MGST2_MOUSE
ID MGST2_MOUSE Reviewed; 147 AA.
AC A2RST1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Microsomal glutathione S-transferase 2;
DE Short=Microsomal GST-2;
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:Q99735};
DE AltName: Full=Glutathione peroxidase MGST2;
DE EC=1.11.1.- {ECO:0000250|UniProtKB:Q99735};
DE AltName: Full=Leukotriene C4 synthase MGST2;
DE EC=4.4.1.20 {ECO:0000250|UniProtKB:Q99735};
DE AltName: Full=Microsomal glutathione S-transferase II;
DE Short=Microsomal GST-II;
GN Name=Mgst2 {ECO:0000312|MGI:MGI:2448481}; Synonyms=Gst2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=26656251; DOI=10.1038/ncomms10112;
RA Dvash E., Har-Tal M., Barak S., Meir O., Rubinstein M.;
RT "Leukotriene C4 is the major trigger of stress-induced oxidative DNA
RT damage.";
RL Nat. Commun. 6:10112-10112(2015).
CC -!- FUNCTION: Catalyzes several different glutathione-dependent reactions.
CC Catalyzes the glutathione-dependent reduction of lipid hydroperoxides,
CC such as 5-HPETE. Has glutathione transferase activity, toward
CC xenobiotic electrophiles, such as 1-chloro-2, 4-dinitrobenzene (CDNB).
CC Catalyzes also the conjugation of leukotriene A4 with reduced
CC glutathione to form leukotriene C4 (LTC4) (By similarity). Involved in
CC oxidative DNA damage induced by ER stress and anticancer agents by
CC activating LTC4 biosynthetic machinery in nonimmune cells
CC (PubMed:26656251). {ECO:0000250|UniProtKB:Q99735,
CC ECO:0000269|PubMed:26656251}.
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:Q99735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-
CC S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18;
CC Evidence={ECO:0000250|UniProtKB:Q99735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=leukotriene C4 = glutathione + leukotriene A4;
CC Xref=Rhea:RHEA:17617, ChEBI:CHEBI:57463, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:57973; EC=4.4.1.20;
CC Evidence={ECO:0000250|UniProtKB:Q99735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2
CC glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate +
CC glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC ChEBI:CHEBI:90632; Evidence={ECO:0000250|UniProtKB:Q99735};
CC -!- ACTIVITY REGULATION: Each monomer binds on GSH molecule but only one
CC subunit is catalytically active. {ECO:0000250|UniProtKB:Q99735}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q99735}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q99735}; Multi-pass membrane protein
CC {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:Q99735};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice display resistance to induced ER
CC stress with reduced cell death and mortality.
CC {ECO:0000269|PubMed:26656251}.
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; AC102860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132234; AAI32235.1; -; mRNA.
DR EMBL; BC132260; AAI32261.1; -; mRNA.
DR CCDS; CCDS38428.1; -.
DR RefSeq; NP_778160.2; NM_174995.3.
DR AlphaFoldDB; A2RST1; -.
DR SMR; A2RST1; -.
DR STRING; 10090.ENSMUSP00000096705; -.
DR PhosphoSitePlus; A2RST1; -.
DR MaxQB; A2RST1; -.
DR PaxDb; A2RST1; -.
DR ProteomicsDB; 337268; -.
DR Antibodypedia; 2759; 180 antibodies from 28 providers.
DR DNASU; 211666; -.
DR Ensembl; ENSMUST00000099106; ENSMUSP00000096705; ENSMUSG00000074604.
DR GeneID; 211666; -.
DR KEGG; mmu:211666; -.
DR UCSC; uc008ped.1; mouse.
DR CTD; 4258; -.
DR MGI; MGI:2448481; Mgst2.
DR VEuPathDB; HostDB:ENSMUSG00000074604; -.
DR eggNOG; ENOG502S082; Eukaryota.
DR GeneTree; ENSGT00940000160288; -.
DR HOGENOM; CLU_110291_3_0_1; -.
DR InParanoid; A2RST1; -.
DR OMA; YARHKYF; -.
DR OrthoDB; 1609516at2759; -.
DR PhylomeDB; A2RST1; -.
DR TreeFam; TF105328; -.
DR Reactome; R-MMU-156590; Glutathione conjugation.
DR Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
DR BioGRID-ORCS; 211666; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Mgst2; mouse.
DR PRO; PR:A2RST1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; A2RST1; protein.
DR Bgee; ENSMUSG00000074604; Expressed in mucosa of stomach and 128 other tissues.
DR ExpressionAtlas; A2RST1; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0004464; F:leukotriene-C4 synthase activity; ISS:UniProtKB.
DR GO; GO:0006750; P:glutathione biosynthetic process; ISO:MGI.
DR GO; GO:0019370; P:leukotriene biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0046466; P:membrane lipid catabolic process; ISO:MGI.
DR Gene3D; 1.20.120.550; -; 1.
DR InterPro; IPR001446; 5_LipOase_AP.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
DR Pfam; PF01124; MAPEG; 1.
DR PRINTS; PR00488; 5LPOXGNASEAP.
DR SUPFAM; SSF161084; SSF161084; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Leukotriene biosynthesis; Lipid metabolism; Lyase;
KW Membrane; Microsome; Oxidoreductase; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..147
FT /note="Microsomal glutathione S-transferase 2"
FT /id="PRO_0000449878"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 147 AA; 16786 MW; 57CFDC147DDF85E4 CRC64;
MAGDSSLLAA VSLLSACQQS YFAWRVGRAR LKHKIAPPAV TGPLEFERIF RAQQNSLEFY
PVFIVMLWMA GWYFNQVFAA CLGLLYIYAR HKYFWGYAEA AEKRITGFRL SLGILTLLPV
LAVLGVASRF LNEYLDFHVA KKLRKPF
