MGST1_PIG
ID MGST1_PIG Reviewed; 155 AA.
AC P79382;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Microsomal glutathione S-transferase 1;
DE Short=Microsomal GST-1;
DE EC=2.5.1.18;
DE AltName: Full=Microsomal GST-I;
GN Name=MGST1; Synonyms=GST12;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kawakami K., Kimura M., Suzuki H., Hamasima N.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; AB000884; BAA19201.1; -; mRNA.
DR RefSeq; NP_999465.1; NM_214300.1.
DR AlphaFoldDB; P79382; -.
DR SMR; P79382; -.
DR PeptideAtlas; P79382; -.
DR PRIDE; P79382; -.
DR Ensembl; ENSSSCT00000048776; ENSSSCP00000038329; ENSSSCG00000032580.
DR Ensembl; ENSSSCT00005018533; ENSSSCP00005011141; ENSSSCG00005011954.
DR Ensembl; ENSSSCT00005018568; ENSSSCP00005011164; ENSSSCG00005011954.
DR Ensembl; ENSSSCT00015003957; ENSSSCP00015001378; ENSSSCG00015003104.
DR Ensembl; ENSSSCT00025021694; ENSSSCP00025008928; ENSSSCG00025016137.
DR Ensembl; ENSSSCT00030083657; ENSSSCP00030038426; ENSSSCG00030059915.
DR Ensembl; ENSSSCT00035051698; ENSSSCP00035020735; ENSSSCG00035038953.
DR Ensembl; ENSSSCT00040088442; ENSSSCP00040038872; ENSSSCG00040064750.
DR Ensembl; ENSSSCT00045035331; ENSSSCP00045024519; ENSSSCG00045020728.
DR Ensembl; ENSSSCT00045035372; ENSSSCP00045024554; ENSSSCG00045020728.
DR Ensembl; ENSSSCT00050045888; ENSSSCP00050018865; ENSSSCG00050034218.
DR Ensembl; ENSSSCT00055032068; ENSSSCP00055025531; ENSSSCG00055016266.
DR Ensembl; ENSSSCT00060067096; ENSSSCP00060028737; ENSSSCG00060049400.
DR Ensembl; ENSSSCT00065062036; ENSSSCP00065026886; ENSSSCG00065045328.
DR Ensembl; ENSSSCT00070045300; ENSSSCP00070038179; ENSSSCG00070022772.
DR GeneID; 397567; -.
DR KEGG; ssc:397567; -.
DR CTD; 4257; -.
DR VGNC; VGNC:103301; MGST1.
DR GeneTree; ENSGT00390000011980; -.
DR InParanoid; P79382; -.
DR OMA; TFSMAYN; -.
DR OrthoDB; 1591261at2759; -.
DR Proteomes; UP000008227; Chromosome 5.
DR Proteomes; UP000314985; Chromosome 5.
DR Bgee; ENSSSCG00000032580; Expressed in omentum and 42 other tissues.
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:0004602; F:glutathione peroxidase activity; IEA:Ensembl.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0071449; P:cellular response to lipid hydroperoxide; IEA:Ensembl.
DR GO; GO:0034635; P:glutathione transport; IEA:Ensembl.
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_0000217738"
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; 17650 MW; C48A76872F493A32 CRC64;
MADLTELMKN EVFMAFASYA TIVLSKMMFM STATAFYRLT RKVFANPEDC SSFGKGENAK
KYLRTDERVE RVRRAHLNDL ENIVPFLGIG LLYSLSGPDL STAILHFRLF VGARIYHTIA
YLTPLPQPNR GLAFFLGYGV TLSMAYRLLK SRLYL
