85..206
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 47
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P09211"
FT MUTAGEN 111
FT /note="F->Y: Reduction in activity and altered substrate
FT specificity; inactive towards 4-nitroquinoline-1-oxide,
FT active towards ethacrynic acid and tPBO."
FT /evidence="ECO:0000269|PubMed:12710888"
FT MUTAGEN 208
FT /note="P->G,H: Reduction in activity."
FT /evidence="ECO:0000269|PubMed:12710888"
FT CONFLICT 203
FT /note="K -> R (in Ref. 2; AAH68854)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 24428 MW; E5BF0166C08CC5BA CRC64;
MPGYVLTYFP VRGRAEPIRL LLADQGISWK EDEVQIPDWF SGKDARKKEA VFGQLPQFQD
GDYVLYQSNS ILRYLGNKHG LTGANDEERG HIDMVNDGVE DLRQKYGRLI FFEYETGKDK
YLKELPSQLD FFERILSKNA NGSKFVVGQK ISFADYNLLD ILQCHLDLCS KSLSAYPLLT
AYVERLVARP KISEYLKSDA RNKRPITPKH KK
