LCAT_HUMAN
ID LCAT_HUMAN Reviewed; 440 AA.
AC P04180; Q53XQ3;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Phosphatidylcholine-sterol acyltransferase;
DE 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};
DE AltName: Full=1-alkyl-2-acetylglycerophosphocholine esterase;
DE EC=3.1.1.47 {ECO:0000269|PubMed:8016111};
DE AltName: Full=Lecithin-cholesterol acyltransferase;
DE AltName: Full=Phospholipid-cholesterol acyltransferase;
DE AltName: Full=Platelet-activating factor acetylhydrolase {ECO:0000303|PubMed:8016111};
DE Short=PAF acetylhydrolase;
DE Flags: Precursor;
GN Name=LCAT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=3797244; DOI=10.1093/nar/14.23.9397;
RA McLean J., Wion K., Drayna D., Fielding C., Lawn R.;
RT "Human lecithin-cholesterol acyltransferase gene: complete gene sequence
RT and sites of expression.";
RL Nucleic Acids Res. 14:9397-9406(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-39; 172-182; 269-280 AND
RP 387-406, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=3458198; DOI=10.1073/pnas.83.8.2335;
RA McLean J., Fielding C., Drayna D., Dieplinger H., Baer B., Kohr W.,
RA Henzel W., Lawn R.;
RT "Cloning and expression of human lecithin-cholesterol acyltransferase
RT cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2335-2339(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nickerson D.A., Smith J.D., Fullerton S.M., Clark A.G., Stengard J.H.,
RA Salomaa V., Boerwinkle E., Sing C.F., Weiss K.M.;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-440.
RX PubMed=2823898; DOI=10.1016/0167-4781(87)90066-2;
RA Tata F., Chaves M.E., Markham A.F., Scrace G.D., Waterfield M.D.,
RA McIntyre N., Williamson R., Humphries S.E.;
RT "The isolation and characterisation of cDNA and genomic clones for human
RT lecithin: cholesterol acyltransferase.";
RL Biochim. Biophys. Acta 910:142-148(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-440.
RX PubMed=2823801; DOI=10.1016/0006-291x(87)91090-4;
RA Rogne S., Skretting G., Larsen F., Myklebost O., Mevag B., Carlson L.A.,
RA Holmquist L., Gjone E., Prydz H.;
RT "The isolation and characterisation of a cDNA clone for human
RT lecithin:cholesterol acyl transferase and its use to analyse the genes in
RT patients with LCAT deficiency and fish eye disease.";
RL Biochem. Biophys. Res. Commun. 148:161-169(1987).
RN [10]
RP PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX PubMed=2880847; DOI=10.1016/s0021-9258(18)61472-3;
RA Yang C., Manoogian D., Pao Q., Lee F., Knapp R.D., Gotto A.M. Jr.,
RA Pownall H.J.;
RT "Lecithin:cholesterol acyltransferase. Functional regions and a structural
RT model of the enzyme.";
RL J. Biol. Chem. 262:3086-3091(1987).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8016111; DOI=10.1073/pnas.91.13.6035;
RA Liu M., Subbaiah P.V.;
RT "Hydrolysis and transesterification of platelet-activating factor by
RT lecithin-cholesterol acyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6035-6039(1994).
RN [12]
RP GLYCOSYLATION AT ASN-44; ASN-108; ASN-296; ASN-408; THR-431 AND SER-433,
RP STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=7613477; DOI=10.1002/pro.5560040419;
RA Schindler P.A., Settineri C.A., Collet X., Fielding C.J., Burlingame A.L.;
RT "Site-specific detection and structural characterization of the
RT glycosylation of human plasma proteins lecithin:cholesterol acyltransferase
RT and apolipoprotein D using HPLC/electrospray mass spectrometry and
RT sequential glycosidase digestion.";
RL Protein Sci. 4:791-803(1995).
RN [13]
RP CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=8820107;
RA Subbaiah P.V., Liu M.;
RT "Comparative studies on the substrate specificity of lecithin:cholesterol
RT acyltransferase towards the molecular species of phosphatidylcholine in the
RT plasma of 14 vertebrates.";
RL J. Lipid Res. 37:113-122(1996).
RN [14]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=10222237; DOI=10.1006/bbrc.1999.0601;
RA Collet X., Francone O., Besnard F., Fielding C.J.;
RT "Secretion of lecithin:cholesterol acyltransferase by brain neuroglial cell
RT lines.";
RL Biochem. Biophys. Res. Commun. 258:73-76(1999).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10329423; DOI=10.1006/bbrc.1999.0690;
RA Kosek A.B., Durbin D., Jonas A.;
RT "Binding affinity and reactivity of lecithin cholesterol acyltransferase
RT with native lipoproteins.";
RL Biochem. Biophys. Res. Commun. 258:548-551(1999).
RN [16]
RP FUNCTION IN HIGH-DENSITY LIPOPROTEIN PARTICLE REMODELING.
RX PubMed=10722751; DOI=10.1074/jbc.275.12.9019;
RA Clay M.A., Pyle D.H., Rye K.A., Barter P.J.;
RT "Formation of spherical, reconstituted high density lipoproteins containing
RT both apolipoproteins A-I and A-II is mediated by lecithin:cholesterol
RT acyltransferase.";
RL J. Biol. Chem. 275:9019-9025(2000).
RN [17]
RP FUNCTION.
RX PubMed=12354767; DOI=10.1074/jbc.m206812200;
RA Aoki J., Taira A., Takanezawa Y., Kishi Y., Hama K., Kishimoto T.,
RA Mizuno K., Saku K., Taguchi R., Arai H.;
RT "Serum lysophosphatidic acid is produced through diverse phospholipase
RT pathways.";
RL J. Biol. Chem. 277:48737-48744(2002).
RN [18]
RP SUBSTRATE SPECIFICITY, MUTAGENESIS OF GLU-173, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=14636062; DOI=10.1021/bi035460u;
RA Zhao Y., Wang J., Gebre A.K., Chisholm J.W., Parks J.S.;
RT "Negative charge at amino acid 149 is the molecular determinant for
RT substrate specificity of lecithin: cholesterol acyltransferase for
RT phosphatidylcholine containing 20-carbon sn-2 fatty acyl chains.";
RL Biochemistry 42:13941-13949(2003).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44 AND ASN-296.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [20]
RP ASSOCIATION WITH OBESITY.
