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Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase)

 LCAT_HUMAN              Reviewed;         440 AA.
P04180; Q53XQ3;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
12-SEP-2018, entry version 192.
RecName: Full=Phosphatidylcholine-sterol acyltransferase;
EC=2.3.1.43 {ECO:0000269|PubMed:10222237, ECO:0000269|PubMed:10329423, ECO:0000269|PubMed:14636062, ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:25727495, ECO:0000269|PubMed:26195816, ECO:0000269|PubMed:3458198};
AltName: Full=Lecithin-cholesterol acyltransferase;
AltName: Full=Phospholipid-cholesterol acyltransferase;
Flags: Precursor;
Name=LCAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=3797244; DOI=10.1093/nar/14.23.9397;
McLean J., Wion K., Drayna D., Fielding C., Lawn R.;
"Human lecithin-cholesterol acyltransferase gene: complete gene
sequence and sites of expression.";
Nucleic Acids Res. 14:9397-9406(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-39; 172-182;
269-280 AND 387-406, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=3458198; DOI=10.1073/pnas.83.8.2335;
McLean J., Fielding C., Drayna D., Dieplinger H., Baer B., Kohr W.,
Henzel W., Lawn R.;
"Cloning and expression of human lecithin-cholesterol acyltransferase
cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 83:2335-2339(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Nickerson D.A., Smith J.D., Fullerton S.M., Clark A.G., Stengard J.H.,
Salomaa V., Boerwinkle E., Sing C.F., Weiss K.M.;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 17-440.
PubMed=2823898; DOI=10.1016/0167-4781(87)90066-2;
Tata F., Chaves M.E., Markham A.F., Scrace G.D., Waterfield M.D.,
McIntyre N., Williamson R., Humphries S.E.;
"The isolation and characterisation of cDNA and genomic clones for
human lecithin: cholesterol acyltransferase.";
Biochim. Biophys. Acta 910:142-148(1987).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-440.
PubMed=2823801; DOI=10.1016/0006-291X(87)91090-4;
Rogne S., Skretting G., Larsen F., Myklebost O., Mevag B.,
Carlson L.A., Holmquist L., Gjone E., Prydz H.;
"The isolation and characterisation of a cDNA clone for human
lecithin:cholesterol acyl transferase and its use to analyse the genes
in patients with LCAT deficiency and fish eye disease.";
Biochem. Biophys. Res. Commun. 148:161-169(1987).
[10]
PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
PubMed=2880847;
Yang C., Manoogian D., Pao Q., Lee F., Knapp R.D., Gotto A.M. Jr.,
Pownall H.J.;
"Lecithin:cholesterol acyltransferase. Functional regions and a
structural model of the enzyme.";
J. Biol. Chem. 262:3086-3091(1987).
[11]
GLYCOSYLATION AT ASN-44; ASN-108; ASN-296; ASN-408; THR-431 AND
SER-433, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=7613477; DOI=10.1002/pro.5560040419;
Schindler P.A., Settineri C.A., Collet X., Fielding C.J.,
Burlingame A.L.;
"Site-specific detection and structural characterization of the
glycosylation of human plasma proteins lecithin:cholesterol
acyltransferase and apolipoprotein D using HPLC/electrospray mass
spectrometry and sequential glycosidase digestion.";
Protein Sci. 4:791-803(1995).
[12]
CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=8820107;
Subbaiah P.V., Liu M.;
"Comparative studies on the substrate specificity of
lecithin:cholesterol acyltransferase towards the molecular species of
phosphatidylcholine in the plasma of 14 vertebrates.";
J. Lipid Res. 37:113-122(1996).
[13]
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
PubMed=10222237; DOI=10.1006/bbrc.1999.0601;
Collet X., Francone O., Besnard F., Fielding C.J.;
"Secretion of lecithin:cholesterol acyltransferase by brain neuroglial
cell lines.";
Biochem. Biophys. Res. Commun. 258:73-76(1999).
[14]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10329423; DOI=10.1006/bbrc.1999.0690;
Kosek A.B., Durbin D., Jonas A.;
"Binding affinity and reactivity of lecithin cholesterol
acyltransferase with native lipoproteins.";
Biochem. Biophys. Res. Commun. 258:548-551(1999).
[15]
FUNCTION IN HIGH-DENSITY LIPOPROTEIN PARTICLE REMODELING.
PubMed=10722751; DOI=10.1074/jbc.275.12.9019;
Clay M.A., Pyle D.H., Rye K.A., Barter P.J.;
"Formation of spherical, reconstituted high density lipoproteins
containing both apolipoproteins A-I and A-II is mediated by
lecithin:cholesterol acyltransferase.";
J. Biol. Chem. 275:9019-9025(2000).
[16]
SUBSTRATE SPECIFICITY, MUTAGENESIS OF GLU-173, FUNCTION, AND CATALYTIC
ACTIVITY.
PubMed=14636062; DOI=10.1021/bi035460u;
Zhao Y., Wang J., Gebre A.K., Chisholm J.W., Parks J.S.;
"Negative charge at amino acid 149 is the molecular determinant for
substrate specificity of lecithin: cholesterol acyltransferase for
phosphatidylcholine containing 20-carbon sn-2 fatty acyl chains.";
Biochemistry 42:13941-13949(2003).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44 AND ASN-296.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[18]
ASSOCIATION WITH OBESITY.
PubMed=17950106; DOI=10.1016/j.metabol.2007.06.022;
Bajnok L., Seres I., Varga Z., Jeges S., Peti A., Karanyi Z.,
Juhasz A., Csongradi E., Mezosi E., Nagy E.V., Paragh G.;
"Relationship of endogenous hyperleptinemia to serum paraoxonase 1,
cholesteryl ester transfer protein, and lecithin cholesterol
acyltransferase in obese individuals.";
Metabolism 56:1542-1549(2007).
