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Leukotriene C4 synthase (LTC4 synthase) (EC 4.4.1.20) (Leukotriene-C(4) synthase)

 LTC4S_HUMAN             Reviewed;         150 AA.
Q16873; Q8N6P0; Q9UC73; Q9UD18;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 161.
RecName: Full=Leukotriene C4 synthase;
Short=LTC4 synthase;
EC=4.4.1.20;
AltName: Full=Leukotriene-C(4) synthase;
Name=LTC4S;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-22 AND 35-48.
TISSUE=Bone marrow;
PubMed=8052639; DOI=10.1073/pnas.91.16.7663;
Lam B.K., Penrose J.F., Freeman G.J., Austen K.F.;
"Expression cloning of a cDNA for human leukotriene C4 synthase, an
integral membrane protein conjugating reduced glutathione to
leukotriene A4.";
Proc. Natl. Acad. Sci. U.S.A. 91:7663-7667(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7937884; DOI=10.1073/pnas.91.21.9745;
Welsch D.J., Creely D.P., Hauser S.D., Mathis K.J., Krivi G.G.,
Isakson P.C.;
"Molecular cloning and expression of human leukotriene-C4 synthase.";
Proc. Natl. Acad. Sci. U.S.A. 91:9745-9749(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8626689; DOI=10.1074/jbc.271.19.11356;
Penrose J.F., Spector J., Baldasaro M., Xu K., Boyce J., Arm J.P.,
Austen K.F., Lam B.K.;
"Molecular cloning of the gene for human leukotriene C4 synthase.
Organization, nucleotide sequence, and chromosomal localization to
5q35.";
J. Biol. Chem. 271:11356-11361(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8898379;
Bigby T.D., Hodulik C.R., Arden K.C., Fu L.;
"Molecular cloning of the human leukotriene C4 synthase gene and
assignment to chromosome 5q35.";
Mol. Med. 2:637-646(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-142.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 1-35.
PubMed=8446623; DOI=10.1073/pnas.90.5.2015;
Nicholson D.W., Ali A., Vaillancourt J.P., Calaycay J.R.,
Mumford R.A., Zamboni R.J., Ford-Hutchinson A.W.;
"Purification to homogeneity and the N-terminal sequence of human
leukotriene C4 synthase: a homodimeric glutathione S-transferase
composed of 18-kDa subunits.";
Proc. Natl. Acad. Sci. U.S.A. 90:2015-2019(1993).
[7]
PROTEIN SEQUENCE OF 1-19, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Lung;
PubMed=7599836; DOI=10.1164/ajrccm.152.1.7599836;
Penrose J.F., Spector J., Lam B.K., Friend D.S., Xu K., Jack R.M.,
Austen K.F.;
"Purification of human lung leukotriene C4 synthase and preparation of
a polyclonal antibody.";
Am. J. Respir. Crit. Care Med. 152:283-289(1995).
[8]
PROTEIN SEQUENCE OF 1-17.
TISSUE=Monocyte;
PubMed=7766706; DOI=10.1016/0005-2760(95)00031-7;
Goppelt-Struebe M.;
"Two step purification of human and murine leukotriene C4 synthase.";
Biochim. Biophys. Acta 1256:257-261(1995).
[9]
INVOLVEMENT IN LTC4 SYNTHASE DEFICIENCY.
PubMed=9820300; DOI=10.1016/S0140-6736(98)01186-6;
Mayatepek E., Flock B.;
"Leukotriene C4-synthesis deficiency: a new inborn error of metabolism
linked to a fatal developmental syndrome.";
Lancet 352:1514-1517(1998).
[10]
INVOLVEMENT IN LTC4 SYNTHASE DEFICIENCY.
PubMed=10896305; DOI=10.1023/A:1005664204956;
Mayatepek E., Zelezny R., Lehmann W.D., Hammond J.W., Hoffmann G.F.;
"Defects in the synthesis of cysteinyl leukotrienes: a new group of
inborn errors of metabolism.";
J. Inherit. Metab. Dis. 23:404-408(2000).
[11]
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=12023288; DOI=10.1074/jbc.M203074200;
Christmas P., Weber B.M., McKee M., Brown D., Soberman R.J.;
"Membrane localization and topology of leukotriene C4 synthase.";
J. Biol. Chem. 277:28902-28908(2002).
[12]
INTERACTION WITH ALOX5AP AND ALOX5, AND SUBCELLULAR LOCATION.
PubMed=19233132; DOI=10.1016/j.bbrc.2009.02.074;
Strid T., Svartz J., Franck N., Hallin E., Ingelsson B.,
Soederstroem M., Hammarstroem S.;
"Distinct parts of leukotriene C(4) synthase interact with 5-
lipoxygenase and 5-lipoxygenase activating protein.";
Biochem. Biophys. Res. Commun. 381:518-522(2009).
[13]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
ACTIVE SITE, TOPOLOGY, AND SUBUNIT.
