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   27-MAR-2024, entry version 93.
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   AGR; Xenbase:XB-GENE-5846294; -.
DR   CTD; 398321; -.
DR   Xenbase; XB-GENE-5846294; gstp1.L.
DR   OrthoDB; 5302341at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 398321; Expressed in zone of skin and 12 other cell types or 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   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:SF141; 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   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
//