[19]
ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=19065001; DOI=10.1194/jlr.M800584-JLR200;
Hirsch-Reinshagen V., Donkin J., Stukas S., Chan J., Wilkinson A.,
Fan J., Parks J.S., Kuivenhoven J.A., Lutjohann D., Pritchard H.,
Wellington C.L.;
"LCAT synthesized by primary astrocytes esterifies cholesterol on
glia-derived lipoproteins.";
J. Lipid Res. 50:885-893(2009).
[20]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-440, DISULFIDE BONDS,
FUNCTION, CATALYTIC ACTIVITY, AND GLYCOSYLATION AT ASN-108; ASN-296
AND ASN-408.
PubMed=26195816; DOI=10.1194/jlr.M059873;
Piper D.E., Romanow W.G., Gunawardane R.N., Fordstrom P.,
Masterman S., Pan O., Thibault S.T., Zhang R., Meininger D.,
Schwarz M., Wang Z., King C., Zhou M., Walker N.P.;
"The high resolution crystal structure of human LCAT.";
J. Lipid Res. 56:1711-1719(2015).
[21]
X-RAY CRYSTALLOGRAPHY (8.69 ANGSTROMS) OF 45-421, CATALYTIC ACTIVITY,
DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-108; ASN-296 AND ASN-408.
PubMed=25727495; DOI=10.1038/ncomms7250;
Glukhova A., Hinkovska-Galcheva V., Kelly R., Abe A., Shayman J.A.,
Tesmer J.J.;
"Structure and function of lysosomal phospholipase A2 and
lecithin:cholesterol acyltransferase.";
Nat. Commun. 6:6250-6250(2015).
[22]
VARIANT FED LEU-34.
PubMed=1571050; DOI=10.1016/0006-291X(92)91772-I;
Skretting G., Prydz H.;
"An amino acid exchange in exon I of the human lecithin: cholesterol
acyltransferase (LCAT) gene is associated with fish eye disease.";
Biochem. Biophys. Res. Commun. 182:583-587(1992).
[23]
VARIANTS FED ILE-147 AND MET-371.
PubMed=1737840; DOI=10.1172/JCI115612;
Klein H.-G., Lohse P., Pritchard P.H., Bojanovski D., Schmidt H.,
Brewer H.B. Jr.;
"Two different allelic mutations in the lecithin-cholesterol
acyltransferase gene associated with the fish eye syndrome. Lecithin-
cholesterol acyltransferase (Thr123-->Ile) and lecithin-cholesterol
acyltransferase (Thr347-->Met).";
J. Clin. Invest. 89:499-506(1992).
[24]
VARIANT LCATD TRP-171.
PubMed=2370048; DOI=10.1007/BF00193195;
Taramelli R., Pontoglio M., Candiani G., Ottolenghi S., Dieplinger H.,
Catapano A., Albers J., Vergani C., McLean J.;
"Lecithin cholesterol acyl transferase deficiency: molecular analysis
of a mutated allele.";
Hum. Genet. 85:195-199(1990).
[25]
VARIANTS LCATD LYS-252 AND ILE-317.
PubMed=1681161; DOI=10.1016/0140-6736(91)90665-C;
Gotoda T., Yamada N., Murase T., Sakuma M., Murayama N., Shimano H.,
Kozaki K., Albers J.J., Yazaki Y., Akanuma Y.;
"Differential phenotypic expression by three mutant alleles in
familial lecithin:cholesterol acyltransferase deficiency.";
Lancet 338:778-781(1991).
[26]
VARIANT FED LYS-276.
PubMed=1516702; DOI=10.1016/0014-5793(92)80795-I;
Skretting G., Blomhoff J.P., Solheim J., Prydz H.;
"The genetic defect of the original Norwegian lecithin:cholesterol
acyltransferase deficiency families.";
FEBS Lett. 309:307-310(1992).
[27]
VARIANT LCATD ILE-317.
PubMed=1859405; DOI=10.1016/0006-291X(91)90129-U;
Maeda E., Naka Y., Matozaki T., Sakuma M., Akanuma Y., Yoshino G.,
Kasuga M.;
"Lecithin-cholesterol acyltransferase (LCAT) deficiency with a
missense mutation in exon 6 of the LCAT gene.";
Biochem. Biophys. Res. Commun. 178:460-466(1991).
[28]
VARIANTS LCATD THR-117; TRP-159; PRO-233 AND MET-345, AND VARIANT
CYS-182.
PubMed=8432868; DOI=10.1172/JCI116248;
Funke H., von Eckardstein A., Pritchard P.H., Hornby A.E.,
Wiebusch H., Motti C., Hayden M.R., Dachet C., Jacotot B., Gerdes U.,
Faergeman O., Albers J.J., Colleoni N., Catapano A., Frohlich J.,
Assmann G.;
"Genetic and phenotypic heterogeneity in familial lecithin:
cholesterol acyltransferase (LCAT) deficiency. Six newly identified
defective alleles further contribute to the structural heterogeneity
in this disease.";
J. Clin. Invest. 91:677-683(1993).
[29]
VARIANT LCATD THR-117, AND VARIANT CYS-182.
PubMed=8318557; DOI=10.1016/0925-4439(93)90039-4;
Hill J.S., O K., Wang X., Pritchard P.H.;
"Lecithin:cholesterol acyltransferase deficiency: identification of a
causative gene mutation and a co-inherited protein polymorphism.";
Biochim. Biophys. Acta 1181:321-323(1993).
[30]
VARIANT LCATD HIS-164, AND CHARACTERIZATION OF VARIANT LCATD HIS-164.
