GSTM4_HUMAN
ID GSTM4_HUMAN Reviewed; 218 AA.
AC Q03013; A8K765; Q05465; Q32NC1; Q4JNT8; Q6FH87;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Glutathione S-transferase Mu 4;
DE EC=2.5.1.18 {ECO:0000269|PubMed:8203914, ECO:0000269|PubMed:8373352};
DE AltName: Full=GST class-mu 4;
DE AltName: Full=GST-Mu2;
DE AltName: Full=GSTM4-4;
DE AltName: Full=Leukotriene C4 synthase GSTM4;
DE EC=4.4.1.20 {ECO:0000269|PubMed:27791009};
GN Name=GSTM4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=8349586; DOI=10.1016/s0021-9258(19)85287-0;
RA Comstock K.E., Johnson K.J., Rifenbery D., Henner W.D.;
RT "Isolation and analysis of the gene and cDNA for a human Mu class
RT glutathione S-transferase, GSTM4.";
RL J. Biol. Chem. 268:16958-16965(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-212.
RX PubMed=8471052; DOI=10.1042/bj2910041;
RA Zhong S., Spurr N.K., Hayes J.D., Wolf C.R.;
RT "Deduced amino acid sequence, gene structure and chromosomal location of a
RT novel human class Mu glutathione S-transferase, GSTM4.";
RL Biochem. J. 291:41-50(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS,
RP CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RC TISSUE=Testis;
RX PubMed=8373352; DOI=10.1042/bj2940373;
RA Ross V.L., Board P.G.;
RT "Molecular cloning and heterologous expression of an alternatively spliced
RT human Mu class glutathione S-transferase transcript.";
RL Biochem. J. 294:373-380(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=16854533; DOI=10.1016/j.gene.2006.05.012;
RA Denson J., Xi Z., Wu Y., Yang W., Neale G., Zhang J.;
RT "Screening for inter-individual splicing differences in human GSTM4 and the
RT discovery of a single nucleotide substitution related to the tandem
RT skipping of two exons.";
RL Gene 379:148-155(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Lung;
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-160.
RC TISSUE=Lymphocyte;
RX PubMed=2006920; DOI=10.1042/bj2740587;
RA Taylor J.B., Oliver J., Sherrington R., Pemble S.E.;
RT "Structure of human glutathione S-transferase class Mu genes.";
RL Biochem. J. 274:587-593(1991).
RN [11]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8203914; DOI=10.1006/abbi.1994.1266;
RA Comstock K.E., Widersten M., Hao X.Y., Henner W.D., Mannervik B.;
RT "A comparison of the enzymatic and physicochemical properties of human
RT glutathione transferase M4-4 and three other human Mu class enzymes.";
RL Arch. Biochem. Biophys. 311:487-495(1994).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS).
RX PubMed=10587441; DOI=10.1021/bi991714t;
RA Patskovsky Y.V., Patskovska L.N., Listowsky I.;
RT "An asparagine-phenylalanine substitution accounts for catalytic
RT differences between hGSTM3-3 and other human class mu glutathione S-
RT transferases.";
RL Biochemistry 38:16187-16194(1999).
RN [13]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27791009; DOI=10.1073/pnas.1607003113;
RA Dalli J., Vlasakov I., Riley I.R., Rodriguez A.R., Spur B.W., Petasis N.A.,
RA Chiang N., Serhan C.N.;
RT "Maresin conjugates in tissue regeneration biosynthesis enzymes in human
RT macrophages.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:12232-12237(2016).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles (PubMed:8203914,
CC PubMed:8373352). Catalyzes the conjugation of leukotriene A4 with
CC reduced glutathione (GSH) to form leukotriene C4 (PubMed:27791009). Can
CC also catalyzes the transfer of a glutathionyl group from glutathione
CC (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin
CC conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator
CC that possess potent anti-inflammatory and proresolving actions
CC (PubMed:27791009). {ECO:0000269|PubMed:27791009,
CC ECO:0000269|PubMed:8203914, ECO:0000269|PubMed:8373352}.
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; Evidence={ECO:0000269|PubMed:8203914,
CC ECO:0000269|PubMed:8373352};
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:8203914, ECO:0000269|PubMed:8373352};
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:0000269|PubMed:27791009};
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:0000269|PubMed:27791009};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 mM for glutathione {ECO:0000269|PubMed:8203914};
CC KM=98 uM for leukotriene A4 {ECO:0000269|PubMed:27791009};
CC KM=42.5 mM for (13R)-S-glutathionyl-(14S)-hydroxy-
CC (4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate
CC {ECO:0000269|PubMed:27791009};
CC KM=9.0 mM for 1-chloro-2,4-dinitrobenzene
CC {ECO:0000269|PubMed:8203914};
CC Vmax=1.6 mmol/min/mg enzyme with leukotriene A4 as substrate
CC {ECO:0000269|PubMed:27791009};
CC Vmax=5.1 mmol/min/mg enzyme with (13S,14S)-epoxy-
CC (4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate as substrate
CC {ECO:0000269|PubMed:27791009};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8373352}.
