ID A0A0G2JU12_RAT Unreviewed; 128 AA. AC A0A0G2JU12; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 29-SEP-2021, entry version 33. DE SubName: Full=Microsomal glutathione S-transferase 2 {ECO:0000313|Ensembl:ENSRNOP00000068920}; GN Name=Mgst2 {ECO:0000313|Ensembl:ENSRNOP00000068920, 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, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000068920, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068920, 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} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068920}; RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004477}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. 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; AABR07010563; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; A0A0G2JU12; -. DR STRING; 10116.ENSRNOP00000017785; -. DR PhosphoSitePlus; A0A0G2JU12; -. DR jPOST; A0A0G2JU12; -. DR PaxDb; A0A0G2JU12; -. DR Ensembl; ENSRNOT00000088846; ENSRNOP00000068920; ENSRNOG00000061857. DR RGD; 1311218; Mgst2. DR eggNOG; ENOG502S082; Eukaryota. DR GeneTree; ENSGT00940000160288; -. DR OMA; HKYFWGY; -. 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 female gonad and 21 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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; -; 1. DR InterPro; IPR001446; 5_LipOase_AP. 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. 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, ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2JU12}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 40..70 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 91..112 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 128 AA; 14829 MW; 12EE88372ADD3CDE CRC64; GYFALQVGRV RLKYKIAPPA VTGSLEFERI FRAQQNSLEF YSVFIISLWM AGWYFNQVFA TCLGLLYIYA RHKYFWGYAE AAEKRIIGFR LSLGILALLT VLAVLGVASR FLDEYLDFHV AKKLKRPF //