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   24-JAN-2024, entry version 165.
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}, Gstm7-7
GN   {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   iPTMnet; Q8R5I6; -.
DR   PhosphoSitePlus; Q8R5I6; -.
DR   SwissPalm; Q8R5I6; -.
DR   EPD; Q8R5I6; -.
DR   jPOST; Q8R5I6; -.
DR   MaxQB; Q8R5I6; -.
DR   PaxDb; 10090-ENSMUSP00000029489; -.
DR   PeptideAtlas; Q8R5I6; -.
DR   ProteomicsDB; 338791; -.
DR   Pumba; Q8R5I6; -.
DR   Antibodypedia; 33768; 198 antibodies from 27 providers.
DR   DNASU; 14865; -.
DR   Ensembl; ENSMUST00000029489.15; ENSMUSP00000029489.9; ENSMUSG00000027890.18.
DR   GeneID; 14865; -.
DR   KEGG; mmu:14865; -.
DR   UCSC; uc008qxy.2; mouse.
DR   AGR; MGI:95862; -.
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; WRTAQWC; -.
DR   OrthoDB; 5488107at2759; -.
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 77 CRISPR screens.
DR   PRO; PR:Q8R5I6; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8R5I6; Protein.
DR   Bgee; ENSMUSG00000027890; Expressed in urinary bladder urothelium and 198 other cell types or 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   CDD; cd03209; GST_C_Mu; 1.
DR   CDD; cd03075; GST_N_Mu; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR11571:SF137; GLUTATHIONE S-TRANSFERASE MU 4; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01267; GSTRNSFRASEM.
DR   SFLD; SFLDG01205; AMPS.1; 1.
DR   SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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
//