PubMed=7607641; DOI=10.1007/BF00214196;
Steyrer E., Haubenwallner S., Hoerl G., Giessauf W., Kostner G.M.,
Zechner R.;
"A single G to A nucleotide transition in exon IV of the lecithin:
cholesterol acyltransferase (LCAT) gene results in an Arg140 to His
substitution and causes LCAT-deficiency.";
Hum. Genet. 96:105-109(1995).
[31]
VARIANTS LCATD ARG-57 AND LEU-LEU-PRO-PRO-ALA-ALA-PRO-PHE-TRP-LEU-17
INS.
PubMed=7711728; DOI=10.1093/hmg/4.1.143;
Wiebusch H., Cullen P., Owen J.S., Collins D., Sharp P.S., Funke H.,
Assmann G.;
"Deficiency of lecithin:cholesterol acyltransferase due to compound
heterozygosity of two novel mutations (Gly33Arg and 30 bp ins) in the
LCAT gene.";
Hum. Mol. Genet. 4:143-145(1995).
[32]
VARIANTS FED GLN-34 AND GLN-159.
PubMed=8620346; DOI=10.1161/01.ATV.16.2.294;
Kuivenhoven J.A., Stalenhoef A.F., Hill J.S., Demacker P.N.,
Errami A., Kastelein J.J., Pritchard P.H.;
"Two novel molecular defects in the LCAT gene are associated with fish
eye disease.";
Arterioscler. Thromb. Vasc. Biol. 16:294-303(1996).
[33]
VARIANT LCATD SER-54.
PubMed=8807342;
DOI=10.1002/(SICI)1098-1004(1996)8:1<79::AID-HUMU13>3.0.CO;2-O;
Owen J.S., Wiebusch H., Cullen P., Watts G.F., Lima V.L.M., Funke H.,
Assmann G.;
"Complete deficiency of plasma lecithin-cholesterol acyltransferase
(LCAT) activity due to a novel homozygous mutation (Gly-30-Ser) in the
LCAT gene.";
Hum. Mutat. 8:79-82(1996).
[34]
VARIANT LCATD ILE-29.
PubMed=9007616; DOI=10.1007/BF02602958;
Okubo M., Aoyama Y., Shio H., Albers J.J., Murase T.;
"A novel missense mutation (Asn5-->Ile) in lecithin: cholesterol
acyltransferase (LCAT) gene in a Japanese patient with LCAT
deficiency.";
Int. J. Clin. Lab. Res. 26:250-254(1996).
[35]
VARIANT FED CYS-123.
PubMed=9261271; DOI=10.1161/01.ATV.17.7.1382;
Blanco-Vaca F., Qu S.J., Fiol C., Fan H.Z., Pao Q.,
Marzal-Casacuberta A., Albers J.J., Hurtado I., Gracia V., Pinto X.,
Marti T., Pownall H.J.;
"Molecular basis of fish-eye disease in a patient from Spain.
Characterization of a novel mutation in the LCAT gene and lipid
analysis of the cornea.";
Arterioscler. Thromb. Vasc. Biol. 17:1382-1391(1997).
[36]
VARIANTS LCATD MET-37 AND SER-331.
PubMed=9741700;
Argyropoulos G., Jenkins A., Klein R.L., Lyons T., Wagenhorst B.,
St Armand J., Marcovina S.M., Albers J.J., Pritchard P.H.,
Garvey W.T.;
"Transmission of two novel mutations in a pedigree with familial
lecithin:cholesterol acyltransferase deficiency: structure-function
relationships and studies in a compound heterozygous proband.";
J. Lipid Res. 39:1870-1876(1998).
[37]
VARIANT LCATD ALA-298.
PubMed=11423760; DOI=10.1159/000046001;
Sessa A., Battini G., Meroni M., Daidone G., Carnera I.,
Brambilla P.L., Vigano G., Giordano F., Pallotti F., Torri Tarelli L.,
Calabresi L., Rolleri M., Bertolini S.;
"Hypocomplementemic type II membranoproliferative glomerulonephritis
in a male patient with familial lecithin-cholesterol acyltransferase
deficiency due to two different allelic mutations.";
Nephron 88:268-272(2001).
[38]
VARIANTS LCATD MET-345 AND VAL-406, AND VARIANT THR-232.
PubMed=12957688; DOI=10.1016/S0021-9150(03)00241-7;
Nanjee M.N., Stocks J., Cooke C.J., Molhuizen H.O., Marcovina S.,
Crook D., Kastelein J.P., Miller N.E.;
"A novel LCAT mutation (Phe382-->Val) in a kindred with familial LCAT
deficiency and defective apolipoprotein B-100.";
Atherosclerosis 170:105-113(2003).
[39]
VARIANT THR-232.
PubMed=12966036; DOI=10.1093/hmg/ddg314;
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
Alvin G.B., Das K., Gilliam T.C.;
"Association of extreme blood lipid profile phenotypic variation with
11 reverse cholesterol transport genes and 10 non-genetic
cardiovascular disease risk factors.";
Hum. Mol. Genet. 12:2733-2743(2003).
[40]
VARIANTS FED GLU-70 AND ALA-298, VARIANTS LCATD CYS-164; TRP-171;
ASN-205; ASN-242; HIS-268; ILE-298 AND MET-333, AND VARIANTS PRO-115;
THR-165 AND ARG-396.
PubMed=15994445; DOI=10.1161/01.ATV.0000175751.30616.13;
Calabresi L., Pisciotta L., Costantin A., Frigerio I., Eberini I.,
Alessandrini P., Arca M., Bon G.B., Boscutti G., Busnach G.,
Frasca G., Gesualdo L., Gigante M., Lupattelli G., Montali A.,
Pizzolitto S., Rabbone I., Rolleri M., Ruotolo G., Sampietro T.,
Sessa A., Vaudo G., Cantafora A., Veglia F., Calandra S.,
Bertolini S., Franceschini G.;
"The molecular basis of lecithin:cholesterol acyltransferase
deficiency syndromes: a comprehensive study of molecular and
biochemical findings in 13 unrelated Italian families.";
Arterioscler. Thromb. Vasc. Biol. 25:1972-1978(2005).
