MGST2_HUMAN
ID MGST2_HUMAN Reviewed; 147 AA.
AC Q99735; D6RBB5; Q7Z5B8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Microsomal glutathione S-transferase 2;
DE Short=Microsomal GST-2;
DE EC=2.5.1.18 {ECO:0000269|PubMed:23409838, ECO:0000269|PubMed:26066610, ECO:0000269|PubMed:8703034};
DE AltName: Full=Glutathione peroxidase MGST2 {ECO:0000305};
DE EC=1.11.1.- {ECO:0000269|PubMed:23409838, ECO:0000269|PubMed:9278457};
DE AltName: Full=Leukotriene C4 synthase MGST2 {ECO:0000305};
DE EC=4.4.1.20 {ECO:0000269|PubMed:11322876, ECO:0000269|PubMed:23409838, ECO:0000269|PubMed:26656251, ECO:0000269|PubMed:8703034};
DE AltName: Full=Microsomal glutathione S-transferase II {ECO:0000303|PubMed:8703034};
DE Short=Microsomal GST-II {ECO:0000303|PubMed:8703034};
GN Name=MGST2; Synonyms=GST2;
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 [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8703034; DOI=10.1074/jbc.271.36.22203;
RA Jakobsson P.-J., Mancini J.A., Ford-Hutchinson A.W.;
RT "Identification and characterization of a novel human microsomal
RT glutathione S-transferase with leukotriene C4 synthase activity and
RT significant sequence identity to 5-lipoxygenase-activating protein and
RT leukotriene C4 synthase.";
RL J. Biol. Chem. 271:22203-22210(1996).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9278457; DOI=10.1074/jbc.272.36.22934;
RA Jakobsson P.-J., Mancini J.A., Riendeau D., Ford-Hutchinson A.W.;
RT "Identification and characterization of a novel microsomal enzyme with
RT glutathione-dependent transferase and peroxidase activities.";
RL J. Biol. Chem. 272:22934-22939(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-101.
RG NIEHS SNPs program;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Neuroblastoma;
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 [7]
RP CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=11322876; DOI=10.1046/j.1432-1327.2001.02142.x;
RA Sjoestroem M., Jakobsson P.J., Heimburger M., Palmblad J.,
RA Haeggstroem J.Z.;
RT "Human umbilical vein endothelial cells generate leukotriene C4 via
RT microsomal glutathione S-transferase type 2 and express the CysLT(1)
RT receptor.";
RL Eur. J. Biochem. 268:2578-2586(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, SUBSTRATE
RP SPECIFICITY, AND ACTIVITY REGULATION.
RX PubMed=23409838; DOI=10.1021/bi3014104;
RA Ahmad S., Niegowski D., Wetterholm A., Haeggstroem J.Z., Morgenstern R.,
RA Rinaldo-Matthis A.;
RT "Catalytic characterization of human microsomal glutathione S-transferase
RT 2: identification of rate-limiting steps.";
RL Biochemistry 52:1755-1764(2013).
RN [12]
RP SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=26066610; DOI=10.1016/j.bbapap.2015.06.003;
RA Ahmad S., Thulasingam M., Palombo I., Daley D.O., Johnson K.A.,
RA Morgenstern R., Haeggstroem J.Z., Rinaldo-Matthis A.;
RT "Trimeric microsomal glutathione transferase 2 displays one third of the
RT sites reactivity.";
RL Biochim. Biophys. Acta 1854:1365-1371(2015).
RN [13]
RP FUNCTION, AND INDUCTION.
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 (PubMed:8703034, PubMed:9278457, PubMed:23409838, PubMed:26656251,
CC PubMed:26066610). Catalyzes the glutathione-dependent reduction of
CC lipid hydroperoxides, such as 5-HPETE (PubMed:9278457,
CC PubMed:23409838). Has glutathione transferase activity, toward
CC xenobiotic electrophiles, such as 1-chloro-2, 4-dinitrobenzene (CDNB)
CC (PubMed:23409838, PubMed:8703034). Catalyzes also the conjugation of
CC leukotriene A4 with reduced glutathione to form leukotriene C4 (LTC4)
CC (PubMed:23409838, PubMed:26656251). Involved in oxidative DNA damage
CC induced by ER stress and anticancer agents by activating LTC4
CC biosynthetic machinery in nonimmune cells (PubMed:26656251).
