GSTM4_MOUSE
ID GSTM4_MOUSE Reviewed; 218 AA.
AC Q8R5I6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Glutathione S-transferase Mu 4;
DE EC=2.5.1.18 {ECO:0000269|PubMed:12069689};
DE AltName: Full=GST class-mu 4;
DE AltName: Full=GSTM4-4;
DE AltName: Full=Glutathione transferase GSTM7-7 {ECO:0000303|PubMed:12069689};
DE AltName: Full=Leukotriene C4 synthase GSTM4;
DE EC=4.4.1.20 {ECO:0000250|UniProtKB:Q03013};
GN Name=Gstm4 {ECO:0000303|PubMed:11991805, ECO:0000312|MGI:MGI:95862};
GN Synonyms=Gstm7 {ECO:0000303|PubMed:12069689},
GN Gstm7-7 {ECO:0000303|PubMed:12069689};
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].
RX PubMed=11991805; DOI=10.1042/bj20020320;
RA Chanas S.A., Jiang Q., McMahon M., McWalter G.K., McLellan L.I.,
RA Elcombe C.R., Henderson C.J., Wolf C.R., Moffat G.J., Itoh K., Yamamoto M.,
RA Hayes J.D.;
RT "Loss of the Nrf2 transcription factor causes a marked reduction in
RT constitutive and inducible expression of the glutathione S-transferase
RT Gsta1, Gsta2, Gstm1, Gstm2, Gstm3 and Gstm4 genes in the livers of male and
RT female mice.";
RL Biochem. J. 365:405-416(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBUNIT, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=A/J;
RX PubMed=12069689; DOI=10.1042/bj20020041;
RA Guo J., Zimniak L., Zimniak P., Orchard J.L., Singh S.V.;
RT "Cloning and expression of a novel Mu class murine glutathione transferase
RT isoenzyme.";
RL Biochem. J. 366:817-824(2002).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3;
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 [5] {ECO:0007744|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Catalyzes the
CC conjugation of leukotriene A4 with reduced glutathione (GSH) to form
CC leukotriene C4. Can also catalyze the transfer of a glutathionyl group
CC from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to
CC form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive
CC lipid mediator that possess potent anti-inflammatory and proresolving
CC actions. {ECO:0000250|UniProtKB:Q03013}.
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:0000269|PubMed:12069689};
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:0000269|PubMed:12069689};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(13S,14S)-epoxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate +
CC glutathione = (13R)-S-glutathionyl-(14S)-hydroxy-
CC (4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:53508,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:131958, ChEBI:CHEBI:137407;
CC Evidence={ECO:0000250|UniProtKB:Q03013};
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:Q03013};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12069689}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q03013}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12069689}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu family. {ECO:0000305}.
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DR EMBL; AF501320; AAM67419.1; -; mRNA.
DR EMBL; AF464943; AAL76248.1; -; mRNA.
DR EMBL; AL671877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030444; AAH30444.1; -; mRNA.
DR CCDS; CCDS17748.1; -.
DR RefSeq; NP_081040.1; NM_026764.3.
DR AlphaFoldDB; Q8R5I6; -.
DR SMR; Q8R5I6; -.
DR STRING; 10090.ENSMUSP00000029489; -.
DR PhosphoSitePlus; Q8R5I6; -.
DR EPD; Q8R5I6; -.
DR jPOST; Q8R5I6; -.
DR MaxQB; Q8R5I6; -.
DR PaxDb; Q8R5I6; -.
DR PeptideAtlas; Q8R5I6; -.
DR PRIDE; Q8R5I6; -.
DR ProteomicsDB; 338791; -.
DR Antibodypedia; 33768; 172 antibodies from 27 providers.
DR DNASU; 14865; -.
DR Ensembl; ENSMUST00000029489; ENSMUSP00000029489; ENSMUSG00000027890.
DR GeneID; 14865; -.
DR KEGG; mmu:14865; -.
DR UCSC; uc008qxy.2; mouse.
DR CTD; 2948; -.
DR MGI; MGI:95862; Gstm4.
DR VEuPathDB; HostDB:ENSMUSG00000027890; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000154679; -.
DR HOGENOM; CLU_039475_2_0_1; -.
DR InParanoid; Q8R5I6; -.
DR OMA; RVATWGN; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; Q8R5I6; -.
DR TreeFam; TF353040; -.
DR Reactome; R-MMU-156590; Glutathione conjugation.
DR Reactome; R-MMU-9026762; Biosynthesis of maresin conjugates in tissue regeneration (MCTR).
DR BioGRID-ORCS; 14865; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8R5I6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8R5I6; protein.
DR Bgee; ENSMUSG00000027890; Expressed in urinary bladder urothelium and 195 other tissues.
DR ExpressionAtlas; Q8R5I6; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0043295; F:glutathione binding; ISO:MGI.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:MGI.
DR GO; GO:0004464; F:leukotriene-C4 synthase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:MGI.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0018916; P:nitrobenzene metabolic process; IDA:MGI.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:MGI.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR003081; GST_mu.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01267; GSTRNSFRASEM.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid metabolism; Lyase; Reference proteome; Transferase.
FT CHAIN 1..218
FT /note="Glutathione S-transferase Mu 4"
FT /id="PRO_0000449827"
FT DOMAIN 1..88
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 90..208
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
FT BINDING 7..8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 46..50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 59..60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 72..73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P08515"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 218 AA; 25519 MW; 81F15DBB46118102 CRC64;
MPMTLGYWDI RGLAHAIRLL LEYTGSSYEE KRYTMGDAPD YDRSQWLSEK FKLGLDFPNL
PYLIDGSHKI TQSNAILRYI ARKHNLCGET EEEKIRVDIL ENQAMDVSNQ LARVCYSPDF
EKLKVEYLEQ LPGMVKLFSQ FLGQRTWFVG EKITFVDFLA YDILDLHLIF EPTCLDAFPN
LKDFVARFEV LKRISAYMKT SRFLRTPLYT KVATWGNK
