MGST1_BOVIN
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 03-AUG-2022, entry version 86.
DE RecName: Full=Microsomal glutathione S-transferase 1;
DE Short=Microsomal GST-1;
DE EC=2.5.1.18;
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. Has a wide
CC substrate specificity (By similarity). {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 -!- ACTIVITY REGULATION: Can be activated by reagents that attack Cys-50
CC sulfhydryl, such as N-ethylmaleimide. Activation also occurs via
CC nitration of Tyr-93 by peroxynitrite (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; The trimer binds only one molecule of glutathione.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Mitochondrion outer
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Peroxynitrite induces nitration at Tyr-93 which activates the
CC enzyme. {ECO:0000250}.
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; Q64L89; -.
DR PeptideAtlas; Q64L89; -.
DR PRIDE; 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:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.20.120.550; -; 1.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
DR InterPro; IPR040162; MGST1-like.
DR PANTHER; PTHR10689; PTHR10689; 1.
DR Pfam; PF01124; MAPEG; 1.
DR SUPFAM; SSF161084; SSF161084; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Membrane; Microsome; Mitochondrion;
KW Mitochondrion outer membrane; Nitration; 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"
FT TRANSMEM 10..33
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 34..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 63..96
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 97..99
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 100..123
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 124..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 129..148
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 149..155
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT SITE 50
FT /note="Activates the enzyme when modified"
FT /evidence="ECO:0000250"
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