CC {ECO:0000269|PubMed:23409838, ECO:0000269|PubMed:26066610,
CC ECO:0000269|PubMed:26656251, ECO:0000269|PubMed:8703034,
CC ECO:0000269|PubMed:9278457}.
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:23409838, ECO:0000269|PubMed:26066610,
CC ECO:0000269|PubMed:8703034};
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:23409838, ECO:0000269|PubMed:8703034};
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:11322876, ECO:0000269|PubMed:23409838,
CC ECO:0000269|PubMed:26656251, ECO:0000269|PubMed:8703034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17618;
CC Evidence={ECO:0000305|PubMed:23409838, ECO:0000305|PubMed:26656251};
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:0000269|PubMed:23409838,
CC ECO:0000269|PubMed:9278457};
CC -!- ACTIVITY REGULATION: Each monomer can bind on GSH molecule but only one
CC subunit is catalytically active. {ECO:0000269|PubMed:23409838,
CC ECO:0000269|PubMed:26066610}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 uM for (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate (5-
CC HPETE) {ECO:0000269|PubMed:23409838, ECO:0000269|PubMed:9278457};
CC KM=28 uM for leukotriene A4 {ECO:0000269|PubMed:11322876};
CC KM=40 uM for leukotriene A4 {ECO:0000269|PubMed:23409838};
CC Note=kcat is 0.6 sec(-1) for leukotriene A4 as substrate
CC (PubMed:23409838). kcat is 14.3 sec(-1) for 1-chloro-2,4-
CC dinitrobenzene as substrate (PubMed:23409838). kcat is 0.1 sec(-1)
CC for 5-HPETE as substrate (PubMed:23409838).
CC {ECO:0000269|PubMed:23409838};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:26066610}.
CC -!- INTERACTION:
CC Q99735; P78348: ASIC1; NbExp=3; IntAct=EBI-11324706, EBI-79189;
CC Q99735; Q9HD36: BCL2L10; NbExp=3; IntAct=EBI-11324706, EBI-2126349;
CC Q99735; Q92843: BCL2L2; NbExp=3; IntAct=EBI-11324706, EBI-707714;
CC Q99735; P16619: CCL3L3; NbExp=3; IntAct=EBI-11324706, EBI-12934095;
CC Q99735; Q86T13: CLEC14A; NbExp=3; IntAct=EBI-11324706, EBI-17710733;
CC Q99735; O43889-2: CREB3; NbExp=3; IntAct=EBI-11324706, EBI-625022;
CC Q99735; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-11324706, EBI-6942903;
CC Q99735; Q4LDR2: CTXN3; NbExp=5; IntAct=EBI-11324706, EBI-12019274;
CC Q99735; Q96LL9: DNAJC30; NbExp=3; IntAct=EBI-11324706, EBI-8639143;
CC Q99735; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-11324706, EBI-6166686;
CC Q99735; P48165: GJA8; NbExp=3; IntAct=EBI-11324706, EBI-17458373;
CC Q99735; Q8TED1: GPX8; NbExp=3; IntAct=EBI-11324706, EBI-11721746;
CC Q99735; Q99735: MGST2; NbExp=3; IntAct=EBI-11324706, EBI-11324706;
CC Q99735; P26678: PLN; NbExp=3; IntAct=EBI-11324706, EBI-692836;
CC Q99735; Q96T60: PNKP; NbExp=3; IntAct=EBI-11324706, EBI-1045072;
CC Q99735; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-11324706, EBI-8652744;
CC Q99735; O75396: SEC22B; NbExp=3; IntAct=EBI-11324706, EBI-1058865;
CC Q99735; Q16585: SGCB; NbExp=3; IntAct=EBI-11324706, EBI-5663627;
CC Q99735; Q9UNK0: STX8; NbExp=3; IntAct=EBI-11324706, EBI-727240;
CC Q99735; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-11324706, EBI-17684533;
CC Q99735; Q6UWW9: TMEM207; NbExp=3; IntAct=EBI-11324706, EBI-13301303;
CC Q99735; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-11324706, EBI-10243654;
CC Q99735; Q15836: VAMP3; NbExp=3; IntAct=EBI-11324706, EBI-722343;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:8703034}; Multi-pass membrane protein
CC {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:8703034}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99735-2; Sequence=VSP_044538;
CC -!- TISSUE SPECIFICITY: Liver, spleen, skeletal muscle, heart, adrenals,
CC pancreas, prostate, testis, fetal liver, and fetal spleen. Very low
CC expression in lung, brain, placenta and bone marrow (PubMed:8703034).