[41]
VARIANT LCATD MET-333.
PubMed=16051254; DOI=10.1016/j.atherosclerosis.2005.06.022;
Idzior-Walus B., Sieradzki J., Kostner G., Malecki M.T., Klupa T.,
Wesolowska T., Rostworowski W., Hartwich J., Walus M., Kiec A.D.,
Naruszewicz M.;
"Familial lecithin-cholesterol acyltransferase deficiency: biochemical
characteristics and molecular analysis of a new LCAT mutation in a
Polish family.";
Atherosclerosis 185:413-420(2006).
[42]
VARIANT ARG-95, VARIANT LCATD HIS-164, AND CHARACTERIZATION OF VARIANT
ARG-95.
PubMed=16216249; DOI=10.1016/j.atherosclerosis.2005.08.038;
Hoerl G., Kroisel P.M., Wagner E., Tiran B., Petek E., Steyrer E.;
"Compound heterozygosity (G71R/R140H) in the lecithin:cholesterol
acyltransferase (LCAT) gene results in an intermediate phenotype
between LCAT-deficiency and fish-eye disease.";
Atherosclerosis 187:101-109(2006).
[43]
VARIANTS THR-232 AND ARG-396.
PubMed=16874701;
Gigante M., Ranieri E., Cerullo G., Calabresi L., Iolascon A.,
Assmann G., Morrone L., Pisciotta L., Schena F.P., Gesualdo L.;
"LCAT deficiency: molecular and phenotypic characterization of an
Italian family.";
J. Nephrol. 19:375-381(2006).
[44]
VARIANTS 134-GLU-TYR-135 DELINS ASP-ASN; PHE-246; CYS-268 AND CYS-322,
VARIANTS FED SER-99; PHE-338 AND CYS-347, CHARACTERIZATION OF VARIANTS
134-GLU-TYR-135 DELINS ASP-ASN; PHE-246; CYS-268 AND CYS-322, AND
CHARACTERIZATION OF VARIANTS FED SER-99; PHE-338 CYS-347 AND CYS-347.
PubMed=21901787; DOI=10.1002/humu.21578;
Holleboom A.G., Kuivenhoven J.A., Peelman F., Schimmel A.W., Peter J.,
Defesche J.C., Kastelein J.J., Hovingh G.K., Stroes E.S.,
Motazacker M.M.;
"High prevalence of mutations in LCAT in patients with low HDL
cholesterol levels in The Netherlands: identification and
characterization of eight novel mutations.";
Hum. Mutat. 32:1290-1298(2011).
-!- FUNCTION: Central enzyme in the extracellular metabolism of plasma
lipoproteins. Synthesized mainly in the liver and secreted into
plasma where it converts cholesterol and phosphatidylcholines
(lecithins) to cholesteryl esters and lysophosphatidylcholines on
the surface of high and low density lipoproteins (HDLs and LDLs)
(PubMed:10329423, PubMed:19065001, PubMed:26195816). The
cholesterol ester is then transported back to the liver. Has a
preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines
(PubMed:8820107). Also produced in the brain by primary
astrocytes, and esterifies free cholesterol on nascent APOE-
containing lipoproteins secreted from glia and influences cerebral
spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and
the cholesterol transporter ABCA1, plays a key role in the
maturation of glial-derived, nascent lipoproteins. Required for
remodeling high-density lipoprotein particles into their spherical
forms (PubMed:10722751). {ECO:0000269|PubMed:10329423,
ECO:0000269|PubMed:10722751, ECO:0000269|PubMed:14636062,
ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:26195816,
ECO:0000269|PubMed:8820107}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + a sterol = 1-
acylglycerophosphocholine + a sterol ester. {ECO:0000255|PROSITE-
ProRule:PRU10037, ECO:0000269|PubMed:10222237,
ECO:0000269|PubMed:10329423, ECO:0000269|PubMed:14636062,
ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:25727495,
ECO:0000269|PubMed:26195816, ECO:0000269|PubMed:3458198,
ECO:0000269|PubMed:8820107}.
-!- ACTIVITY REGULATION: APOA1 is the most potent activator in plasma.
Also activated by APOE, APOC1 and APOA4.
{ECO:0000269|PubMed:19065001}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.97 mM for LDL {ECO:0000269|PubMed:10329423};
KM=0.4 mM for HDL(2) {ECO:0000269|PubMed:10329423};
KM=0.10 mM for HDL(3) {ECO:0000269|PubMed:10329423};
Vmax=8.3 mmol/min/mg enzyme with LDL as substrate
{ECO:0000269|PubMed:10329423};
Vmax=0.58 mmol/min/mg enzyme with HDL(2) as substrate
{ECO:0000269|PubMed:10329423};
Vmax=2.0 mmol/min/mg enzyme with HDL(3) as substrate
{ECO:0000269|PubMed:10329423};
Note=Affinity for LDL is 2.3 to 4-fold lower than for HDL.
Relative reactivities are 16% for HDL(3), 1.3% for HDL(2) and
6.5% for LDL.;
-!- INTERACTION:
P02647:APOA1; NbExp=2; IntAct=EBI-9104464, EBI-701692;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10222237,
ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:3458198,
ECO:0000269|PubMed:8820107}. Note=Secreted into blood plasma
(PubMed:3458198, PubMed:8820107, PubMed:10222237). Produced in
astrocytes and secreted into cerebral spinal fluid (CSF).
{ECO:0000269|PubMed:10222237, ECO:0000269|PubMed:3458198,
ECO:0000269|PubMed:8820107}.
