MGST1_MOUSE
ID MGST1_MOUSE Reviewed; 155 AA.
AC Q91VS7; Q9CQ57; Q9R191;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 143.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Raza H., Mullick J., Avadhani N.G.;
RT "Cloning, characterization and bacterial expression of full length cDNA for
RT the mouse liver microsomal glutathione S-transferase.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-55 AND LYS-60, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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: Acetylation of Lys-42 and Lys-55 is observed in liver mitochondria
CC from fasted mice but not from fed mice.
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; AF159050; AAD51096.1; -; mRNA.
DR EMBL; AK002800; BAB22368.1; -; mRNA.
DR EMBL; AK005122; BAB23827.1; -; mRNA.
DR EMBL; BC009155; AAH09155.1; -; mRNA.
DR CCDS; CCDS20668.1; -.
DR RefSeq; NP_064330.2; NM_019946.4.
DR AlphaFoldDB; Q91VS7; -.
DR SMR; Q91VS7; -.
DR BioGRID; 208104; 1.
DR STRING; 10090.ENSMUSP00000008684; -.
DR iPTMnet; Q91VS7; -.
DR PhosphoSitePlus; Q91VS7; -.
DR SwissPalm; Q91VS7; -.
DR jPOST; Q91VS7; -.
DR MaxQB; Q91VS7; -.
DR PaxDb; Q91VS7; -.
DR PRIDE; Q91VS7; -.
DR ProteomicsDB; 295939; -.
DR Antibodypedia; 23831; 235 antibodies from 32 providers.
DR DNASU; 56615; -.
DR Ensembl; ENSMUST00000008684; ENSMUSP00000008684; ENSMUSG00000008540.
DR Ensembl; ENSMUST00000120230; ENSMUSP00000113859; ENSMUSG00000008540.
DR Ensembl; ENSMUST00000120302; ENSMUSP00000113257; ENSMUSG00000008540.
DR GeneID; 56615; -.
DR KEGG; mmu:56615; -.
DR UCSC; uc009enk.1; mouse.
DR CTD; 4257; -.
DR MGI; MGI:1913850; Mgst1.
DR VEuPathDB; HostDB:ENSMUSG00000008540; -.
DR eggNOG; ENOG502S0BD; Eukaryota.
DR GeneTree; ENSGT00390000011980; -.
DR HOGENOM; CLU_105467_1_0_1; -.
DR InParanoid; Q91VS7; -.
DR OMA; TFSMAYN; -.
DR PhylomeDB; Q91VS7; -.
DR TreeFam; TF105327; -.
DR Reactome; R-MMU-156590; Glutathione conjugation.
DR Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 56615; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Mgst1; mouse.
DR PRO; PR:Q91VS7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91VS7; protein.
DR Bgee; ENSMUSG00000008540; Expressed in left lobe of liver and 286 other tissues.
DR ExpressionAtlas; Q91VS7; baseline and differential.
DR Genevisible; Q91VS7; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
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:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0043295; F:glutathione binding; ISO:MGI.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0071449; P:cellular response to lipid hydroperoxide; ISO:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:MGI.
DR GO; GO:0034635; P:glutathione transport; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0010243; P:response to organonitrogen compound; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
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 1: Evidence at protein 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_0000217737"
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:0007744|PubMed:23576753"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 5
FT /note="R -> K (in Ref. 1; AAD51096)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="G -> V (in Ref. 3; AAH09155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 155 AA; 17552 MW; C1E202663496C762 CRC64;
MADLRQLMDN EVLMAFTSYA TIILTKMMFM SSATAFQRIT NKVFANPEDC AGFGKGENAK
KFVRTDEKVE RVRRAHLNDL ENIVPFLGIG LLYSLSGPDL STALMHFRIF VGARIYHTIA
YLTPLPQPNR GLAFFVGYGV TLSMAYRLLR SRLYL