RX PubMed=17950106; DOI=10.1016/j.metabol.2007.06.022;
RA Bajnok L., Seres I., Varga Z., Jeges S., Peti A., Karanyi Z., Juhasz A.,
RA Csongradi E., Mezosi E., Nagy E.V., Paragh G.;
RT "Relationship of endogenous hyperleptinemia to serum paraoxonase 1,
RT cholesteryl ester transfer protein, and lecithin cholesterol
RT acyltransferase in obese individuals.";
RL Metabolism 56:1542-1549(2007).
RN [21]
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19065001; DOI=10.1194/jlr.m800584-jlr200;
RA Hirsch-Reinshagen V., Donkin J., Stukas S., Chan J., Wilkinson A., Fan J.,
RA Parks J.S., Kuivenhoven J.A., Lutjohann D., Pritchard H., Wellington C.L.;
RT "LCAT synthesized by primary astrocytes esterifies cholesterol on glia-
RT derived lipoproteins.";
RL J. Lipid Res. 50:885-893(2009).
RN [22]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=24620755; DOI=10.1111/jnc.12713;
RA La Marca V., Spagnuolo M.S., Cigliano L., Marasco D., Abrescia P.;
RT "The enzyme lecithin-cholesterol acyltransferase esterifies cerebrosterol
RT and limits the toxic effect of this oxysterol on SH-SY5Y cells.";
RL J. Neurochem. 130:97-108(2014).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-440, DISULFIDE BONDS,
RP FUNCTION, CATALYTIC ACTIVITY, AND GLYCOSYLATION AT ASN-108; ASN-296 AND
RP ASN-408.
RX PubMed=26195816; DOI=10.1194/jlr.m059873;
RA Piper D.E., Romanow W.G., Gunawardane R.N., Fordstrom P., Masterman S.,
RA Pan O., Thibault S.T., Zhang R., Meininger D., Schwarz M., Wang Z.,
RA King C., Zhou M., Walker N.P.;
RT "The high resolution crystal structure of human LCAT.";
RL J. Lipid Res. 56:1711-1719(2015).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (8.69 ANGSTROMS) OF 45-421, CATALYTIC ACTIVITY,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-108; ASN-296 AND ASN-408.
RX PubMed=25727495; DOI=10.1038/ncomms7250;
RA Glukhova A., Hinkovska-Galcheva V., Kelly R., Abe A., Shayman J.A.,
RA Tesmer J.J.;
RT "Structure and function of lysosomal phospholipase A2 and
RT lecithin:cholesterol acyltransferase.";
RL Nat. Commun. 6:6250-6250(2015).
RN [25]
RP VARIANT FED LEU-34.
RX PubMed=1571050; DOI=10.1016/0006-291x(92)91772-i;
RA Skretting G., Prydz H.;
RT "An amino acid exchange in exon I of the human lecithin: cholesterol
RT acyltransferase (LCAT) gene is associated with fish eye disease.";
RL Biochem. Biophys. Res. Commun. 182:583-587(1992).
RN [26]
RP VARIANTS FED ILE-147 AND MET-371.
RX PubMed=1737840; DOI=10.1172/jci115612;
RA Klein H.-G., Lohse P., Pritchard P.H., Bojanovski D., Schmidt H.,
RA Brewer H.B. Jr.;
RT "Two different allelic mutations in the lecithin-cholesterol
RT acyltransferase gene associated with the fish eye syndrome. Lecithin-
RT cholesterol acyltransferase (Thr123-->Ile) and lecithin-cholesterol
RT acyltransferase (Thr347-->Met).";
RL J. Clin. Invest. 89:499-506(1992).
RN [27]
RP VARIANT LCATD TRP-171.
RX PubMed=2370048; DOI=10.1007/bf00193195;
RA Taramelli R., Pontoglio M., Candiani G., Ottolenghi S., Dieplinger H.,
RA Catapano A., Albers J., Vergani C., McLean J.;
RT "Lecithin cholesterol acyl transferase deficiency: molecular analysis of a
RT mutated allele.";
RL Hum. Genet. 85:195-199(1990).
RN [28]
RP VARIANTS LCATD LYS-252 AND ILE-317.
RX PubMed=1681161; DOI=10.1016/0140-6736(91)90665-c;
RA Gotoda T., Yamada N., Murase T., Sakuma M., Murayama N., Shimano H.,
RA Kozaki K., Albers J.J., Yazaki Y., Akanuma Y.;
RT "Differential phenotypic expression by three mutant alleles in familial
RT lecithin:cholesterol acyltransferase deficiency.";
RL Lancet 338:778-781(1991).
RN [29]
RP VARIANT FED LYS-276.
RX PubMed=1516702; DOI=10.1016/0014-5793(92)80795-i;
RA Skretting G., Blomhoff J.P., Solheim J., Prydz H.;
RT "The genetic defect of the original Norwegian lecithin:cholesterol
RT acyltransferase deficiency families.";
RL FEBS Lett. 309:307-310(1992).
RN [30]
RP VARIANT LCATD ILE-317.
RX PubMed=1859405; DOI=10.1016/0006-291x(91)90129-u;
RA Maeda E., Naka Y., Matozaki T., Sakuma M., Akanuma Y., Yoshino G.,
RA Kasuga M.;
RT "Lecithin-cholesterol acyltransferase (LCAT) deficiency with a missense
RT mutation in exon 6 of the LCAT gene.";
RL Biochem. Biophys. Res. Commun. 178:460-466(1991).
RN [31]
RP VARIANTS LCATD THR-117; TRP-159; PRO-233 AND MET-345, AND VARIANT CYS-182.