-!- TISSUE SPECIFICITY: Detected in blood plasma (PubMed:3458198,
PubMed:8820107, PubMed:10222237). Detected in cerebral spinal
fluid (at protein level) (PubMed:10222237). Detected in liver
(PubMed:3797244, PubMed:3458198). Expressed mainly in brain, liver
and testes. {ECO:0000269|PubMed:10222237,
ECO:0000269|PubMed:3458198, ECO:0000269|PubMed:3797244,
ECO:0000269|PubMed:8820107}.
-!- PTM: O- and N-glycosylated. O-glycosylation on Thr-431 and Ser-433
consists of sialylated galactose beta 1-->3N-acetylgalactosamine
structures. N-glycosylated sites contain sialylated triantennary
and/or biantennary complex structures.
{ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:7613477}.
-!- DISEASE: Lecithin-cholesterol acyltransferase deficiency (LCATD)
[MIM:245900]: A disorder of lipoprotein metabolism characterized
by inadequate esterification of plasmatic cholesterol. Two
clinical forms are recognized: complete LCAT deficiency and fish-
eye disease. LCATD is generally referred to the complete form
which is associated with absence of both alpha and beta LCAT
activities resulting in esterification anomalies involving both
HDL (alpha-LCAT activity) and LDL (beta-LCAT activity). It causes
a typical triad of diffuse corneal opacities, target cell
hemolytic anemia, and proteinuria with renal failure.
{ECO:0000269|PubMed:11423760, ECO:0000269|PubMed:12957688,
ECO:0000269|PubMed:15994445, ECO:0000269|PubMed:16051254,
ECO:0000269|PubMed:16216249, ECO:0000269|PubMed:1681161,
ECO:0000269|PubMed:1859405, ECO:0000269|PubMed:2370048,
ECO:0000269|PubMed:7607641, ECO:0000269|PubMed:7711728,
ECO:0000269|PubMed:8318557, ECO:0000269|PubMed:8432868,
ECO:0000269|PubMed:8807342, ECO:0000269|PubMed:9007616,
ECO:0000269|PubMed:9741700}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Fish-eye disease (FED) [MIM:136120]: A disorder of
lipoprotein metabolism due to partial lecithin-cholesterol
acyltransferase deficiency that affects only alpha-LCAT activity.
FED is characterized by low plasma HDL and corneal opacities due
to accumulation of cholesterol deposits in the cornea ('fish-
eye'). {ECO:0000269|PubMed:1516702, ECO:0000269|PubMed:1571050,
ECO:0000269|PubMed:15994445, ECO:0000269|PubMed:1737840,
ECO:0000269|PubMed:21901787, ECO:0000269|PubMed:8620346,
ECO:0000269|PubMed:9261271}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Levels of LCAT activity correlates inversely with
leptin levels as well as with obesity for a wide range of BMI
values.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Lecithin-cholesterol
acyltransferase entry;
URL="https://en.wikipedia.org/wiki/Lecithin-cholesterol_acyltransferase";
-----------------------------------------------------------------------
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EMBL; X04981; CAA28651.1; -; Genomic_DNA.
EMBL; M12625; AAA59498.1; -; mRNA.
EMBL; AY422210; AAR03499.1; -; Genomic_DNA.
EMBL; BT009748; AAP88750.1; -; mRNA.
EMBL; AC040162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471092; EAW83190.1; -; Genomic_DNA.
EMBL; BC014781; AAH14781.1; -; mRNA.
EMBL; M26268; AAA59499.1; -; mRNA.
EMBL; X06537; CAB56610.1; -; mRNA.
EMBL; M17959; AAA59500.1; -; Genomic_DNA.
CCDS; CCDS10854.1; -.
PIR; A00571; XXHUN.
RefSeq; NP_000220.1; NM_000229.1.
UniGene; Hs.387239; -.
PDB; 4X96; X-ray; 8.69 A; A/B/C/D=45-421.
PDB; 4XWG; X-ray; 2.65 A; A=25-440.
PDB; 4XX1; X-ray; 3.60 A; A/B/J=25-440.
PDB; 5BV7; X-ray; 2.45 A; A=25-440.
PDB; 5TXF; X-ray; 3.10 A; A/B/C/D=25-440.
PDBsum; 4X96; -.
PDBsum; 4XWG; -.
PDBsum; 4XX1; -.
PDBsum; 5BV7; -.
PDBsum; 5TXF; -.
ProteinModelPortal; P04180; -.
SMR; P04180; -.
BioGrid; 110123; 6.
DIP; DIP-29620N; -.
IntAct; P04180; 1.
STRING; 9606.ENSP00000264005; -.
BindingDB; P04180; -.
ChEMBL; CHEMBL5942; -.
SwissLipids; SLP:000000660; -.
ESTHER; human-LCAT; PC-sterol_acyltransferase.
GlyConnect; 495; -.
iPTMnet; P04180; -.
PhosphoSitePlus; P04180; -.
UniCarbKB; P04180; -.
BioMuta; LCAT; -.
DMDM; 125993; -.
MaxQB; P04180; -.
PaxDb; P04180; -.
PeptideAtlas; P04180; -.
PRIDE; P04180; -.
ProteomicsDB; 51671; -.
DNASU; 3931; -.
Ensembl; ENST00000264005; ENSP00000264005; ENSG00000213398.
GeneID; 3931; -.
KEGG; hsa:3931; -.
UCSC; uc002euy.2; human.
CTD; 3931; -.
DisGeNET; 3931; -.
EuPathDB; HostDB:ENSG00000213398.7; -.
GeneCards; LCAT; -.
H-InvDB; HIX0134431; -.
HGNC; HGNC:6522; LCAT.
HPA; HPA044767; -.
MalaCards; LCAT; -.
MIM; 136120; phenotype.
