GSTA1_BOVIN
ID GSTA1_BOVIN Reviewed; 222 AA.
AC Q28035; Q3T072;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Glutathione S-transferase A1 {ECO:0000305};
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P08263};
DE AltName: Full=13-hydroperoxyoctadecadienoate peroxidase {ECO:0000250|UniProtKB:P08263};
DE EC=1.11.1.- {ECO:0000250|UniProtKB:P08263};
DE AltName: Full=Androst-5-ene-3,17-dione isomerase {ECO:0000250|UniProtKB:P08263};
DE EC=5.3.3.- {ECO:0000250|UniProtKB:P08263};
DE AltName: Full=GST class-alpha member 1;
DE AltName: Full=Glutathione S-transferase alpha-1;
DE Contains:
DE RecName: Full=Glutathione S-transferase A1, N-terminally processed;
GN Name=GSTA1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein; TISSUE=Corpus luteum;
RX PubMed=10433206; DOI=10.1210/endo.140.8.6886;
RA Rabahi F., Brule S., Sirois J., Beckers J.-F.M.P., Silversides D.W.,
RA Lussier J.G.;
RT "High expression of bovine alpha glutathione S-transferase (GSTA1, GSTA2)
RT subunits is mainly associated with steroidogenically active cells and
RT regulated by gonadotropins in bovine ovarian follicles.";
RL Endocrinology 140:3507-3517(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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 -!- TISSUE SPECIFICITY: Expressed in corpus luteum, adrenal gland, testis,
CC liver, lung, thyroid and kidney.
CC -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC {ECO:0000305}.
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DR EMBL; U49179; AAB72239.1; -; mRNA.
DR EMBL; BC102540; AAI02541.1; -; mRNA.
DR RefSeq; NP_001071617.1; NM_001078149.1.
DR AlphaFoldDB; Q28035; -.
DR SMR; Q28035; -.
DR STRING; 9913.ENSBTAP00000005618; -.
DR PaxDb; Q28035; -.
DR PeptideAtlas; Q28035; -.
DR PRIDE; Q28035; -.
DR GeneID; 777644; -.
DR KEGG; bta:777644; -.
DR CTD; 2938; -.
DR eggNOG; KOG1695; Eukaryota.
DR HOGENOM; CLU_039475_4_0_1; -.
DR InParanoid; Q28035; -.
DR OrthoDB; 1162336at2759; -.
DR TreeFam; TF105321; -.
DR BRENDA; 2.5.1.18; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004769; F:steroid delta-isomerase activity; ISS:UniProtKB.
DR GO; GO:1901687; P:glutathione derivative biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin 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; IPR040079; Glutathione_S-Trfase.
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; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01266; GSTRNSFRASEA.
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; Isomerase; Lipid metabolism; Oxidoreductase;
KW Peroxidase; Reference proteome; Transferase.
FT CHAIN 1..222
FT /note="Glutathione S-transferase A1"
FT /id="PRO_0000421781"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT CHAIN 2..222
FT /note="Glutathione S-transferase A1, N-terminally
FT processed"
FT /id="PRO_0000185780"
FT DOMAIN 3..83
FT /note="GST N-terminal"
FT DOMAIN 85..208
FT /note="GST C-terminal"
FT BINDING 9
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P13745"
FT BINDING 45
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 A1, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT MOD_RES 4
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30115"
FT CONFLICT 190..191
FT /note="NI -> SL (in Ref. 1; AAB72239)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 25452 MW; F2708C849CB04655 CRC64;
MAGKPTLHYF NGRGRMECIR WLLAAAGVEF EEKFIEKPED LDKLKNDGSL MFQQVPMVEI
DGMKLVQTRA ILNYIATKYN LYGKDMKERA LIDMYSEGVA DLGEMIMHFP LCPPAEKDAK
LTLIREKTTN RYLPAFENVL KSHGQDYLVG NKLSRADIHL VELLYYVEEL DPSLLANFPL
LKALKARVSN IPAVKKFLQP GSQRKPPTDE KKIEEARKVF KF