RX PubMed=8432868; DOI=10.1172/jci116248;
RA Funke H., von Eckardstein A., Pritchard P.H., Hornby A.E., Wiebusch H.,
RA Motti C., Hayden M.R., Dachet C., Jacotot B., Gerdes U., Faergeman O.,
RA Albers J.J., Colleoni N., Catapano A., Frohlich J., Assmann G.;
RT "Genetic and phenotypic heterogeneity in familial lecithin: cholesterol
RT acyltransferase (LCAT) deficiency. Six newly identified defective alleles
RT further contribute to the structural heterogeneity in this disease.";
RL J. Clin. Invest. 91:677-683(1993).
RN [32]
RP VARIANT LCATD THR-117, AND VARIANT CYS-182.
RX PubMed=8318557; DOI=10.1016/0925-4439(93)90039-4;
RA Hill J.S., O K., Wang X., Pritchard P.H.;
RT "Lecithin:cholesterol acyltransferase deficiency: identification of a
RT causative gene mutation and a co-inherited protein polymorphism.";
RL Biochim. Biophys. Acta 1181:321-323(1993).
RN [33]
RP VARIANT LCATD HIS-164, AND CHARACTERIZATION OF VARIANT LCATD HIS-164.
RX PubMed=7607641; DOI=10.1007/bf00214196;
RA Steyrer E., Haubenwallner S., Hoerl G., Giessauf W., Kostner G.M.,
RA Zechner R.;
RT "A single G to A nucleotide transition in exon IV of the lecithin:
RT cholesterol acyltransferase (LCAT) gene results in an Arg140 to His
RT substitution and causes LCAT-deficiency.";
RL Hum. Genet. 96:105-109(1995).
RN [34]
RP VARIANTS LCATD ARG-57 AND LEU-LEU-PRO-PRO-ALA-ALA-PRO-PHE-TRP-LEU-17 INS.
RX PubMed=7711728; DOI=10.1093/hmg/4.1.143;
RA Wiebusch H., Cullen P., Owen J.S., Collins D., Sharp P.S., Funke H.,
RA Assmann G.;
RT "Deficiency of lecithin:cholesterol acyltransferase due to compound
RT heterozygosity of two novel mutations (Gly33Arg and 30 bp ins) in the LCAT
RT gene.";
RL Hum. Mol. Genet. 4:143-145(1995).
RN [35]
RP VARIANTS FED GLN-34 AND GLN-159.
RX PubMed=8620346; DOI=10.1161/01.atv.16.2.294;
RA Kuivenhoven J.A., Stalenhoef A.F., Hill J.S., Demacker P.N., Errami A.,
RA Kastelein J.J., Pritchard P.H.;
RT "Two novel molecular defects in the LCAT gene are associated with fish eye
RT disease.";
RL Arterioscler. Thromb. Vasc. Biol. 16:294-303(1996).
RN [36]
RP VARIANT LCATD SER-54.
RX PubMed=8807342;
RX DOI=10.1002/(sici)1098-1004(1996)8:1<79::aid-humu13>3.0.co;2-o;
RA Owen J.S., Wiebusch H., Cullen P., Watts G.F., Lima V.L.M., Funke H.,
RA Assmann G.;
RT "Complete deficiency of plasma lecithin-cholesterol acyltransferase (LCAT)
RT activity due to a novel homozygous mutation (Gly-30-Ser) in the LCAT
RT gene.";
RL Hum. Mutat. 8:79-82(1996).
RN [37]
RP VARIANT LCATD ILE-29.
RX PubMed=9007616; DOI=10.1007/bf02602958;
RA Okubo M., Aoyama Y., Shio H., Albers J.J., Murase T.;
RT "A novel missense mutation (Asn5-->Ile) in lecithin: cholesterol
RT acyltransferase (LCAT) gene in a Japanese patient with LCAT deficiency.";
RL Int. J. Clin. Lab. Res. 26:250-254(1996).
RN [38]
RP VARIANT FED CYS-123.
RX PubMed=9261271; DOI=10.1161/01.atv.17.7.1382;
RA Blanco-Vaca F., Qu S.J., Fiol C., Fan H.Z., Pao Q., Marzal-Casacuberta A.,
RA Albers J.J., Hurtado I., Gracia V., Pinto X., Marti T., Pownall H.J.;
RT "Molecular basis of fish-eye disease in a patient from Spain.
RT Characterization of a novel mutation in the LCAT gene and lipid analysis of
RT the cornea.";
RL Arterioscler. Thromb. Vasc. Biol. 17:1382-1391(1997).
RN [39]
RP VARIANTS LCATD MET-37 AND SER-331.
RX PubMed=9741700;
RA Argyropoulos G., Jenkins A., Klein R.L., Lyons T., Wagenhorst B.,
RA St Armand J., Marcovina S.M., Albers J.J., Pritchard P.H., Garvey W.T.;
RT "Transmission of two novel mutations in a pedigree with familial
RT lecithin:cholesterol acyltransferase deficiency: structure-function
RT relationships and studies in a compound heterozygous proband.";
RL J. Lipid Res. 39:1870-1876(1998).
RN [40]
RP VARIANT LCATD ALA-298.
RX PubMed=11423760; DOI=10.1159/000046001;
RA Sessa A., Battini G., Meroni M., Daidone G., Carnera I., Brambilla P.L.,
RA Vigano G., Giordano F., Pallotti F., Torri Tarelli L., Calabresi L.,
RA Rolleri M., Bertolini S.;
RT "Hypocomplementemic type II membranoproliferative glomerulonephritis in a
RT male patient with familial lecithin-cholesterol acyltransferase deficiency
RT due to two different allelic mutations.";
RL Nephron 88:268-272(2001).
RN [41]
RP VARIANTS LCATD MET-345 AND VAL-406, AND VARIANT THR-232.
RX PubMed=12957688; DOI=10.1016/s0021-9150(03)00241-7;
RA Nanjee M.N., Stocks J., Cooke C.J., Molhuizen H.O., Marcovina S., Crook D.,
RA Kastelein J.P., Miller N.E.;
RT "A novel LCAT mutation (Phe382-->Val) in a kindred with familial LCAT
RT deficiency and defective apolipoprotein B-100.";
RL Atherosclerosis 170:105-113(2003).
RN [42]
RP VARIANT THR-232.