MIM; 245900; phenotype.
MIM; 606967; gene.
neXtProt; NX_P04180; -.
OpenTargets; ENSG00000213398; -.
Orphanet; 79293; Familial LCAT deficiency.
Orphanet; 79292; Fish-eye disease.
PharmGKB; PA226; -.
eggNOG; KOG2369; Eukaryota.
eggNOG; ENOG410Y9CF; LUCA.
GeneTree; ENSGT00390000004902; -.
HOGENOM; HOG000238654; -.
HOVERGEN; HBG017055; -.
InParanoid; P04180; -.
KO; K00650; -.
OMA; TYGKPVF; -.
OrthoDB; EOG091G07S3; -.
PhylomeDB; P04180; -.
TreeFam; TF313258; -.
BRENDA; 2.3.1.43; 2681.
Reactome; R-HSA-8964058; HDL remodeling.
SABIO-RK; P04180; -.
SIGNOR; P04180; -.
ChiTaRS; LCAT; human.
GeneWiki; Lecithin%E2%80%94cholesterol_acyltransferase; -.
GenomeRNAi; 3931; -.
PRO; PR:P04180; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000213398; Expressed in 136 organ(s), highest expression level in right lobe of liver.
CleanEx; HS_LCAT; -.
ExpressionAtlas; P04180; baseline and differential.
Genevisible; P04180; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0034186; F:apolipoprotein A-I binding; IPI:BHF-UCL.
GO; GO:0004607; F:phosphatidylcholine-sterol O-acyltransferase activity; IDA:UniProtKB.
GO; GO:0034435; P:cholesterol esterification; IDA:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IDA:UniProtKB.
GO; GO:0030301; P:cholesterol transport; IDA:MGI.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:UniProtKB.
GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:BHF-UCL.
GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB.
GO; GO:0006644; P:phospholipid metabolic process; IDA:BHF-UCL.
GO; GO:0090107; P:regulation of high-density lipoprotein particle assembly; IEA:Ensembl.
GO; GO:0043691; P:reverse cholesterol transport; IDA:BHF-UCL.
GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR003386; LACT/PDAT_acylTrfase.
Pfam; PF02450; LCAT; 1.
SUPFAM; SSF53474; SSF53474; 2.
PROSITE; PS00120; LIPASE_SER; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Cholesterol metabolism;
Complete proteome; Corneal dystrophy; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Lipid metabolism;
Polymorphism; Reference proteome; Secreted; Signal;
Steroid metabolism; Sterol metabolism; Transferase.
SIGNAL 1 24 {ECO:0000269|PubMed:3458198}.
CHAIN 25 440 Phosphatidylcholine-sterol
acyltransferase.
/FTId=PRO_0000017802.
COMPBIAS 426 439 Pro-rich.
ACT_SITE 205 205 Nucleophile.
{ECO:0000305|PubMed:26195816}.
ACT_SITE 369 369 Charge relay system.
{ECO:0000305|PubMed:26195816}.
ACT_SITE 401 401 Charge relay system.
{ECO:0000305|PubMed:26195816}.
SITE 173 173 Determinant for substrate specificity.
{ECO:0000305|PubMed:14636062}.
CARBOHYD 44 44 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:7613477}.
CARBOHYD 108 108 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000244|PDB:4X96,
ECO:0000269|PubMed:26195816,
ECO:0000269|PubMed:7613477}.
CARBOHYD 296 296 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000244|PDB:4X96,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:26195816,
ECO:0000269|PubMed:7613477}.
CARBOHYD 408 408 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000244|PDB:4X96,
ECO:0000269|PubMed:26195816,
ECO:0000269|PubMed:7613477}.
CARBOHYD 431 431 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:7613477}.
CARBOHYD 433 433 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:7613477}.
DISULFID 74 98 {ECO:0000244|PDB:4X96,
ECO:0000244|PDB:4XWG,
ECO:0000244|PDB:4XX1,
ECO:0000269|PubMed:26195816,
ECO:0000269|PubMed:2880847}.
DISULFID 337 380 {ECO:0000244|PDB:4X96,
ECO:0000244|PDB:4XWG,
ECO:0000244|PDB:4XX1,
ECO:0000269|PubMed:26195816,
ECO:0000269|PubMed:2880847}.
VARIANT 17 17 L -> LLLPPAAPFWL (in LCATD).
/FTId=VAR_004251.
VARIANT 29 29 N -> I (in LCATD).
{ECO:0000269|PubMed:9007616}.
/FTId=VAR_039020.
VARIANT 34 34 P -> L (in FED; dbSNP:rs121908051).
{ECO:0000269|PubMed:1571050}.
/FTId=VAR_004252.
VARIANT 34 34 P -> Q (in FED).
{ECO:0000269|PubMed:8620346}.
/FTId=VAR_039021.
VARIANT 37 37 T -> M (in LCATD; dbSNP:rs971887742).
{ECO:0000269|PubMed:9741700}.
/FTId=VAR_039022.
VARIANT 54 54 G -> S (in LCATD).
{ECO:0000269|PubMed:8807342}.
/FTId=VAR_004253.
VARIANT 57 57 G -> R (in LCATD).
{ECO:0000269|PubMed:7711728}.
/FTId=VAR_004254.
VARIANT 70 70 V -> E (in FED; dbSNP:rs748427834).
{ECO:0000269|PubMed:15994445}.
/FTId=VAR_039023.
VARIANT 95 95 G -> R (in a compound heterozygote
carrying H-164; intermediate phenotype
between LCATD and FED; reduction of
activity). {ECO:0000269|PubMed:16216249}.
/FTId=VAR_039024.
VARIANT 99 99 W -> S (in FED; loss of activity).
{ECO:0000269|PubMed:21901787}.
/FTId=VAR_066862.
