GSTA1_PIG
ID GSTA1_PIG Reviewed; 222 AA.
AC P51781;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Glutathione S-transferase alpha M14;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P08263};
DE AltName: Full=GST class-alpha;
DE Contains:
DE RecName: Full=Glutathione S-transferase alpha M14, N-terminally processed;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA Hatey F., Tosser G.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glutathione S-transferase that catalyzes the nucleophilic
CC attack of the sulfur atom of glutathione on the electrophilic groups of
CC a wide range of exogenous and endogenous compounds. Involved in the
CC formation of glutathione conjugates of both prostaglandin A2 (PGA2) and
CC prostaglandin J2 (PGJ2). It also catalyzes the isomerization of D5-
CC androstene-3,17-dione (AD) into D4-androstene-3,17-dione and may
CC therefore play an important role in hormone biosynthesis. Through its
CC glutathione-dependent peroxidase activity toward the fatty acid
CC hydroperoxide (13S)-hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE it
CC is also involved in the metabolism of oxidized linoleic acid.
CC {ECO:0000250|UniProtKB:P08263}.
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:P08263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + prostaglandin A2 = prostaglandin A2-S-(R)-
CC glutathione; Xref=Rhea:RHEA:50796, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:133370, ChEBI:CHEBI:133768;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50797;
CC Evidence={ECO:0000250|UniProtKB:P08263};
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:P08263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50805;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione =
CC (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide +
CC H2O; Xref=Rhea:RHEA:48888, ChEBI:CHEBI:15377, ChEBI:CHEBI:57466,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90850;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48889;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=androst-5-ene-3,17-dione = androst-4-ene-3,17-dione;
CC Xref=Rhea:RHEA:43936, ChEBI:CHEBI:16422, ChEBI:CHEBI:83865;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43937;
CC Evidence={ECO:0000250|UniProtKB:P08263};
CC -!- SUBUNIT: Homodimer or heterodimer of GSTA1 and GSTA2.
CC {ECO:0000250|UniProtKB:P08263}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {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; Z69585; CAA93433.1; -; mRNA.
DR RefSeq; NP_999554.1; NM_214389.1.
DR AlphaFoldDB; P51781; -.
DR SMR; P51781; -.
DR STRING; 9823.ENSSSCP00000002831; -.
DR PaxDb; P51781; -.
DR PeptideAtlas; P51781; -.
DR GeneID; 397682; -.
DR KEGG; ssc:397682; -.
DR CTD; 2938; -.
DR eggNOG; KOG1695; Eukaryota.
DR OrthoDB; 1162336at2759; -.
DR BRENDA; 2.5.1.18; 6170.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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; IPR003080; GST_alpha.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01266; GSTRNSFRASEA.
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; Reference proteome; Transferase.
FT CHAIN 1..222
FT /note="Glutathione S-transferase alpha M14"
FT /id="PRO_0000421782"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT CHAIN 2..222
FT /note="Glutathione S-transferase alpha M14, N-terminally
FT processed"
FT /id="PRO_0000185797"
FT DOMAIN 3..83
FT /note="GST N-terminal"
FT DOMAIN 85..208
FT /note="GST C-terminal"
FT REGION 199..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 9
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P13745"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P30711"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P13745"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P80894"
FT MOD_RES 2
FT /note="N-acetylalanine; in Glutathione S-transferase alpha
FT M14, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT MOD_RES 4
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30115"
SQ SEQUENCE 222 AA; 25281 MW; 8AAF741EEC8DDD4B CRC64;
MAGKPILHYF NGRGRMECIR WLLAAAGVEF EEKFIKTPED LDKLTNDGSL LFQQVPMVEI
DGMKLVQTRA ILNYIATKYN LYGKDAKERA LIDMYTEGVA DLGEMILLLP LCPPNEKDAK
VASIKEKSTN RYLPAFEKVL KSHGQDYLVG NKLSRADIQL VELLYYVEEL DPSLLANFPL
LKALKTRVSN LPTVKKFLQP GSQRKPPMDA KKIRRSQEYF PD