RX PubMed=12966036; DOI=10.1093/hmg/ddg314;
RA Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
RA Alvin G.B., Das K., Gilliam T.C.;
RT "Association of extreme blood lipid profile phenotypic variation with 11
RT reverse cholesterol transport genes and 10 non-genetic cardiovascular
RT disease risk factors.";
RL Hum. Mol. Genet. 12:2733-2743(2003).
RN [43]
RP VARIANTS FED GLU-70 AND ALA-298, VARIANTS LCATD CYS-164; TRP-171; ASN-205;
RP ASN-242; HIS-268; ILE-298 AND MET-333, AND VARIANTS PRO-115; THR-165 AND
RP ARG-396.
RX PubMed=15994445; DOI=10.1161/01.atv.0000175751.30616.13;
RA Calabresi L., Pisciotta L., Costantin A., Frigerio I., Eberini I.,
RA Alessandrini P., Arca M., Bon G.B., Boscutti G., Busnach G., Frasca G.,
RA Gesualdo L., Gigante M., Lupattelli G., Montali A., Pizzolitto S.,
RA Rabbone I., Rolleri M., Ruotolo G., Sampietro T., Sessa A., Vaudo G.,
RA Cantafora A., Veglia F., Calandra S., Bertolini S., Franceschini G.;
RT "The molecular basis of lecithin:cholesterol acyltransferase deficiency
RT syndromes: a comprehensive study of molecular and biochemical findings in
RT 13 unrelated Italian families.";
RL Arterioscler. Thromb. Vasc. Biol. 25:1972-1978(2005).
RN [44]
RP VARIANT LCATD MET-333.
RX PubMed=16051254; DOI=10.1016/j.atherosclerosis.2005.06.022;
RA Idzior-Walus B., Sieradzki J., Kostner G., Malecki M.T., Klupa T.,
RA Wesolowska T., Rostworowski W., Hartwich J., Walus M., Kiec A.D.,
RA Naruszewicz M.;
RT "Familial lecithin-cholesterol acyltransferase deficiency: biochemical
RT characteristics and molecular analysis of a new LCAT mutation in a Polish
RT family.";
RL Atherosclerosis 185:413-420(2006).
RN [45]
RP VARIANT ARG-95, VARIANT LCATD HIS-164, AND CHARACTERIZATION OF VARIANT
RP ARG-95.
RX PubMed=16216249; DOI=10.1016/j.atherosclerosis.2005.08.038;
RA Hoerl G., Kroisel P.M., Wagner E., Tiran B., Petek E., Steyrer E.;
RT "Compound heterozygosity (G71R/R140H) in the lecithin:cholesterol
RT acyltransferase (LCAT) gene results in an intermediate phenotype between
RT LCAT-deficiency and fish-eye disease.";
RL Atherosclerosis 187:101-109(2006).
RN [46]
RP VARIANTS THR-232 AND ARG-396.
RX PubMed=16874701;
RA Gigante M., Ranieri E., Cerullo G., Calabresi L., Iolascon A., Assmann G.,
RA Morrone L., Pisciotta L., Schena F.P., Gesualdo L.;
RT "LCAT deficiency: molecular and phenotypic characterization of an Italian
RT family.";
RL J. Nephrol. 19:375-381(2006).
RN [47]
RP VARIANTS 134-GLU-TYR-135 DELINS ASP-ASN; PHE-246; CYS-268 AND CYS-322,
RP VARIANTS FED SER-99; PHE-338 AND CYS-347, CHARACTERIZATION OF VARIANTS
RP 134-GLU-TYR-135 DELINS ASP-ASN; PHE-246; CYS-268 AND CYS-322, AND
RP CHARACTERIZATION OF VARIANTS FED SER-99; PHE-338 CYS-347 AND CYS-347.
RX PubMed=21901787; DOI=10.1002/humu.21578;
RA Holleboom A.G., Kuivenhoven J.A., Peelman F., Schimmel A.W., Peter J.,
RA Defesche J.C., Kastelein J.J., Hovingh G.K., Stroes E.S., Motazacker M.M.;
RT "High prevalence of mutations in LCAT in patients with low HDL cholesterol
RT levels in The Netherlands: identification and characterization of eight
RT novel mutations.";
RL Hum. Mutat. 32:1290-1298(2011).
CC -!- FUNCTION: Central enzyme in the extracellular metabolism of plasma
CC lipoproteins. Synthesized mainly in the liver and secreted into plasma
CC where it converts cholesterol and phosphatidylcholines (lecithins) to
CC cholesteryl esters and lysophosphatidylcholines on the surface of high
CC and low density lipoproteins (HDLs and LDLs) (PubMed:10329423,
CC PubMed:19065001, PubMed:26195816). The cholesterol ester is then
CC transported back to the liver. Has a preference for plasma 16:0-18:2 or
CC 18:O-18:2 phosphatidylcholines (PubMed:8820107). Also produced in the
CC brain by primary astrocytes, and esterifies free cholesterol on nascent
CC APOE-containing lipoproteins secreted from glia and influences cerebral
CC spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and the
CC cholesterol transporter ABCA1, plays a key role in the maturation of
CC glial-derived, nascent lipoproteins. Required for remodeling high-
CC density lipoprotein particles into their spherical forms
CC (PubMed:10722751). Catalyzes the hydrolysis of 1-O-alkyl-2-acetyl-sn-
CC glycero-3-phosphocholine (platelet-activating factor or PAF) to 1-O-
CC alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (PubMed:8016111). Also
CC catalyzes the transfer of the acetate group from PAF to 1-hexadecanoyl-
CC sn-glycero-3-phosphocholine forming lyso-PAF (PubMed:8016111).
