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 05-MAY-2009, entry version 58. DE RecName: Full=Leukotriene C4 synthase; DE EC=4.4.1.20; DE AltName: Full=Leukotriene-C(4) synthase; DE Short=LTC4 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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98000279; PubMed=9342232; RX 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; RG The mouse genome sequencing consortium; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 1-27. RC TISSUE=Mast cell; RX MEDLINE=95284134; 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: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC Nucleus envelope (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- SIMILARITY: Belongs to the MAPEG family. 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 IPI; IPI00121507; -. DR PIR; S68961; S68961. DR RefSeq; NP_032547.1; -. DR UniGene; Mm.245151; -. DR PhosphoSite; Q60860; -. DR Ensembl; ENSMUSG00000020377; Mus musculus. DR GeneID; 17001; -. DR KEGG; mmu:17001; -. DR MGI; MGI:107498; Ltc4s. DR HOGENOM; Q60860; -. DR HOVERGEN; Q60860; -. DR OMA; Q60860; VLLQAYF. DR BRENDA; 4.4.1.20; 244. DR NextBio; 291112; -. DR ArrayExpress; Q60860; -. DR Bgee; Q60860; -. DR CleanEx; MM_LTC4S; -. DR GermOnline; ENSMUSG00000020377; Mus musculus. DR GO; GO:0016021; C:integral to membrane; IEA:InterPro. DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB. DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro. DR GO; GO:0004464; F:leukotriene-C4 synthase activity; IDA:MGI. DR GO; GO:0008289; F:lipid binding; IDA:MGI. DR GO; GO:0019370; P:leukotriene biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR001446; 5_LipOase_AP. DR InterPro; IPR018295; FLAP/GST2/LTC4S_CS. DR InterPro; IPR001129; MAPEG. DR Pfam; PF01124; MAPEG; 1. DR PRINTS; PR00488; 5LPOXGNASEAP. DR PROSITE; PS01297; FLAP_GST2_LTC4S; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Leukotriene biosynthesis; Lyase; Membrane; KW Nucleus; Transmembrane. FT CHAIN 1 150 Leukotriene C4 synthase. FT /FTId=PRO_0000217749. FT TRANSMEM 7 27 Potential. FT TRANSMEM 68 88 Potential. FT TRANSMEM 115 135 Potential. SQ SEQUENCE 150 AA; 16814 MW; 120ABC53892189C0 CRC64; MKDEVALLAT VTLVGVLLQA YFSLQVISAR RAFHVSPPLT SGPPEFERVF RAQVNCSEYF PLFLATLWVA GIFFHEGAAA LCGLFYLFAR LRYFQGYARS AQLRLTPLYA SARALWLLVA MAALGLLVHF LPGTLRTALF RWLQMLLPMA //