CC Abundantly expressed in human umbilical vein endothelial cells (at
CC protein level) (PubMed:11322876). {ECO:0000269|PubMed:11322876,
CC ECO:0000269|PubMed:8703034}.
CC -!- INDUCTION: Upon ER stress with brefeldin A or with tunicamycin, MGST2
CC is down-regulated, in several non-haematopoietic cell types, during the
CC early, protective phase of the unfolded protein response (UPR), and up-
CC regulated at the late, death-promoting phase of the unfolded protein
CC response (UPR). {ECO:0000269|PubMed:26656251}.
CC -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mgst2/";
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DR EMBL; U77604; AAC51768.1; -; mRNA.
DR EMBL; CR407640; CAG28568.1; -; mRNA.
DR EMBL; AY341028; AAP88934.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC108053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025416; AAH25416.1; -; mRNA.
DR EMBL; BG519599; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS3749.1; -. [Q99735-1]
DR CCDS; CCDS56339.1; -. [Q99735-2]
DR RefSeq; NP_001191295.1; NM_001204366.1. [Q99735-1]
DR RefSeq; NP_001191297.1; NM_001204368.1. [Q99735-2]
DR RefSeq; NP_002404.1; NM_002413.4. [Q99735-1]
DR RefSeq; XP_016863700.1; XM_017008211.1. [Q99735-1]
DR RefSeq; XP_016863701.1; XM_017008212.1. [Q99735-1]
DR RefSeq; XP_016863702.1; XM_017008213.1. [Q99735-1]
DR PDB; 6SSR; X-ray; 3.80 A; A/B/C=2-147.
DR PDB; 6SSS; X-ray; 2.50 A; A/B/C/D/E/F=2-147.
DR PDB; 6SSU; X-ray; 2.50 A; A/B/C=2-147.
DR PDB; 6SSW; X-ray; 3.00 A; A/B/C=2-147.
DR PDBsum; 6SSR; -.
DR PDBsum; 6SSS; -.
DR PDBsum; 6SSU; -.
DR PDBsum; 6SSW; -.
DR AlphaFoldDB; Q99735; -.
DR SMR; Q99735; -.
DR BioGRID; 110414; 31.
DR IntAct; Q99735; 25.
DR MINT; Q99735; -.
DR STRING; 9606.ENSP00000482639; -.
DR ChEMBL; CHEMBL1743185; -.
DR DrugBank; DB01008; Busulfan.
DR DrugBank; DB00143; Glutathione.
DR SwissLipids; SLP:000001464; -.
DR iPTMnet; Q99735; -.
DR PhosphoSitePlus; Q99735; -.
DR BioMuta; MGST2; -.
DR DMDM; 2842764; -.
DR EPD; Q99735; -.
DR jPOST; Q99735; -.
DR MassIVE; Q99735; -.
DR MaxQB; Q99735; -.
DR PaxDb; Q99735; -.
DR PeptideAtlas; Q99735; -.
DR PRIDE; Q99735; -.
DR ProteomicsDB; 13587; -.
DR ProteomicsDB; 78451; -. [Q99735-1]
DR TopDownProteomics; Q99735-1; -. [Q99735-1]
DR Antibodypedia; 2759; 180 antibodies from 28 providers.
DR DNASU; 4258; -.
DR Ensembl; ENST00000265498.6; ENSP00000265498.1; ENSG00000085871.9. [Q99735-1]
DR Ensembl; ENST00000503816.1; ENSP00000423008.1; ENSG00000085871.9. [Q99735-1]
DR Ensembl; ENST00000506797.5; ENSP00000424278.1; ENSG00000085871.9. [Q99735-2]
DR Ensembl; ENST00000616265.4; ENSP00000482639.1; ENSG00000085871.9. [Q99735-1]
DR GeneID; 4258; -.
