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 24-JAN-2024, entry version 110. DE RecName: Full=Microsomal glutathione S-transferase 1; DE Short=Microsomal GST-1; DE EC=2.5.1.18 {ECO:0000250|UniProtKB:P08011}; 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. 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}. 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; AB000884; BAA19201.1; -; mRNA. DR RefSeq; NP_999465.1; NM_214300.1. DR AlphaFoldDB; P79382; -. DR SMR; P79382; -. DR STRING; 9823.ENSSSCP00000038329; -. DR PeptideAtlas; P79382; -. DR Ensembl; ENSSSCT00000048776.2; ENSSSCP00000038329.1; ENSSSCG00000032580.3. DR Ensembl; ENSSSCT00005018533.1; ENSSSCP00005011141.1; ENSSSCG00005011954.1. DR Ensembl; ENSSSCT00005018568.1; ENSSSCP00005011164.1; ENSSSCG00005011954.1. DR Ensembl; ENSSSCT00015003957.1; ENSSSCP00015001378.1; ENSSSCG00015003104.1. DR Ensembl; ENSSSCT00025021694.1; ENSSSCP00025008928.1; ENSSSCG00025016137.1. DR Ensembl; ENSSSCT00030083657.1; ENSSSCP00030038426.1; ENSSSCG00030059915.1. DR Ensembl; ENSSSCT00035051698.1; ENSSSCP00035020735.1; ENSSSCG00035038953.1. DR Ensembl; ENSSSCT00040088442.1; ENSSSCP00040038872.1; ENSSSCG00040064750.1. DR Ensembl; ENSSSCT00045035331.1; ENSSSCP00045024519.1; ENSSSCG00045020728.1. DR Ensembl; ENSSSCT00045035372.1; ENSSSCP00045024554.1; ENSSSCG00045020728.1. DR Ensembl; ENSSSCT00050045888.1; ENSSSCP00050018865.1; ENSSSCG00050034218.1. DR Ensembl; ENSSSCT00055032068.1; ENSSSCP00055025531.1; ENSSSCG00055016266.1. DR Ensembl; ENSSSCT00060067096.1; ENSSSCP00060028737.1; ENSSSCG00060049400.1. DR Ensembl; ENSSSCT00065062036.1; ENSSSCP00065026886.1; ENSSSCG00065045328.1. DR Ensembl; ENSSSCT00070045300.1; ENSSSCP00070038179.1; ENSSSCG00070022772.1. 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; 5347993at2759; -. DR Reactome; R-SSC-156590; Glutathione conjugation. DR Reactome; R-SSC-5423646; Aflatoxin activation and detoxification. DR Reactome; R-SSC-6798695; Neutrophil degranulation. DR Proteomes; UP000008227; Chromosome 5. DR Proteomes; UP000314985; Chromosome 5. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR Bgee; ENSSSCG00000032580; Expressed in omentum and 42 other cell types or tissues. 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: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; 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_0000217738" 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; 17650 MW; C48A76872F493A32 CRC64; MADLTELMKN EVFMAFASYA TIVLSKMMFM STATAFYRLT RKVFANPEDC SSFGKGENAK KYLRTDERVE RVRRAHLNDL ENIVPFLGIG LLYSLSGPDL STAILHFRLF VGARIYHTIA YLTPLPQPNR GLAFFLGYGV TLSMAYRLLK SRLYL //