ID LTC4S_MOUSE Reviewed; 150 AA. AC Q60860; Q5SVR7; Q9QVS1; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 26-FEB-2020, entry version 133. DE RecName: Full=Leukotriene C4 synthase; DE Short=LTC4 synthase; DE EC=4.4.1.20; DE AltName: Full=Leukotriene-C(4) synthase; GN Name=Ltc4s; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9342232; DOI=10.1111/j.1432-1033.1997.00807.x; RA Penrose J.F., Baldasaro M.H., Webster M., Xu K., Austen K.F., Lam B.K.; RT "Molecular cloning of the gene for mouse leukotriene-C4 synthase."; RL Eur. J. Biochem. 248:807-813(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP PROTEIN SEQUENCE OF 1-27. RC TISSUE=Mast cell; RX PubMed=7766706; DOI=10.1016/0005-2760(95)00031-7; RA Goppelt-Struebe M.; RT "Two step purification of human and murine leukotriene C4 synthase."; RL Biochim. Biophys. Acta 1256:257-261(1995). RN [4] RP IDENTIFICATION, AND TISSUE SPECIFICITY. RX PubMed=8706658; DOI=10.1111/j.1432-1033.1996.0606w.x; RA Lam B.K., Penrose J.F., Rokach J., Xu K., Baldasaro M.H., Austen K.F.; RT "Molecular cloning, expression and characterization of mouse leukotriene C4 RT synthase."; RL Eur. J. Biochem. 238:606-612(1996). CC -!- FUNCTION: Catalyzes the conjugation of leukotriene A4 with reduced CC glutathione to form leukotriene C4. 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 -!- SUBUNIT: Homotrimer. Interacts with ALOX5AP and ALOX5 (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. Endoplasmic reticulum membrane CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8706658}. CC -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}. 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; U27195; AAA75042.1; -; mRNA. DR EMBL; AL627187; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS24631.1; -. DR PIR; S68961; S68961. DR RefSeq; NP_032547.1; NM_008521.2. DR PDB; 4NTA; X-ray; 2.70 A; A=2-150. DR PDB; 4NTB; X-ray; 2.70 A; A=2-150. DR PDB; 4NTF; X-ray; 2.65 A; A=2-150. DR PDBsum; 4NTA; -. DR PDBsum; 4NTB; -. DR PDBsum; 4NTF; -. DR SMR; Q60860; -. DR STRING; 10090.ENSMUSP00000099833; -. DR SwissLipids; SLP:000001453; -. DR iPTMnet; Q60860; -. DR PhosphoSitePlus; Q60860; -. DR MaxQB; Q60860; -. DR PaxDb; Q60860; -. DR PeptideAtlas; Q60860; -. DR PRIDE; Q60860; -. DR Ensembl; ENSMUST00000102772; ENSMUSP00000099833; ENSMUSG00000020377. DR GeneID; 17001; -. DR KEGG; mmu:17001; -. DR UCSC; uc007isa.1; mouse. DR CTD; 4056; -. DR MGI; MGI:107498; Ltc4s. DR eggNOG; ENOG410IX5F; Eukaryota. DR eggNOG; ENOG4111JV7; LUCA. DR GeneTree; ENSGT00940000160738; -. DR HOGENOM; CLU_110291_3_0_1; -. DR InParanoid; Q60860; -. DR KO; K00807; -. DR OMA; IFRAQAN; -. DR OrthoDB; 1609516at2759; -. DR TreeFam; TF105328; -. DR BRENDA; 4.4.1.20; 3474. DR Reactome; R-MMU-2142688; Synthesis of 5-eicosatetraenoic acids. DR Reactome; R-MMU-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX). DR Reactome; R-MMU-2142700; Synthesis of Lipoxins (LX). DR Reactome; R-MMU-9026762; Biosynthesis of maresin conjugates in tissue regeneration (MCTR). DR Reactome; R-MMU-9026766; Biosynthesis of protectin and resolvin conjugates in tissue regeneration (PCTR and RCTR). DR ChiTaRS; Ltc4s; mouse. DR PRO; PR:Q60860; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q60860; protein. DR Bgee; ENSMUSG00000020377; Expressed in epididymal fat pad and 76 other tissues. DR ExpressionAtlas; Q60860; baseline and differential. DR Genevisible; Q60860; MM. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. 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:MGI. DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB. DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro. DR GO; GO:0043295; F:glutathione binding; ISO:MGI. DR GO; GO:0004602; F:glutathione peroxidase activity; IBA:GO_Central. DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0004464; F:leukotriene-C4 synthase activity; IDA:MGI. DR GO; GO:0008289; F:lipid binding; IDA:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0019370; P:leukotriene biosynthetic process; ISO:MGI. DR GO; GO:0006691; P:leukotriene metabolic process; IDA:MGI. 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; Direct protein sequencing; Endoplasmic reticulum; KW Leukotriene biosynthesis; Lyase; Membrane; Nucleus; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1..150 FT /note="Leukotriene C4 synthase" FT /id="PRO_0000217749" FT TOPO_DOM 1..6 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 7..27 FT /note="Helical" FT /evidence="ECO:0000250" FT TOPO_DOM 28..48 FT /note="Lumenal" FT /evidence="ECO:0000250" FT TRANSMEM 49..69 FT /note="Helical" FT /evidence="ECO:0000250" FT TOPO_DOM 70..73 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 74..94 FT /note="Helical" FT /evidence="ECO:0000250" FT TOPO_DOM 95..104 FT /note="Lumenal" FT /evidence="ECO:0000250" FT TRANSMEM 105..124 FT /note="Helical" FT /evidence="ECO:0000250" FT TOPO_DOM 125..150 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT REGION 51..55 FT /note="Glutathione binding" FT /evidence="ECO:0000250" FT REGION 58..59 FT /note="Glutathione binding" FT /evidence="ECO:0000250" FT REGION 93..97 FT /note="Glutathione binding" FT /evidence="ECO:0000250" FT ACT_SITE 31 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 104 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT BINDING 30 FT /note="Glutathione" FT /evidence="ECO:0000250" FT HELIX 2..5 FT /evidence="ECO:0000244|PDB:4NTF" FT HELIX 6..32 FT /evidence="ECO:0000244|PDB:4NTF" FT HELIX 44..73 FT /evidence="ECO:0000244|PDB:4NTF" FT HELIX 76..99 FT /evidence="ECO:0000244|PDB:4NTF" FT HELIX 102..104 FT /evidence="ECO:0000244|PDB:4NTF" FT HELIX 105..141 FT /evidence="ECO:0000244|PDB:4NTF" SQ SEQUENCE 150 AA; 16814 MW; 120ABC53892189C0 CRC64; MKDEVALLAT VTLVGVLLQA YFSLQVISAR RAFHVSPPLT SGPPEFERVF RAQVNCSEYF PLFLATLWVA GIFFHEGAAA LCGLFYLFAR LRYFQGYARS AQLRLTPLYA SARALWLLVA MAALGLLVHF LPGTLRTALF RWLQMLLPMA //