DR KEGG; hsa:4258; -.
DR MANE-Select; ENST00000265498.6; ENSP00000265498.1; NM_002413.5; NP_002404.1.
DR UCSC; uc003ihy.4; human. [Q99735-1]
DR CTD; 4258; -.
DR DisGeNET; 4258; -.
DR GeneCards; MGST2; -.
DR HGNC; HGNC:7063; MGST2.
DR HPA; ENSG00000085871; Tissue enhanced (liver).
DR MIM; 601733; gene.
DR neXtProt; NX_Q99735; -.
DR OpenTargets; ENSG00000085871; -.
DR PharmGKB; PA30792; -.
DR VEuPathDB; HostDB:ENSG00000085871; -.
DR eggNOG; ENOG502S082; Eukaryota.
DR GeneTree; ENSGT00940000160288; -.
DR HOGENOM; CLU_110291_3_0_1; -.
DR InParanoid; Q99735; -.
DR OMA; YARHKYF; -.
DR OrthoDB; 1609516at2759; -.
DR PhylomeDB; Q99735; -.
DR TreeFam; TF105328; -.
DR PathwayCommons; Q99735; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
DR SignaLink; Q99735; -.
DR BioGRID-ORCS; 4258; 6 hits in 1081 CRISPR screens.
DR ChiTaRS; MGST2; human.
DR GeneWiki; MGST2; -.
DR GenomeRNAi; 4258; -.
DR Pharos; Q99735; Tbio.
DR PRO; PR:Q99735; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q99735; protein.
DR Bgee; ENSG00000085871; Expressed in mucosa of transverse colon and 200 other tissues.
DR Genevisible; Q99735; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0043295; F:glutathione binding; IDA:UniProtKB.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:BHF-UCL.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0004464; F:leukotriene-C4 synthase activity; IDA:UniProtKB.
DR GO; GO:0006750; P:glutathione biosynthetic process; IDA:UniProtKB.
DR GO; GO:0019370; P:leukotriene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IDA:BHF-UCL.
DR GO; GO:0046466; P:membrane lipid catabolic process; IDA:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; NAS:BHF-UCL.
DR Gene3D; 1.20.120.550; -; 1.
DR InterPro; IPR001446; 5_LipOase_AP.
DR InterPro; IPR018295; FLAP/GST2/LTC4S_CS.
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.
DR PROSITE; PS01297; FLAP_GST2_LTC4S; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endoplasmic reticulum;
KW Leukotriene biosynthesis; Lipid metabolism; Lyase; Membrane; Microsome;
KW Oxidoreductase; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..147
FT /note="Microsomal glutathione S-transferase 2"
FT /id="PRO_0000217740"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 53..147
FT /note="QQNCVEFYPIFIITLWMAGWYFNQVFATCLGLVYIYGRHLYFWGYSEAAKKR
FT ITGFRLSLGILALLTLLGALGIANSFLDEYLDLNIAKKLRRQF -> HFCYLSGSGVHI
FT WPSPILLGIFRSC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044538"
FT VARIANT 101
FT /note="A -> V (in dbSNP:rs8192111)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_019997"
FT HELIX 6..32
FT /evidence="ECO:0007829|PDB:6SSS"
FT HELIX 44..73
FT /evidence="ECO:0007829|PDB:6SSS"
FT HELIX 76..99
FT /evidence="ECO:0007829|PDB:6SSS"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:6SSS"
FT HELIX 105..133
FT /evidence="ECO:0007829|PDB:6SSS"
SQ SEQUENCE 147 AA; 16621 MW; D0E89B46885D16EF CRC64;
MAGNSILLAA VSILSACQQS YFALQVGKAR LKYKVTPPAV TGSPEFERVF RAQQNCVEFY
PIFIITLWMA GWYFNQVFAT CLGLVYIYGR HLYFWGYSEA AKKRITGFRL SLGILALLTL
LGALGIANSF LDEYLDLNIA KKLRRQF
