ID A0A0G2JU12_RAT Unreviewed; 119 AA. AC A0A0G2JU12; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 2. DT 22-FEB-2023, entry version 39. DE SubName: Full=Microsomal glutathione S-transferase 2 {ECO:0000313|Ensembl:ENSRNOP00000068920.2}; 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 (OCT-2022) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004477}. 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.ENSRNOP00000017785; -. DR PhosphoSitePlus; A0A0G2JU12; -. DR jPOST; A0A0G2JU12; -. DR PaxDb; A0A0G2JU12; -. 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 OMA; YARHKYF; -. DR Reactome; R-RNO-156590; Glutathione conjugation. DR Reactome; R-RNO-5423646; Aflatoxin activation and detoxification. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000061857; Expressed in ovary and 19 other tissues. DR GO; GO:0005737; C:cytoplasm; IDA:RGD. 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:InterPro. 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 GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD. DR Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1. DR InterPro; IPR001446; 5_LipOase_AP. 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 Leukotriene biosynthesis {ECO:0000256|ARBA:ARBA00022751}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2JU12}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; 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 //