ID   GSTA4_BOVIN             Reviewed;         222 AA.
AC   Q5E9G0;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 120.
DE   RecName: Full=Glutathione S-transferase A4;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-alpha member 4;
DE   AltName: Full=Glutathione S-transferase alpha-4;
GN   Name=GSTA4;
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 [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the GST superfamily. Alpha family.
CC       {ECO:0000305}.
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DR   EMBL; BT020960; AAX08977.1; -; mRNA.
DR   RefSeq; NP_001015651.1; NM_001015651.1.
DR   AlphaFoldDB; Q5E9G0; -.
DR   SMR; Q5E9G0; -.
DR   STRING; 9913.ENSBTAP00000063570; -.
DR   PaxDb; 9913-ENSBTAP00000028640; -.
DR   Ensembl; ENSBTAT00000028640.5; ENSBTAP00000028640.4; ENSBTAG00000004288.6.
DR   GeneID; 533917; -.
DR   KEGG; bta:533917; -.
DR   CTD; 2941; -.
DR   VEuPathDB; HostDB:ENSBTAG00000004288; -.
DR   VGNC; VGNC:53979; GSTA4.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00940000162778; -.
DR   HOGENOM; CLU_039475_4_0_1; -.
DR   InParanoid; Q5E9G0; -.
DR   OMA; TVYNVFM; -.
DR   TreeFam; TF105321; -.
DR   Reactome; R-BTA-156590; Glutathione conjugation.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000004288; Expressed in pituitary gland and 106 other cell types or tissues.
DR   ExpressionAtlas; Q5E9G0; baseline.
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   CDD; cd03208; GST_C_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; 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:SF123; GLUTATHIONE S-TRANSFERASE A4; 1.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01266; GSTRNSFRASEA.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..222
FT                   /note="Glutathione S-transferase A4"
FT                   /id="PRO_0000249771"
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         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:P14942"
SQ   SEQUENCE   222 AA;  25659 MW;  A0C06C858741A67B CRC64;
     MATKPKLHYP NGRGRMESVR WVLAAAGVEF DEEFLETKEQ LQKLQDGNHL LFQQVPMVEI
     DGMKLVQTRS ILHYIADKHH LFGKDLKERT LIDMYVEGTL DLLELLIMHP FLKPDDQQKE
     VANMAQKAII RYFPVFEKVL RGHGQRFLVG NQLSLADIIL LQTILALEEK IPNILSAFPH
     LQEYTVKISN IPTIKKFLEP GSKKKPPPDD IYVRTVYNIF MP
//