CC -!- INTERACTION:
CC Q03013; P05067: APP; NbExp=3; IntAct=EBI-713363, EBI-77613;
CC Q03013; P21266: GSTM3; NbExp=4; IntAct=EBI-713363, EBI-350350;
CC Q03013; Q6FGJ9: GSTM3; NbExp=3; IntAct=EBI-713363, EBI-10209603;
CC Q03013; P46439: GSTM5; NbExp=3; IntAct=EBI-713363, EBI-4312072;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8373352}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q03013-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03013-2; Sequence=VSP_011773, VSP_011774;
CC Name=3;
CC IsoId=Q03013-3; Sequence=VSP_047688;
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues.
CC -!- SIMILARITY: Belongs to the GST superfamily. Mu 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; M96234; AAA57347.1; -; mRNA.
DR EMBL; M96233; AAA57346.1; -; Genomic_DNA.
DR EMBL; X68677; CAA48637.1; -; Genomic_DNA.
DR EMBL; M99422; AAA58623.1; -; mRNA.
DR EMBL; DQ062813; AAY98515.1; -; mRNA.
DR EMBL; CR541869; CAG46667.1; -; mRNA.
DR EMBL; AK291880; BAF84569.1; -; mRNA.
DR EMBL; AC000031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56405.1; -; Genomic_DNA.
DR EMBL; BC015513; AAH15513.1; -; mRNA.
DR EMBL; BC108729; AAI08730.1; -; mRNA.
DR EMBL; X56837; CAA40167.1; -; Genomic_DNA.
DR CCDS; CCDS806.1; -. [Q03013-2]
DR CCDS; CCDS807.1; -. [Q03013-1]
DR PIR; A47486; A47486.
DR PIR; S32425; S32425.
DR RefSeq; NP_000841.1; NM_000850.4. [Q03013-1]
DR RefSeq; NP_671489.1; NM_147148.2. [Q03013-2]
DR PDB; 4GTU; X-ray; 3.30 A; A/B/C/D/E/F/G/H=2-218.
DR PDBsum; 4GTU; -.
DR AlphaFoldDB; Q03013; -.
DR SMR; Q03013; -.
DR BioGRID; 109203; 20.
DR IntAct; Q03013; 14.
DR STRING; 9606.ENSP00000358851; -.
DR ChEMBL; CHEMBL2100; -.
DR DrugBank; DB03706; 1-Hydroxy-2-S-glutathionyl-3-para-nitrophenoxy-propane.
DR DrugBank; DB03597; gamma-Glutamyl[S-(2-iodobenzyl)cysteinyl]glycine.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB03310; Glutathione disulfide.
DR DrugBank; DB03003; Glutathione sulfonic acid.
DR DrugBank; DB04132; S-Hexylglutathione.
DR DrugBank; DB03032; S-octylglutathione.
DR SwissLipids; SLP:000001727; -.
DR iPTMnet; Q03013; -.
DR PhosphoSitePlus; Q03013; -.
DR BioMuta; GSTM4; -.
DR DMDM; 1170096; -.
DR REPRODUCTION-2DPAGE; IPI00008770; -.
DR EPD; Q03013; -.
DR jPOST; Q03013; -.
DR MassIVE; Q03013; -.
DR MaxQB; Q03013; -.
DR PaxDb; Q03013; -.
DR PeptideAtlas; Q03013; -.
DR PRIDE; Q03013; -.
DR ProteomicsDB; 58159; -. [Q03013-1]
DR ProteomicsDB; 58160; -. [Q03013-2]
DR ProteomicsDB; 62190; -.
DR Antibodypedia; 33768; 172 antibodies from 27 providers.
DR DNASU; 2948; -.
DR Ensembl; ENST00000326729.9; ENSP00000316471.5; ENSG00000168765.18. [Q03013-2]
DR Ensembl; ENST00000369836.9; ENSP00000358851.4; ENSG00000168765.18. [Q03013-1]
DR GeneID; 2948; -.
DR KEGG; hsa:2948; -.
DR MANE-Select; ENST00000369836.9; ENSP00000358851.4; NM_000850.5; NP_000841.1.