VARIANT 115 115 S -> P. {ECO:0000269|PubMed:15994445}.
/FTId=VAR_039025.
VARIANT 117 117 A -> T (in LCATD; dbSNP:rs28940886).
{ECO:0000269|PubMed:8318557,
ECO:0000269|PubMed:8432868}.
/FTId=VAR_004255.
VARIANT 123 123 R -> C (in FED; dbSNP:rs140068549).
{ECO:0000269|PubMed:9261271}.
/FTId=VAR_039026.
VARIANT 134 135 EY -> DN (in a patient with low HDL-
cholesterol levels; results in reduced
activity). {ECO:0000269|PubMed:21901787}.
/FTId=VAR_066863.
VARIANT 147 147 T -> I (in FED; dbSNP:rs121908050).
{ECO:0000269|PubMed:1737840}.
/FTId=VAR_004256.
VARIANT 159 159 R -> Q (in FED; dbSNP:rs768017317).
{ECO:0000269|PubMed:8620346}.
/FTId=VAR_039027.
VARIANT 159 159 R -> W (in LCATD; dbSNP:rs28940887).
{ECO:0000269|PubMed:8432868}.
/FTId=VAR_004257.
VARIANT 164 164 R -> C (in LCATD).
{ECO:0000269|PubMed:15994445}.
/FTId=VAR_039028.
VARIANT 164 164 R -> H (in LCATD; also in a compound
heterozygote carrying R-95 with
intermediate phenotype between LCATD and
FED; loss of activity;
dbSNP:rs769485083).
{ECO:0000269|PubMed:16216249,
ECO:0000269|PubMed:7607641}.
/FTId=VAR_004258.
VARIANT 165 165 A -> T. {ECO:0000269|PubMed:15994445}.
/FTId=VAR_039029.
VARIANT 171 171 R -> W (in LCATD).
{ECO:0000269|PubMed:15994445,
ECO:0000269|PubMed:2370048}.
/FTId=VAR_004259.
VARIANT 180 180 Y -> N (in LCATD; dbSNP:rs749740660).
/FTId=VAR_004260.
VARIANT 182 182 R -> C (in dbSNP:rs387906300).
{ECO:0000269|PubMed:8318557,
ECO:0000269|PubMed:8432868}.
/FTId=VAR_004261.
VARIANT 205 205 S -> N (in LCATD).
{ECO:0000269|PubMed:15994445}.
/FTId=VAR_039030.
VARIANT 232 232 S -> T (in dbSNP:rs4986970).
{ECO:0000269|PubMed:12957688,
ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:16874701}.
/FTId=VAR_017030.
VARIANT 233 233 L -> P (in LCATD; dbSNP:rs28942087).
{ECO:0000269|PubMed:8432868}.
/FTId=VAR_004262.
VARIANT 242 242 K -> N (in LCATD).
{ECO:0000269|PubMed:15994445}.
/FTId=VAR_039031.
VARIANT 246 246 V -> F (in a patient with low HDL-
cholesterol levels; the mutant is hardly
secreted and is catalytically inactive).
{ECO:0000269|PubMed:21901787}.
/FTId=VAR_066864.
VARIANT 252 252 N -> K (in LCATD; dbSNP:rs121908049).
{ECO:0000269|PubMed:1681161}.
/FTId=VAR_004263.
VARIANT 268 268 R -> C (in a patient with low HDL-
cholesterol levels; the mutant is hardly
secreted and is catalytically inactive;
dbSNP:rs745320775).
{ECO:0000269|PubMed:21901787}.
/FTId=VAR_066865.
VARIANT 268 268 R -> H (in LCATD; dbSNP:rs780824776).
{ECO:0000269|PubMed:15994445}.
/FTId=VAR_039032.
VARIANT 276 276 M -> K (in FED; dbSNP:rs121908054).
{ECO:0000269|PubMed:1516702}.
/FTId=VAR_004264.
VARIANT 298 298 T -> A (in FED and LCATD).
{ECO:0000269|PubMed:11423760,
ECO:0000269|PubMed:15994445}.
/FTId=VAR_039033.
VARIANT 298 298 T -> I (in LCATD).
{ECO:0000269|PubMed:15994445}.
/FTId=VAR_039034.
VARIANT 317 317 M -> I (in LCATD; partially defective
enzyme; dbSNP:rs121908048).
{ECO:0000269|PubMed:1681161,
ECO:0000269|PubMed:1859405}.
/FTId=VAR_004265.
VARIANT 322 322 R -> C (in a patient with low HDL-
cholesterol levels; reduced protein
secretion).
{ECO:0000269|PubMed:21901787}.
/FTId=VAR_066866.
VARIANT 331 331 P -> S (in LCATD).
{ECO:0000269|PubMed:9741700}.
/FTId=VAR_039035.
VARIANT 333 333 V -> M (in LCATD; dbSNP:rs776035233).
{ECO:0000269|PubMed:15994445,
ECO:0000269|PubMed:16051254}.
/FTId=VAR_039036.
VARIANT 338 338 L -> F (in FED; results in reduced
protein secretion and activity).
{ECO:0000269|PubMed:21901787}.
/FTId=VAR_066867.
VARIANT 345 345 T -> M (in LCATD; dbSNP:rs28940888).
{ECO:0000269|PubMed:12957688,
ECO:0000269|PubMed:8432868}.
/FTId=VAR_004266.
VARIANT 347 347 R -> C (in FED; results in reduced
activity; dbSNP:rs202017590).
{ECO:0000269|PubMed:21901787}.
/FTId=VAR_066868.
VARIANT 371 371 T -> M (in FED; dbSNP:rs121908053).
{ECO:0000269|PubMed:1737840}.
/FTId=VAR_004267.
VARIANT 396 396 L -> R (in a patient with LCATD).
