ID A0A0G2JU12_RAT Unreviewed; 119 AA. AC A0A0G2JU12; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 2. DT 02-OCT-2024, entry version 48. DE RecName: Full=Microsomal glutathione S-transferase 2 {ECO:0000256|RuleBase:RU369123}; DE Short=Microsomal GST-2 {ECO:0000256|RuleBase:RU369123}; DE Short=Microsomal GST-II {ECO:0000256|RuleBase:RU369123}; DE EC=1.11.1.- {ECO:0000256|RuleBase:RU369123}; DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU369123}; DE EC=4.4.1.20 {ECO:0000256|RuleBase:RU369123}; DE AltName: Full=Glutathione peroxidase MGST2 {ECO:0000256|RuleBase:RU369123}; DE AltName: Full=Leukotriene C4 synthase MGST2 {ECO:0000256|RuleBase:RU369123}; DE AltName: Full=Microsomal glutathione S-transferase II {ECO:0000256|RuleBase:RU369123}; GN Name=Mgst2 {ECO:0000313|Ensembl:ENSRNOP00000068920.2, GN ECO:0000313|RGD:1311218}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000068920.2, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000068920.2, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068920.2, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000068920.2} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068920.2}; RG Ensembl; RL Submitted (JUN-2024) to UniProtKB. CC -!- FUNCTION: Catalyzes several different glutathione-dependent reactions. CC Catalyzes the glutathione-dependent reduction of lipid hydroperoxides, CC such as 5-HPETE. Has glutathione transferase activity, toward CC xenobiotic electrophiles, such as 1-chloro-2, 4-dinitrobenzene (CDNB). CC Catalyzes also the conjugation of leukotriene A4 with reduced CC glutathione to form leukotriene C4 (LTC4). Involved in oxidative DNA CC damage induced by ER stress and anticancer agents by activating LTC4 CC biosynthetic machinery in nonimmune cells. CC {ECO:0000256|RuleBase:RU369123}. 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:0000256|RuleBase:RU369123}; 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:0000256|RuleBase:RU369123}; 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:0000256|RuleBase:RU369123}; 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:0000256|RuleBase:RU369123}; CC -!- SUBUNIT: Homotrimer. {ECO:0000256|RuleBase:RU369123}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|RuleBase:RU369123}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU369123}. Microsome membrane CC {ECO:0000256|RuleBase:RU369123}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU369123}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the MAPEG family. CC {ECO:0000256|RuleBase:RU369123}. 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 AlphaFoldDB; A0A0G2JU12; -. DR STRING; 10116.ENSRNOP00000068920; -. DR PhosphoSitePlus; A0A0G2JU12; -. DR jPOST; A0A0G2JU12; -. DR PaxDb; 10116-ENSRNOP00000017785; -. DR Ensembl; ENSRNOT00000088846.2; ENSRNOP00000068920.2; ENSRNOG00000061857.2. DR AGR; RGD:1311218; -. DR RGD; 1311218; Mgst2. DR VEuPathDB; HostDB:ENSRNOG00000061857; -. DR eggNOG; ENOG502S082; Eukaryota. DR GeneTree; ENSGT00940000160288; -. DR InParanoid; A0A0G2JU12; -. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000061857; Expressed in ovary and 19 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0008047; F:enzyme activator activity; IEA:UniProtKB-UniRule. DR GO; GO:0043295; F:glutathione binding; ISO:RGD. DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:RGD. DR GO; GO:0004364; F:glutathione transferase activity; IDA:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0004464; F:leukotriene-C4 synthase activity; IDA:RGD. DR GO; GO:0006750; P:glutathione biosynthetic process; ISO:RGD. DR GO; GO:0019370; P:leukotriene biosynthetic process; ISO:RGD. DR GO; GO:0006629; P:lipid metabolic process; ISO:RGD. DR GO; GO:0046466; P:membrane lipid catabolic process; ISO:RGD. DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD. DR Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1. DR InterPro; IPR001446; 5_LipOase_AP. DR InterPro; IPR050997; MAPEG. 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. PE 1: Evidence at protein level; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, KW ECO:0000256|RuleBase:RU369123}; KW Leukotriene biosynthesis {ECO:0000256|ARBA:ARBA00022751, KW ECO:0000256|RuleBase:RU369123}; KW Lipid metabolism {ECO:0000256|RuleBase:RU369123}; KW Lyase {ECO:0000256|RuleBase:RU369123}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Microsome {ECO:0000256|RuleBase:RU369123}; KW Oxidoreductase {ECO:0000256|RuleBase:RU369123}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2JU12}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transferase {ECO:0000256|RuleBase:RU369123}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}. SQ SEQUENCE 119 AA; 13408 MW; BCF22317314A0203 CRC64; MAGDSSLLAA VSLLSACQQS YFALQVGRVR LKYKIAPPAV TGSLEFERIF RAQQNSLEFY SVFIISLWMA GWYFNQEFPM MDLNEADCLE EKVLGFCNLS GSPVHIRPSQ VFLGLCRSR //