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   24-JAN-2024, entry version 144.
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   PaxDb; 9913-ENSBTAP00000005618; -.
DR   PeptideAtlas; 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; 3412208at2759; -.
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   CDD; cd03208; GST_C_Alpha; 1.
DR   CDD; cd03077; GST_N_Alpha; 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; 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   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF107; GLUTATHIONE S-TRANSFERASE A2; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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   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
//