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Database: UniProt/SWISS-PROT
Entry: MGST1_BOVIN
LinkDB: MGST1_BOVIN
Original site: 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   05-DEC-2018, entry version 75.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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-
CC       50 sulfhydryl, such as N-ethylmaleimide. Activation also occurs
CC       via nitration of Tyr-93 by peroxynitrite (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer; The trimer binds only one molecule of
CC       glutathione. {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}.
DR   EMBL; AY334548; AAR00934.1; -; mRNA.
DR   RefSeq; NP_001007816.1; NM_001007815.1.
DR   UniGene; Bt.107316; -.
DR   ProteinModelPortal; 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; ENOG410IXE1; Eukaryota.
DR   eggNOG; ENOG4111VJG; LUCA.
DR   HOGENOM; HOG000231759; -.
DR   HOVERGEN; HBG052470; -.
DR   InParanoid; Q64L89; -.
DR   KO; K00799; -.
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:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central.
DR   GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
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; Complete proteome; Endoplasmic reticulum; Membrane;
KW   Microsome; Mitochondrion; Mitochondrion outer membrane; Nitration;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    155       Microsomal glutathione S-transferase 1.
FT                                /FTId=PRO_0000246086.
FT   TOPO_DOM      3      9       Lumenal. {ECO:0000250}.
FT   TRANSMEM     10     33       Helical. {ECO:0000250}.
FT   TOPO_DOM     34     62       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM     63     96       Helical. {ECO:0000250}.
FT   TOPO_DOM     97     99       Lumenal. {ECO:0000250}.
FT   TRANSMEM    100    123       Helical. {ECO:0000250}.
FT   TOPO_DOM    124    128       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM    129    148       Helical. {ECO:0000250}.
FT   TOPO_DOM    149    155       Lumenal. {ECO:0000250}.
FT   BINDING      38     38       Glutathione. {ECO:0000250}.
FT   BINDING      73     73       Glutathione. {ECO:0000250}.
FT   BINDING      74     74       Glutathione. {ECO:0000250}.
FT   BINDING      76     76       Glutathione. {ECO:0000250}.
FT   BINDING      81     81       Glutathione. {ECO:0000250}.
FT   BINDING     121    121       Glutathione. {ECO:0000250}.
FT   SITE         50     50       Activates the enzyme when modified.
FT                                {ECO:0000250}.
FT   MOD_RES      42     42       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q91VS7}.
FT   MOD_RES      55     55       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q91VS7}.
FT   MOD_RES      60     60       N6-acetyllysine.
FT                                {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
//
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