PubMed=17632548; DOI=10.1038/nature05936;
Ago H., Kanaoka Y., Irikura D., Lam B.K., Shimamura T., Austen K.F.,
Miyano M.;
"Crystal structure of a human membrane protein involved in cysteinyl
leukotriene biosynthesis.";
Nature 448:609-612(2007).
[14]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-150 IN COMPLEX WITH
GLUTATHIONE, SUBUNIT, AND TOPOLOGY.
PubMed=17632546; DOI=10.1038/nature06009;
Martinez Molina D., Wetterholm A., Kohl A., McCarthy A.A.,
Niegowski D., Ohlson E., Hammarberg T., Eshaghi S., Haeggstroem J.Z.,
Nordlund P.;
"Structural basis for synthesis of inflammatory mediators by human
leukotriene C4 synthase.";
Nature 448:613-616(2007).
-!- FUNCTION: Catalyzes the conjugation of leukotriene A4 with reduced
glutathione to form leukotriene C4.
-!- CATALYTIC ACTIVITY: Leukotriene C(4) = leukotriene A(4) +
glutathione.
-!- SUBUNIT: Homotrimer. Interacts with ALOX5AP and ALOX5.
{ECO:0000269|PubMed:17632546, ECO:0000269|PubMed:17632548,
ECO:0000269|PubMed:19233132}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-12241118, EBI-12241118;
-!- SUBCELLULAR LOCATION: Nucleus outer membrane; Multi-pass membrane
protein. Endoplasmic reticulum membrane; Multi-pass membrane
protein.
-!- TISSUE SPECIFICITY: Detected in lung, platelets and the
myelogenous leukemia cell line KG-1 (at protein level). LTC4S
activity is present in eosinophils, basophils, mast cells, certain
phagocytic mononuclear cells, endothelial cells, vascular smooth
muscle cells and platelets. {ECO:0000269|PubMed:7599836}.
-!- DISEASE: Note=LTC4 synthase deficiency is associated with a
neurometabolic developmental disorder characterized by muscular
hypotonia, psychomotor retardation, failure to thrive, and
microcephaly.
-!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U09353; AAA20467.1; -; mRNA.
EMBL; U11552; AAA50555.1; -; mRNA.
EMBL; U50136; AAC50476.1; -; Genomic_DNA.
EMBL; U62025; AAB06723.1; -; Genomic_DNA.
EMBL; BC029498; AAH29498.1; -; mRNA.
CCDS; CCDS34316.1; -.
PIR; I38595; I38595.
PIR; JC5398; JC5398.
RefSeq; NP_665874.1; NM_145867.1.
UniGene; Hs.706741; -.
PDB; 2PNO; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-150.
PDB; 2UUH; X-ray; 2.15 A; A=2-150.
PDB; 2UUI; X-ray; 2.00 A; A=2-150.
PDB; 3B29; X-ray; 3.20 A; A=1-150.
PDB; 3HKK; X-ray; 2.90 A; A=2-150.
PDB; 3LEO; X-ray; 2.10 A; A=2-150.
PDB; 3PCV; X-ray; 1.90 A; A=1-150.
PDB; 4BPM; X-ray; 2.08 A; A=131-150.
PDB; 4J7T; X-ray; 3.20 A; A=2-150.
PDB; 4J7Y; X-ray; 2.90 A; A=2-150.
PDB; 4JC7; X-ray; 2.70 A; A=2-150.
PDB; 4JCZ; X-ray; 2.75 A; A=2-150.
PDB; 4JRZ; X-ray; 2.40 A; A=2-150.
PDB; 4WAB; X-ray; 2.70 A; A=130-150.
PDB; 5HV9; X-ray; 3.00 A; A=2-150.
PDBsum; 2PNO; -.
PDBsum; 2UUH; -.
PDBsum; 2UUI; -.
PDBsum; 3B29; -.
PDBsum; 3HKK; -.
PDBsum; 3LEO; -.
PDBsum; 3PCV; -.
PDBsum; 4BPM; -.
PDBsum; 4J7T; -.
PDBsum; 4J7Y; -.
PDBsum; 4JC7; -.
PDBsum; 4JCZ; -.
PDBsum; 4JRZ; -.
PDBsum; 4WAB; -.
PDBsum; 5HV9; -.
ProteinModelPortal; Q16873; -.
SMR; Q16873; -.
BioGrid; 110234; 4.
DIP; DIP-48473N; -.
IntAct; Q16873; 1.
STRING; 9606.ENSP00000292596; -.
BindingDB; Q16873; -.
ChEMBL; CHEMBL1743183; -.
DrugBank; DB00143; Glutathione.
GuidetoPHARMACOLOGY; 1391; -.
SwissLipids; SLP:000001452; -.
iPTMnet; Q16873; -.
PhosphoSitePlus; Q16873; -.
DMDM; 2833283; -.
PaxDb; Q16873; -.
PeptideAtlas; Q16873; -.
PRIDE; Q16873; -.
DNASU; 4056; -.
Ensembl; ENST00000292596; ENSP00000292596; ENSG00000213316.
Ensembl; ENST00000639087; ENSP00000492334; ENSG00000283887.
