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}.
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; 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
//
