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 22-JUL-2015, entry version 107. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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 RT leukotriene C4 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: Leukotriene C(4) = leukotriene A(4) + CC glutathione. CC -!- SUBUNIT: Homotrimer. Interacts with ALOX5AP and ALOX5 (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. Endoplasmic reticulum CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Widely expressed. CC {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; CAI25121.1; -; Genomic_DNA. DR CCDS; CCDS24631.1; -. DR PIR; S68961; S68961. DR RefSeq; NP_032547.1; NM_008521.1. DR UniGene; Mm.245151; -. 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 ProteinModelPortal; Q60860; -. DR SMR; Q60860; 2-145. DR STRING; 10090.ENSMUSP00000099833; -. DR PhosphoSite; 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 GeneTree; ENSGT00430000030964; -. DR HOGENOM; HOG000116372; -. DR HOVERGEN; HBG105513; -. DR InParanoid; Q60860; -. DR KO; K00807; -. DR TreeFam; TF105328; -. DR BRENDA; 4.4.1.20; 3474. DR Reactome; REACT_280918; Synthesis of Lipoxins (LX). DR Reactome; REACT_321024; Synthesis of Leukotrienes (LT) and Eoxins (EX). DR Reactome; REACT_327774; Synthesis of 5-eicosatetraenoic acids. DR NextBio; 291112; -. DR PRO; PR:Q60860; -. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; Q60860; -. DR CleanEx; MM_LTC4S; -. 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: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; IEA:Ensembl. 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:0004464; F:leukotriene-C4 synthase activity; IDA:MGI. DR GO; GO:0008289; F:lipid binding; IDA:MGI. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0071299; P:cellular response to vitamin A; IEA:Ensembl. DR GO; GO:0019370; P:leukotriene biosynthetic process; IBA:GO_Central. DR GO; GO:0006691; P:leukotriene metabolic process; IDA:MGI. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GOC. DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl. 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. DR InterPro; IPR001129; Membr-assoc_MAPEG. DR Pfam; PF01124; MAPEG; 1. DR PRINTS; PR00488; 5LPOXGNASEAP. DR PROSITE; PS01297; FLAP_GST2_LTC4S; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Endoplasmic reticulum; Leukotriene biosynthesis; Lyase; Membrane; KW Nucleus; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 150 Leukotriene C4 synthase. FT /FTId=PRO_0000217749. FT TOPO_DOM 1 6 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 7 27 Helical. {ECO:0000250}. FT TOPO_DOM 28 48 Lumenal. {ECO:0000250}. FT TRANSMEM 49 69 Helical. {ECO:0000250}. FT TOPO_DOM 70 73 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 74 94 Helical. {ECO:0000250}. FT TOPO_DOM 95 104 Lumenal. {ECO:0000250}. FT TRANSMEM 105 124 Helical. {ECO:0000250}. FT TOPO_DOM 125 150 Cytoplasmic. {ECO:0000250}. FT REGION 51 55 Glutathione binding. {ECO:0000250}. FT REGION 58 59 Glutathione binding. {ECO:0000250}. FT REGION 93 97 Glutathione binding. {ECO:0000250}. FT ACT_SITE 31 31 Proton donor. {ECO:0000250}. FT ACT_SITE 104 104 Proton acceptor. {ECO:0000250}. FT BINDING 30 30 Glutathione. {ECO:0000250}. FT HELIX 2 5 {ECO:0000244|PDB:4NTF}. FT HELIX 6 32 {ECO:0000244|PDB:4NTF}. FT HELIX 44 73 {ECO:0000244|PDB:4NTF}. FT HELIX 76 99 {ECO:0000244|PDB:4NTF}. FT HELIX 102 104 {ECO:0000244|PDB:4NTF}. FT HELIX 105 141 {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 //