ID   GSTA2_BOVIN             Reviewed;         223 AA.
AC   O18879; Q1RML3;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Glutathione S-transferase A2;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-alpha member 2;
DE   AltName: Full=Glutathione S-transferase alpha-2;
GN   Name=GSTA2;
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=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB83995.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF027386; AAB83995.1; ALT_FRAME; mRNA.
DR   EMBL; BC114835; AAI14836.1; -; mRNA.
DR   RefSeq; NP_803481.1; NM_177515.2.
DR   AlphaFoldDB; O18879; -.
DR   SMR; O18879; -.
DR   STRING; 9913.ENSBTAP00000043661; -.
DR   PaxDb; O18879; -.
DR   PeptideAtlas; O18879; -.
DR   PRIDE; O18879; -.
DR   Ensembl; ENSBTAT00000046354; ENSBTAP00000043661; ENSBTAG00000006546.
DR   GeneID; 281805; -.
DR   KEGG; bta:281805; -.
DR   CTD; 2939; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006546; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000154526; -.
DR   HOGENOM; CLU_039475_4_0_1; -.
DR   InParanoid; O18879; -.
DR   OMA; CKPDILA; -.
DR   OrthoDB; 1162336at2759; -.
DR   TreeFam; TF105321; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000006546; Expressed in lung and 93 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; PF14497; GST_C_3; 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; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P30115"
FT   CHAIN           2..223
FT                   /note="Glutathione S-transferase A2"
FT                   /id="PRO_0000185781"
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:P08263"
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         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P30115"
FT   MOD_RES         4
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P30115"
SQ   SEQUENCE   223 AA;  25717 MW;  D61050D129901EB7 CRC64;
     MAGKPKLHYF NGRGRMECIR WLLAAAGVEF EEKFIEQPED LDKLRNDGSL MFQQVPMVEI
     DGMKLVQTRA ILNYIATKYN LYGKDMKERA LIDMYSEGVE DLGEMIMHLP LCPPDQKDAK
     IAQIKERTTN RYFPAFEKVL KNHGQDYLVG NKLSKADIHL VELLYYVEEL DPSLLANFPL
     LKGLKARVSS LPAVKKFLQP GSQRKPPMDE KNLEEAKRIF RIK