CC Catalyzes the esterification of (24S)-hydroxycholesterol (24(S)OH-C),
CC also known as cerebrosterol to produce 24(S)OH-C monoesters
CC (PubMed:24620755). {ECO:0000269|PubMed:10329423,
CC ECO:0000269|PubMed:10722751, ECO:0000269|PubMed:12354767,
CC ECO:0000269|PubMed:14636062, ECO:0000269|PubMed:19065001,
CC ECO:0000269|PubMed:24620755, ECO:0000269|PubMed:26195816,
CC ECO:0000269|PubMed:8016111, ECO:0000269|PubMed:8820107}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a sterol = a 1-
CC acyl-sn-glycero-3-phosphocholine + a sterol ester;
CC Xref=Rhea:RHEA:21204, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=2.3.1.43;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10037,
CC ECO:0000269|PubMed:10222237, ECO:0000269|PubMed:10329423,
CC ECO:0000269|PubMed:14636062, ECO:0000269|PubMed:19065001,
CC ECO:0000269|PubMed:25727495, ECO:0000269|PubMed:26195816,
CC ECO:0000269|PubMed:3458198, ECO:0000269|PubMed:8820107};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC Evidence={ECO:0000269|PubMed:8016111};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000305|PubMed:8016111};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + 1-hexadecanoyl-2-acyl-sn-glycero-3-
CC phosphocholine = (24S)-24-hydroxycholesterol ester + 1-hexadecanoyl-
CC sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:43216, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:77369, ChEBI:CHEBI:82869;
CC Evidence={ECO:0000269|PubMed:24620755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43217;
CC Evidence={ECO:0000305|PubMed:24620755};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphocholine = (24S)-
CC hydroxycholesterol 3-linoleoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine; Xref=Rhea:RHEA:43224, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002, ChEBI:CHEBI:82875;
CC Evidence={ECO:0000269|PubMed:24620755};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43225;
CC Evidence={ECO:0000305|PubMed:24620755};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate;
CC Xref=Rhea:RHEA:53448, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73003, ChEBI:CHEBI:82751;
CC Evidence={ECO:0000269|PubMed:14636062};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53449;
CC Evidence={ECO:0000305|PubMed:14636062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + cholesterol = 1-hexadecanoyl-sn-glycero-3-phosphocholine +
CC cholesteryl (9Z-octadecenoate); Xref=Rhea:RHEA:53456,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:46898, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:14636062};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53457;
CC Evidence={ECO:0000305|PubMed:14636062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(8Z,11Z,14Z-eicosatrienoyl)-sn-glycero-3-
CC phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + cholesteryl (8Z,11Z,14Z)-eicosatrienoate;
CC Xref=Rhea:RHEA:53464, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:84346, ChEBI:CHEBI:86121;
CC Evidence={ECO:0000269|PubMed:14636062};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53465;
CC Evidence={ECO:0000305|PubMed:14636062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z-eicosatrienoyl)-sn-glycero-3-
CC phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + cholesteryl (5Z,8Z,11Z)-eicosatrienoate;
CC Xref=Rhea:RHEA:53460, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:86119, ChEBI:CHEBI:88752;
CC Evidence={ECO:0000269|PubMed:14636062};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53461;
CC Evidence={ECO:0000305|PubMed:14636062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl)-sn-
CC glycero-3-phosphocholine + cholesterol = (5Z,8Z,11Z,14Z,17Z-
CC eicosapentaenoyl)-cholesterol + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine; Xref=Rhea:RHEA:53468, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:84969, ChEBI:CHEBI:86137;
CC Evidence={ECO:0000269|PubMed:14636062};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53469;
CC Evidence={ECO:0000305|PubMed:14636062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + cholesteryl (9Z,12Z)-octadecadienoate;
CC Xref=Rhea:RHEA:53472, ChEBI:CHEBI:16113, ChEBI:CHEBI:41509,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000269|PubMed:14636062};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53473;
CC Evidence={ECO:0000305|PubMed:14636062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(6Z,9Z,12Z-octadecatrienoyl)-sn-glycero-3-
CC phosphocholine + cholesterol = (6Z,9Z,12Z-octadecatrienoyl)-
CC cholesterol + 1-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:53476, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:84786, ChEBI:CHEBI:88756;
CC Evidence={ECO:0000269|PubMed:14636062};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53477;
CC Evidence={ECO:0000305|PubMed:14636062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(11Z,14Z,17Z-eicosatrienoyl)-sn-glycero-3-
CC phosphocholine + cholesterol = (11Z,14Z,17Z-eicosatrienoyl)-
CC cholesterol + 1-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:53516, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:137411, ChEBI:CHEBI:137412;
CC Evidence={ECO:0000269|PubMed:14636062};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53517;
CC Evidence={ECO:0000305|PubMed:14636062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-
CC phosphocholine + cholesterol = (9Z,12Z,15Z-octadecatrienoyl)-
CC cholesterol + 1-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:53520, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:84341, ChEBI:CHEBI:84789;
CC Evidence={ECO:0000269|PubMed:14636062};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53521;
CC Evidence={ECO:0000305|PubMed:14636062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000269|PubMed:14636062};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000305|PubMed:14636062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000269|PubMed:14636062};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000305|PubMed:14636062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + a 1-O-alkyl-2-
CC acetyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-acetyl-sn-
CC glycero-3-phosphocholine + 1-O-alkyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:53636, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75219;
CC Evidence={ECO:0000269|PubMed:8016111};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53637;
CC Evidence={ECO:0000305|PubMed:8016111};
CC -!- ACTIVITY REGULATION: APOA1 is the most potent activator in plasma
CC (PubMed:19065001, PubMed:8016111). Also activated by APOE, APOC1 and
CC APOA4 (PubMed:19065001, PubMed:8016111). Inhibited by haptoglobin and
CC 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) (PubMed:8016111,
CC PubMed:24620755). {ECO:0000269|PubMed:19065001,
CC ECO:0000269|PubMed:24620755, ECO:0000269|PubMed:8016111}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.97 mM for LDL {ECO:0000269|PubMed:10329423};
CC KM=0.4 mM for HDL(2) {ECO:0000269|PubMed:10329423};
CC KM=0.10 mM for HDL(3) {ECO:0000269|PubMed:10329423};
CC KM=12.8 uM for 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine
CC {ECO:0000269|PubMed:8016111};
CC KM=125.5 uM for (24S)-hydroxycholesterol (in the presence of APOA1)
CC {ECO:0000269|PubMed:24620755};
CC KM=417.3 uM for (24S)-hydroxycholesterol (in the presence of APOE)
CC {ECO:0000269|PubMed:24620755};
CC Vmax=8.3 mmol/min/mg enzyme with LDL as substrate
CC {ECO:0000269|PubMed:10329423};
CC Vmax=0.58 mmol/min/mg enzyme with HDL(2) as substrate
CC {ECO:0000269|PubMed:10329423};
CC Vmax=2.0 mmol/min/mg enzyme with HDL(3) as substrate
CC {ECO:0000269|PubMed:10329423};
CC Vmax=0.2 umol/h/mg enzyme with 1-O-alkyl-2-acetyl-sn-glycero-3-
CC phosphocholine as substrate {ECO:0000269|PubMed:8016111};
CC Vmax=12 umol/h/mg enzyme with cholesterol as substrate
CC {ECO:0000269|PubMed:8016111};
CC Note=Affinity for LDL is 2.3 to 4-fold lower than for HDL. Relative
CC reactivities are 16% for HDL(3), 1.3% for HDL(2) and 6.5% for LDL.;
CC -!- INTERACTION:
CC P04180; P02647: APOA1; NbExp=2; IntAct=EBI-9104464, EBI-701692;
CC P04180; O76024: WFS1; NbExp=3; IntAct=EBI-9104464, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10222237,
CC ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:3458198,
CC ECO:0000269|PubMed:8016111, ECO:0000269|PubMed:8820107}. Note=Secreted
CC into blood plasma (PubMed:3458198, PubMed:8820107, PubMed:10222237).