GeneID; 4056; -.
KEGG; hsa:4056; -.
UCSC; uc003mko.4; human.
CTD; 4056; -.
DisGeNET; 4056; -.
EuPathDB; HostDB:ENSG00000213316.9; -.
GeneCards; LTC4S; -.
HGNC; HGNC:6719; LTC4S.
MalaCards; LTC4S; -.
MIM; 246530; gene.
neXtProt; NX_Q16873; -.
OpenTargets; ENSG00000213316; -.
Orphanet; 79507; Hypotonia - failure to thrive - microcephaly.
PharmGKB; PA235; -.
eggNOG; ENOG410IX5F; Eukaryota.
eggNOG; ENOG4111JV7; LUCA.
GeneTree; ENSGT00430000030964; -.
HOGENOM; HOG000116372; -.
HOVERGEN; HBG105513; -.
InParanoid; Q16873; -.
KO; K00807; -.
OMA; AGIFFHQ; -.
OrthoDB; EOG091G12NW; -.
PhylomeDB; Q16873; -.
TreeFam; TF105328; -.
BioCyc; MetaCyc:HS08566-MONOMER; -.
BRENDA; 4.4.1.20; 2681.
Reactome; R-HSA-2142688; Synthesis of 5-eicosatetraenoic acids.
Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-HSA-2142700; Synthesis of Lipoxins (LX).
SABIO-RK; Q16873; -.
SignaLink; Q16873; -.
EvolutionaryTrace; Q16873; -.
GeneWiki; Leukotriene_C4_synthase; -.
GenomeRNAi; 4056; -.
PRO; PR:Q16873; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000213316; -.
CleanEx; HS_LTC4S; -.
ExpressionAtlas; Q16873; baseline.
Genevisible; Q16873; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; TAS:ProtInc.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
GO; GO:0004602; F:glutathione peroxidase activity; IBA:GO_Central.
GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004464; F:leukotriene-C4 synthase activity; IDA:MGI.
GO; GO:0008289; F:lipid binding; IDA:MGI.
GO; GO:0019370; P:leukotriene biosynthetic process; IBA:GO_Central.
GO; GO:0006691; P:leukotriene metabolic process; IDA:MGI.
GO; GO:2001300; P:lipoxin metabolic process; TAS:Reactome.
GO; GO:0019372; P:lipoxygenase pathway; TAS:Reactome.
Gene3D; 1.20.120.550; -; 1.
InterPro; IPR001446; 5_LipOase_AP.
InterPro; IPR018295; FLAP/GST2/LTC4S_CS.
InterPro; IPR023352; MAPEG-like_dom_sf.
InterPro; IPR001129; Membr-assoc_MAPEG.
Pfam; PF01124; MAPEG; 1.
PRINTS; PR00488; 5LPOXGNASEAP.
SUPFAM; SSF161084; SSF161084; 1.
PROSITE; PS01297; FLAP_GST2_LTC4S; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Endoplasmic reticulum; Leukotriene biosynthesis; Lyase; Membrane;
Nucleus; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 150 Leukotriene C4 synthase.
/FTId=PRO_0000217748.
TOPO_DOM 1 6 Cytoplasmic.
TRANSMEM 7 27 Helical.
TOPO_DOM 28 48 Lumenal.
TRANSMEM 49 69 Helical.
TOPO_DOM 70 73 Cytoplasmic.
TRANSMEM 74 94 Helical.
TOPO_DOM 95 104 Lumenal.
TRANSMEM 105 124 Helical.
TOPO_DOM 125 150 Cytoplasmic.
REGION 51 55 Glutathione binding.
REGION 58 59 Glutathione binding.
REGION 93 97 Glutathione binding.
ACT_SITE 31 31 Proton donor.
{ECO:0000305|PubMed:17632548}.
ACT_SITE 104 104 Proton acceptor.
{ECO:0000305|PubMed:17632548}.
BINDING 30 30 Glutathione.
{ECO:0000269|PubMed:17632546,
ECO:0000269|PubMed:17632548}.
VARIANT 142 142 R -> Q (in dbSNP:rs11541078).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_042736.
CONFLICT 21 21 Y -> G (in Ref. 6; AA sequence).
{ECO:0000305}.
HELIX 2 32 {ECO:0000244|PDB:3PCV}.
HELIX 44 73 {ECO:0000244|PDB:3PCV}.
HELIX 76 99 {ECO:0000244|PDB:3PCV}.
HELIX 101 104 {ECO:0000244|PDB:3PCV}.
HELIX 105 145 {ECO:0000244|PDB:3PCV}.
SEQUENCE 150 AA; 16567 MW; 04E269B475063037 CRC64;
MKDEVALLAA VTLLGVLLQA YFSLQVISAR RAFRVSPPLT TGPPEFERVY RAQVNCSEYF
PLFLATLWVA GIFFHEGAAA LCGLVYLFAR LRYFQGYARS AQLRLAPLYA SARALWLLVA
LAALGLLAHF LPAALRAALL GRLRTLLPWA


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