{ECO:0000269|PubMed:15994445,
ECO:0000269|PubMed:16874701}.
/FTId=VAR_039037.
VARIANT 406 406 F -> V (in LCATD).
{ECO:0000269|PubMed:12957688}.
/FTId=VAR_039038.
MUTAGEN 173 173 E->A: Increased activity towards PAPC.
Increased PAPC/POPC activity ratio.
{ECO:0000269|PubMed:14636062}.
MUTAGEN 173 173 E->D: Little change in enzyme specific
activity nor in PAPC/POPC activity ratio.
{ECO:0000269|PubMed:14636062}.
MUTAGEN 173 173 E->K: Decreased enzyme specific activity.
Increased PAPC/POPC activity ratio.
{ECO:0000269|PubMed:14636062}.
MUTAGEN 173 173 E->L: Increased activity towards PAPC.
Increased PAPC/POPC activity ratio.
{ECO:0000269|PubMed:14636062}.
MUTAGEN 173 173 E->Q: Decreased enzyme specific activity.
Increased PAPC/POPC activity ratio.
{ECO:0000269|PubMed:14636062}.
CONFLICT 257 257 I -> H (in Ref. 8; CAB56610/AAA59499).
{ECO:0000305}.
STRAND 49 52 {ECO:0000244|PDB:5BV7}.
STRAND 60 63 {ECO:0000244|PDB:5BV7}.
STRAND 82 86 {ECO:0000244|PDB:5BV7}.
HELIX 88 91 {ECO:0000244|PDB:5BV7}.
HELIX 95 103 {ECO:0000244|PDB:5BV7}.
STRAND 105 107 {ECO:0000244|PDB:5BV7}.
TURN 109 111 {ECO:0000244|PDB:5BV7}.
STRAND 114 117 {ECO:0000244|PDB:5BV7}.
STRAND 121 123 {ECO:0000244|PDB:5BV7}.
TURN 125 128 {ECO:0000244|PDB:4XWG}.
HELIX 131 134 {ECO:0000244|PDB:5BV7}.
STRAND 135 137 {ECO:0000244|PDB:5BV7}.
STRAND 142 145 {ECO:0000244|PDB:5BV7}.
HELIX 146 153 {ECO:0000244|PDB:5BV7}.
TURN 154 156 {ECO:0000244|PDB:5BV7}.
TURN 160 162 {ECO:0000244|PDB:5BV7}.
STRAND 163 165 {ECO:0000244|PDB:5BV7}.
HELIX 174 176 {ECO:0000244|PDB:5BV7}.
HELIX 178 195 {ECO:0000244|PDB:5BV7}.
STRAND 199 204 {ECO:0000244|PDB:5BV7}.
HELIX 206 217 {ECO:0000244|PDB:5BV7}.
HELIX 220 226 {ECO:0000244|PDB:5BV7}.
STRAND 227 234 {ECO:0000244|PDB:5BV7}.
HELIX 242 248 {ECO:0000244|PDB:5BV7}.
TURN 250 252 {ECO:0000244|PDB:5BV7}.
TURN 255 257 {ECO:0000244|PDB:5BV7}.
STRAND 258 260 {ECO:0000244|PDB:5TXF}.
STRAND 270 272 {ECO:0000244|PDB:5BV7}.
HELIX 274 276 {ECO:0000244|PDB:5BV7}.
TURN 280 282 {ECO:0000244|PDB:5BV7}.
STRAND 288 291 {ECO:0000244|PDB:5BV7}.
STRAND 296 298 {ECO:0000244|PDB:5BV7}.
HELIX 299 301 {ECO:0000244|PDB:5TXF}.
HELIX 302 308 {ECO:0000244|PDB:5BV7}.
HELIX 312 321 {ECO:0000244|PDB:5BV7}.
TURN 322 327 {ECO:0000244|PDB:5BV7}.
STRAND 335 350 {ECO:0000244|PDB:5BV7}.
TURN 353 357 {ECO:0000244|PDB:5BV7}.
STRAND 361 373 {ECO:0000244|PDB:5BV7}.
HELIX 374 377 {ECO:0000244|PDB:5BV7}.
HELIX 378 383 {ECO:0000244|PDB:5BV7}.
STRAND 386 389 {ECO:0000244|PDB:5BV7}.
STRAND 391 397 {ECO:0000244|PDB:5BV7}.
HELIX 401 403 {ECO:0000244|PDB:5BV7}.
TURN 404 406 {ECO:0000244|PDB:5BV7}.
HELIX 408 419 {ECO:0000244|PDB:5BV7}.
TURN 420 422 {ECO:0000244|PDB:5BV7}.
SEQUENCE 440 AA; 49578 MW; B315EF118AA7A378 CRC64;
MGPPGSPWQW VTLLLGLLLP PAAPFWLLNV LFPPHTTPKA ELSNHTRPVI LVPGCLGNQL
EAKLDKPDVV NWMCYRKTED FFTIWLDLNM FLPLGVDCWI DNTRVVYNRS SGLVSNAPGV
QIRVPGFGKT YSVEYLDSSK LAGYLHTLVQ NLVNNGYVRD ETVRAAPYDW RLEPGQQEEY
YRKLAGLVEE MHAAYGKPVF LIGHSLGCLH LLYFLLRQPQ AWKDRFIDGF ISLGAPWGGS
IKPMLVLASG DNQGIPIMSS IKLKEEQRIT TTSPWMFPSR MAWPEDHVFI STPSFNYTGR
DFQRFFADLH FEEGWYMWLQ SRDLLAGLPA PGVEVYCLYG VGLPTPRTYI YDHGFPYTDP
VGVLYEDGDD TVATRSTELC GLWQGRQPQP VHLLPLHGIQ HLNMVFSNLT LEHINAILLG
AYRQGPPASP TASPEPPPPE


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