DR UCSC; uc001dyf.4; human. [Q03013-1]
DR CTD; 2948; -.
DR DisGeNET; 2948; -.
DR GeneCards; GSTM4; -.
DR HGNC; HGNC:4636; GSTM4.
DR HPA; ENSG00000168765; Tissue enhanced (intestine).
DR MIM; 138333; gene.
DR neXtProt; NX_Q03013; -.
DR OpenTargets; ENSG00000168765; -.
DR PharmGKB; PA29026; -.
DR VEuPathDB; HostDB:ENSG00000168765; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000154679; -.
DR InParanoid; Q03013; -.
DR OMA; RVATWGN; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; Q03013; -.
DR TreeFam; TF353040; -.
DR BRENDA; 2.5.1.18; 2681.
DR PathwayCommons; Q03013; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR Reactome; R-HSA-9026762; Biosynthesis of maresin conjugates in tissue regeneration (MCTR).
DR SABIO-RK; Q03013; -.
DR SignaLink; Q03013; -.
DR BioGRID-ORCS; 2948; 29 hits in 1072 CRISPR screens.
DR ChiTaRS; GSTM4; human.
DR EvolutionaryTrace; Q03013; -.
DR GeneWiki; GSTM4; -.
DR GenomeRNAi; 2948; -.
DR Pharos; Q03013; Tbio.
DR PRO; PR:Q03013; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q03013; protein.
DR Bgee; ENSG00000168765; Expressed in hindlimb stylopod muscle and 159 other tissues.
DR ExpressionAtlas; Q03013; baseline and differential.
DR Genevisible; Q03013; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0043295; F:glutathione binding; IDA:BHF-UCL.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0004464; F:leukotriene-C4 synthase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:BHF-UCL.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0018916; P:nitrobenzene metabolic process; IEA:Ensembl.
DR GO; GO:0042178; P:xenobiotic catabolic process; IDA:BHF-UCL.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
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 SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
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 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Lipid metabolism; Lyase; Reference proteome; Transferase.
FT CHAIN 1..218
FT /note="Glutathione S-transferase Mu 4"
FT /id="PRO_0000185824"
FT DOMAIN 2..88
FT /note="GST N-terminal"
FT DOMAIN 90..208
FT /note="GST C-terminal"
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"
FT VAR_SEQ 60..120
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16854533"
FT /id="VSP_047688"
FT VAR_SEQ 190..195
FT /note="GLEKIS -> VSCGIM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8373352"
FT /id="VSP_011773"
FT VAR_SEQ 196..218
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8373352"
FT /id="VSP_011774"
FT VARIANT 2
FT /note="S -> P (in dbSNP:rs3211190)"
FT /id="VAR_033979"
FT VARIANT 160
FT /note="A -> V (in dbSNP:rs17838158)"
FT /id="VAR_033980"
FT VARIANT 208
FT /note="L -> V (in dbSNP:rs112611763)"
FT /id="VAR_049487"
FT VARIANT 209
FT /note="Y -> F (in dbSNP:rs112330158)"
FT /id="VAR_049488"
FT VARIANT 211
FT /note="R -> K (in dbSNP:rs200675176)"
FT /id="VAR_049489"
FT VARIANT 212
FT /note="V -> M (in dbSNP:rs149370166)"
FT /evidence="ECO:0000269|PubMed:8471052"
FT /id="VAR_049490"
FT CONFLICT 2..4
FT /note="SMT -> PMI (in Ref. 2; CAA48637)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="I -> M (in Ref. 1; AAA57346)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="D -> G (in Ref. 2; CAA48637)"
FT /evidence="ECO:0000305"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:4GTU"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:4GTU"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4GTU"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:4GTU"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:4GTU"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:4GTU"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:4GTU"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:4GTU"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:4GTU"
FT HELIX 91..114
FT /evidence="ECO:0007829|PDB:4GTU"
FT HELIX 120..142
FT /evidence="ECO:0007829|PDB:4GTU"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:4GTU"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:4GTU"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:4GTU"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:4GTU"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:4GTU"
SQ SEQUENCE 218 AA; 25561 MW; 35E96FA54D566B1E CRC64;
MSMTLGYWDI RGLAHAIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL
PYLIDGAHKI TQSNAILCYI ARKHNLCGET EEEKIRVDIL ENQAMDVSNQ LARVCYSPDF
EKLKPEYLEE LPTMMQHFSQ FLGKRPWFVG DKITFVDFLA YDVLDLHRIF EPNCLDAFPN
LKDFISRFEG LEKISAYMKS SRFLPKPLYT RVAVWGNK
