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   27-MAR-2024, entry version 193.
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
CC         (5-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
CC         1-chloro-2,4-dinitrobenzene as substrate (PubMed:23409838). kcat is
CC         0.1 sec(-1) 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; 35.
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   SwissPalm; Q99735; -.
DR   BioMuta; MGST2; -.
DR   DMDM; 2842764; -.
DR   EPD; Q99735; -.
DR   jPOST; Q99735; -.
DR   MassIVE; Q99735; -.
DR   MaxQB; Q99735; -.
DR   PaxDb; 9606-ENSP00000482639; -.
DR   PeptideAtlas; Q99735; -.
DR   ProteomicsDB; 13587; -.
DR   ProteomicsDB; 78451; -. [Q99735-1]
DR   Pumba; Q99735; -.
DR   TopDownProteomics; Q99735-1; -. [Q99735-1]
DR   Antibodypedia; 2759; 204 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   AGR; HGNC:7063; -.
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; HKYFWGY; -.
DR   OrthoDB; 5396066at2759; -.
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; 7 hits in 1161 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 202 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
DR   Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 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   PANTHER; PTHR10250; MICROSOMAL GLUTATHIONE S-TRANSFERASE; 1.
DR   PANTHER; PTHR10250:SF13; MICROSOMAL GLUTATHIONE S-TRANSFERASE 2; 1.
DR   Pfam; PF01124; MAPEG; 1.
DR   PRINTS; PR00488; 5LPOXGNASEAP.
DR   SUPFAM; SSF161084; MAPEG domain-like; 1.
DR   PROSITE; PS01297; FLAP_GST2_LTC4S; 1.
DR   Genevisible; Q99735; HS.
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
//