CC Produced in astrocytes and secreted into cerebral spinal fluid (CSF)
CC (PubMed:10222237). {ECO:0000269|PubMed:10222237,
CC ECO:0000269|PubMed:3458198, ECO:0000269|PubMed:8820107}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (PubMed:3458198,
CC PubMed:8820107, PubMed:10222237). Detected in cerebral spinal fluid (at
CC protein level) (PubMed:10222237). Detected in liver (PubMed:3797244,
CC PubMed:3458198). Expressed mainly in brain, liver and testes.
CC {ECO:0000269|PubMed:10222237, ECO:0000269|PubMed:3458198,
CC ECO:0000269|PubMed:3797244, ECO:0000269|PubMed:8820107}.
CC -!- PTM: O- and N-glycosylated. O-glycosylation on Thr-431 and Ser-433
CC consists of sialylated galactose beta 1-->3N-acetylgalactosamine
CC structures. N-glycosylated sites contain sialylated triantennary and/or
CC biantennary complex structures. {ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:7613477}.
CC -!- DISEASE: Lecithin-cholesterol acyltransferase deficiency (LCATD)
CC [MIM:245900]: A disorder of lipoprotein metabolism characterized by
CC inadequate esterification of plasmatic cholesterol. Two clinical forms
CC are recognized: complete LCAT deficiency and fish-eye disease. LCATD is
CC generally referred to the complete form which is associated with
CC absence of both alpha and beta LCAT activities resulting in
CC esterification anomalies involving both HDL (alpha-LCAT activity) and
CC LDL (beta-LCAT activity). It causes a typical triad of diffuse corneal
CC opacities, target cell hemolytic anemia, and proteinuria with renal
CC failure. {ECO:0000269|PubMed:11423760, ECO:0000269|PubMed:12957688,
CC ECO:0000269|PubMed:15994445, ECO:0000269|PubMed:16051254,
CC ECO:0000269|PubMed:16216249, ECO:0000269|PubMed:1681161,
CC ECO:0000269|PubMed:1859405, ECO:0000269|PubMed:2370048,
CC ECO:0000269|PubMed:7607641, ECO:0000269|PubMed:7711728,
CC ECO:0000269|PubMed:8318557, ECO:0000269|PubMed:8432868,
CC ECO:0000269|PubMed:8807342, ECO:0000269|PubMed:9007616,
CC ECO:0000269|PubMed:9741700}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Fish-eye disease (FED) [MIM:136120]: A disorder of lipoprotein
CC metabolism due to partial lecithin-cholesterol acyltransferase
CC deficiency that affects only alpha-LCAT activity. FED is characterized
CC by low plasma HDL and corneal opacities due to accumulation of
CC cholesterol deposits in the cornea ('fish-eye').
CC {ECO:0000269|PubMed:1516702, ECO:0000269|PubMed:1571050,
CC ECO:0000269|PubMed:15994445, ECO:0000269|PubMed:1737840,
CC ECO:0000269|PubMed:21901787, ECO:0000269|PubMed:8620346,
CC ECO:0000269|PubMed:9261271}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Levels of LCAT activity correlates inversely with leptin
CC levels as well as with obesity for a wide range of BMI values.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Lecithin-cholesterol acyltransferase
CC entry;
CC URL="https://en.wikipedia.org/wiki/Lecithin-cholesterol_acyltransferase";
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DR EMBL; X04981; CAA28651.1; -; Genomic_DNA.
DR EMBL; M12625; AAA59498.1; -; mRNA.
DR EMBL; AY422210; AAR03499.1; -; Genomic_DNA.
DR EMBL; BT009748; AAP88750.1; -; mRNA.
DR EMBL; AC040162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW83190.1; -; Genomic_DNA.
DR EMBL; BC014781; AAH14781.1; -; mRNA.
DR EMBL; M26268; AAA59499.1; -; mRNA.
DR EMBL; X06537; CAB56610.1; -; mRNA.
DR EMBL; M17959; AAA59500.1; -; Genomic_DNA.
DR CCDS; CCDS10854.1; -.
DR PIR; A00571; XXHUN.
DR RefSeq; NP_000220.1; NM_000229.1.
DR PDB; 4X96; X-ray; 8.69 A; A/B/C/D=45-421.
DR PDB; 4XWG; X-ray; 2.65 A; A=25-440.
DR PDB; 4XX1; X-ray; 3.60 A; A/B/J=25-440.
DR PDB; 5BV7; X-ray; 2.45 A; A=25-440.
DR PDB; 5TXF; X-ray; 3.10 A; A/B/C/D=25-440.
DR PDB; 6MVD; X-ray; 3.10 A; A/B=45-421.
