ID   MGST1_BOVIN             Reviewed;         155 AA.
AC   Q64L89;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   08-NOV-2023, entry version 90.
DE   RecName: Full=Microsomal glutathione S-transferase 1;
DE            Short=Microsomal GST-1;
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:P08011};
GN   Name=MGST1;
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].
RA   Maeda A., Palczewski K.;
RT   "Characterization of bovine microsomal glutathione-S-transferase 1.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000250|UniProtKB:P08011}.
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:P08011};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16438;
CC         Evidence={ECO:0000250|UniProtKB:P08011};
CC   -!- SUBUNIT: Homotrimer; The trimer binds only one molecule of glutathione.
CC       {ECO:0000250|UniProtKB:P08011}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P08011}; Multi-pass membrane protein
CC       {ECO:0000255}. Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P08011}.
CC   -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
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DR   EMBL; AY334548; AAR00934.1; -; mRNA.
DR   RefSeq; NP_001007816.1; NM_001007815.1.
DR   AlphaFoldDB; Q64L89; -.
DR   SMR; Q64L89; -.
DR   STRING; 9913.ENSBTAP00000011257; -.
DR   PaxDb; 9913-ENSBTAP00000011257; -.
DR   PeptideAtlas; Q64L89; -.
DR   GeneID; 493719; -.
DR   KEGG; bta:493719; -.
DR   CTD; 4257; -.
DR   eggNOG; ENOG502S0BD; Eukaryota.
DR   InParanoid; Q64L89; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1.
DR   InterPro; IPR023352; MAPEG-like_dom_sf.
DR   InterPro; IPR001129; Membr-assoc_MAPEG.
DR   InterPro; IPR040162; MGST1-like.
DR   PANTHER; PTHR10689; MICROSOMAL GLUTATHIONE S-TRANSFERASE 1; 1.
DR   PANTHER; PTHR10689:SF3; MICROSOMAL GLUTATHIONE S-TRANSFERASE 1; 1.
DR   Pfam; PF01124; MAPEG; 1.
DR   SUPFAM; SSF161084; MAPEG domain-like; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..155
FT                   /note="Microsomal glutathione S-transferase 1"
FT                   /id="PRO_0000246086"
FT   TOPO_DOM        3..9
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P08011"
FT   TRANSMEM        10..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..62
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P08011"
FT   TRANSMEM        63..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..99
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P08011"
FT   TRANSMEM        100..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..128
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P08011"
FT   TRANSMEM        129..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..155
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P08011"
FT   BINDING         38
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08011"
FT   BINDING         73
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08011"
FT   BINDING         74
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08011"
FT   BINDING         76
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08011"
FT   BINDING         81
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08011"
FT   BINDING         121
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P08011"
FT   MOD_RES         42
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VS7"
FT   MOD_RES         55
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VS7"
FT   MOD_RES         60
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91VS7"
SQ   SEQUENCE   155 AA;  17645 MW;  0D762B5FF480BCDC CRC64;
     MANLSQLMEN EVFMAFASYT TIVLSKMNFM STATAFYRLT KKVFANPEDC AGFGKGENAK
     KYLRTDDRVE RVRRAHLNDL ENIVPFLGIG LLYSLSGPDL STAILHFRLF VRARIYHTIA
     YLTPLPQPNR ALAFFIGYGV TLSMAYRLLK SKLYL
//