DR PDBsum; 4X96; -.
DR PDBsum; 4XWG; -.
DR PDBsum; 4XX1; -.
DR PDBsum; 5BV7; -.
DR PDBsum; 5TXF; -.
DR PDBsum; 6MVD; -.
DR AlphaFoldDB; P04180; -.
DR SMR; P04180; -.
DR BioGRID; 110123; 6.
DR DIP; DIP-29620N; -.
DR IntAct; P04180; 2.
DR STRING; 9606.ENSP00000264005; -.
DR BindingDB; P04180; -.
DR ChEMBL; CHEMBL5942; -.
DR SwissLipids; SLP:000000660; -.
DR ESTHER; human-LCAT; PC-sterol_acyltransferase.
DR GlyConnect; 495; 13 N-Linked glycans (2 sites).
DR GlyGen; P04180; 7 sites, 18 N-linked glycans (3 sites).
DR iPTMnet; P04180; -.
DR PhosphoSitePlus; P04180; -.
DR BioMuta; LCAT; -.
DR DMDM; 125993; -.
DR jPOST; P04180; -.
DR MassIVE; P04180; -.
DR MaxQB; P04180; -.
DR PaxDb; P04180; -.
DR PeptideAtlas; P04180; -.
DR PRIDE; P04180; -.
DR ProteomicsDB; 51671; -.
DR ABCD; P04180; 3 sequenced antibodies.
DR Antibodypedia; 15960; 400 antibodies from 34 providers.
DR DNASU; 3931; -.
DR Ensembl; ENST00000264005.10; ENSP00000264005.5; ENSG00000213398.8.
DR GeneID; 3931; -.
DR KEGG; hsa:3931; -.
DR MANE-Select; ENST00000264005.10; ENSP00000264005.5; NM_000229.2; NP_000220.1.
DR UCSC; uc002euy.2; human.
DR CTD; 3931; -.
DR DisGeNET; 3931; -.
DR GeneCards; LCAT; -.
DR HGNC; HGNC:6522; LCAT.
DR HPA; ENSG00000213398; Tissue enriched (liver).
DR MalaCards; LCAT; -.
DR MIM; 136120; phenotype.
DR MIM; 245900; phenotype.
DR MIM; 606967; gene.
DR neXtProt; NX_P04180; -.
DR OpenTargets; ENSG00000213398; -.
DR Orphanet; 79293; Familial LCAT deficiency.
DR Orphanet; 79292; Fish-eye disease.
DR PharmGKB; PA226; -.
DR VEuPathDB; HostDB:ENSG00000213398; -.
DR eggNOG; KOG2369; Eukaryota.
DR GeneTree; ENSGT00940000160052; -.
DR InParanoid; P04180; -.
DR OMA; WEDTKNL; -.
DR OrthoDB; 828056at2759; -.
DR PhylomeDB; P04180; -.
DR TreeFam; TF313258; -.
DR BRENDA; 2.3.1.43; 2681.
DR PathwayCommons; P04180; -.
DR Reactome; R-HSA-8964058; HDL remodeling.
DR SABIO-RK; P04180; -.
DR SignaLink; P04180; -.
DR SIGNOR; P04180; -.
DR BioGRID-ORCS; 3931; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; LCAT; human.
DR GeneWiki; Lecithin%E2%80%94cholesterol_acyltransferase; -.
DR GenomeRNAi; 3931; -.
DR Pharos; P04180; Tchem.
DR PRO; PR:P04180; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P04180; protein.
DR Bgee; ENSG00000213398; Expressed in right lobe of liver and 121 other tissues.
DR ExpressionAtlas; P04180; baseline and differential.
DR Genevisible; P04180; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IDA:UniProtKB.
DR GO; GO:0034186; F:apolipoprotein A-I binding; IPI:BHF-UCL.
DR GO; GO:0004607; F:phosphatidylcholine-sterol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:Ensembl.
DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0034435; P:cholesterol esterification; IDA:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
DR GO; GO:0008203; P:cholesterol metabolic process; IDA:UniProtKB.
DR GO; GO:0030301; P:cholesterol transport; IDA:MGI.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:BHF-UCL.
DR GO; GO:0090107; P:regulation of high-density lipoprotein particle assembly; IEA:Ensembl.
DR GO; GO:0046688; P:response to copper ion; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; IDA:BHF-UCL.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
DR Gene3D; 3.40.50.1820; -; 3.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR Pfam; PF02450; LCAT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cholesterol metabolism; Corneal dystrophy;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid metabolism; Reference proteome; Secreted; Signal;
KW Steroid metabolism; Sterol metabolism; Transferase.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:3458198"
FT CHAIN 25..440
FT /note="Phosphatidylcholine-sterol acyltransferase"
FT /id="PRO_0000017802"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:26195816"
FT ACT_SITE 369
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:26195816"
FT ACT_SITE 401
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:26195816"
FT SITE 173
FT /note="Determinant for substrate specificity"
FT /evidence="ECO:0000305|PubMed:14636062"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:7613477"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:26195816,
FT ECO:0000269|PubMed:7613477, ECO:0007744|PDB:4X96"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:26195816, ECO:0000269|PubMed:7613477,
FT ECO:0007744|PDB:4X96"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:26195816,
FT ECO:0000269|PubMed:7613477, ECO:0007744|PDB:4X96"
FT CARBOHYD 431
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7613477"
FT CARBOHYD 433
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:7613477"
FT DISULFID 74..98
FT /evidence="ECO:0000269|PubMed:26195816,
FT ECO:0000269|PubMed:2880847, ECO:0007744|PDB:4X96,
FT ECO:0007744|PDB:4XWG, ECO:0007744|PDB:4XX1"
FT DISULFID 337..380
FT /evidence="ECO:0000269|PubMed:26195816,
FT ECO:0000269|PubMed:2880847, ECO:0007744|PDB:4X96,
FT ECO:0007744|PDB:4XWG, ECO:0007744|PDB:4XX1"
FT VARIANT 17
FT /note="L -> LLLPPAAPFWL (in LCATD)"
FT /id="VAR_004251"
FT VARIANT 29
FT /note="N -> I (in LCATD)"
FT /evidence="ECO:0000269|PubMed:9007616"
FT /id="VAR_039020"
FT VARIANT 34
FT /note="P -> L (in FED; dbSNP:rs121908051)"
FT /evidence="ECO:0000269|PubMed:1571050"
FT /id="VAR_004252"
FT VARIANT 34
FT /note="P -> Q (in FED)"
FT /evidence="ECO:0000269|PubMed:8620346"
FT /id="VAR_039021"
FT VARIANT 37
FT /note="T -> M (in LCATD; dbSNP:rs971887742)"
FT /evidence="ECO:0000269|PubMed:9741700"
FT /id="VAR_039022"
FT VARIANT 54
FT /note="G -> S (in LCATD; dbSNP:rs1461145750)"
FT /evidence="ECO:0000269|PubMed:8807342"
FT /id="VAR_004253"
FT VARIANT 57
FT /note="G -> R (in LCATD)"
FT /evidence="ECO:0000269|PubMed:7711728"
FT /id="VAR_004254"
FT VARIANT 70
FT /note="V -> E (in FED; dbSNP:rs748427834)"
FT /evidence="ECO:0000269|PubMed:15994445"
FT /id="VAR_039023"
FT VARIANT 95
FT /note="G -> R (found in a patient with intermediate
FT phenotype between LCATD and FED; reduction of activity)"
FT /evidence="ECO:0000269|PubMed:16216249"
FT /id="VAR_039024"
FT VARIANT 99
FT /note="W -> S (in FED; loss of activity)"
FT /evidence="ECO:0000269|PubMed:21901787"
FT /id="VAR_066862"
FT VARIANT 115
FT /note="S -> P (in dbSNP:rs1412883954)"
FT /evidence="ECO:0000269|PubMed:15994445"
FT /id="VAR_039025"
FT VARIANT 117
FT /note="A -> T (in LCATD; dbSNP:rs28940886)"
FT /evidence="ECO:0000269|PubMed:8318557,
FT ECO:0000269|PubMed:8432868"
FT /id="VAR_004255"
FT VARIANT 123
FT /note="R -> C (in FED; dbSNP:rs140068549)"
FT /evidence="ECO:0000269|PubMed:9261271"
FT /id="VAR_039026"
FT VARIANT 134..135
FT /note="EY -> DN (in a patient with low HDL-cholesterol
FT levels; results in reduced activity)"
FT /evidence="ECO:0000269|PubMed:21901787"
FT /id="VAR_066863"
FT VARIANT 147
FT /note="T -> I (in FED; dbSNP:rs121908050)"
FT /evidence="ECO:0000269|PubMed:1737840"
FT /id="VAR_004256"
FT VARIANT 159
FT /note="R -> Q (in FED; dbSNP:rs768017317)"
FT /evidence="ECO:0000269|PubMed:8620346"
FT /id="VAR_039027"
FT VARIANT 159
FT /note="R -> W (in LCATD; dbSNP:rs28940887)"
FT /evidence="ECO:0000269|PubMed:8432868"
FT /id="VAR_004257"
FT VARIANT 164
FT /note="R -> C (in LCATD; dbSNP:rs1380009545)"
FT /evidence="ECO:0000269|PubMed:15994445"
FT /id="VAR_039028"
FT VARIANT 164
FT /note="R -> H (in LCATD; also found in a patient with
FT intermediate phenotype between LCATD and FED; loss of
FT activity; dbSNP:rs769485083)"
FT /evidence="ECO:0000269|PubMed:16216249,
FT ECO:0000269|PubMed:7607641"
FT /id="VAR_004258"
FT VARIANT 165
FT /note="A -> T (in dbSNP:rs1369994093)"
FT /evidence="ECO:0000269|PubMed:15994445"
FT /id="VAR_039029"
FT VARIANT 171
FT /note="R -> W (in LCATD)"
FT /evidence="ECO:0000269|PubMed:15994445,
FT ECO:0000269|PubMed:2370048"
FT /id="VAR_004259"
FT VARIANT 180
FT /note="Y -> N (in LCATD; dbSNP:rs749740660)"
FT /id="VAR_004260"
FT VARIANT 182
FT /note="R -> C (in dbSNP:rs387906300)"
FT /evidence="ECO:0000269|PubMed:8318557,
FT ECO:0000269|PubMed:8432868"
FT /id="VAR_004261"
FT VARIANT 205
FT /note="S -> N (in LCATD)"
FT /evidence="ECO:0000269|PubMed:15994445"
FT /id="VAR_039030"
FT VARIANT 232
FT /note="S -> T (in dbSNP:rs4986970)"
FT /evidence="ECO:0000269|PubMed:12957688,
FT ECO:0000269|PubMed:12966036, ECO:0000269|PubMed:16874701"
FT /id="VAR_017030"
FT VARIANT 233
FT /note="L -> P (in LCATD; dbSNP:rs28942087)"
FT /evidence="ECO:0000269|PubMed:8432868"
FT /id="VAR_004262"
FT VARIANT 242
FT /note="K -> N (in LCATD)"
FT /evidence="ECO:0000269|PubMed:15994445"
FT /id="VAR_039031"
FT VARIANT 246
FT /note="V -> F (in a patient with low HDL-cholesterol
FT levels; the mutant is hardly secreted and is catalytically
FT inactive)"
FT /evidence="ECO:0000269|PubMed:21901787"
FT /id="VAR_066864"
FT VARIANT 252
FT /note="N -> K (in LCATD; dbSNP:rs121908049)"
FT /evidence="ECO:0000269|PubMed:1681161"
FT /id="VAR_004263"
FT VARIANT 268
FT /note="R -> C (in a patient with low HDL-cholesterol
FT levels; the mutant is hardly secreted and is catalytically
FT inactive; dbSNP:rs745320775)"
FT /evidence="ECO:0000269|PubMed:21901787"
FT /id="VAR_066865"
FT VARIANT 268
FT /note="R -> H (in LCATD; dbSNP:rs780824776)"
FT /evidence="ECO:0000269|PubMed:15994445"
FT /id="VAR_039032"
FT VARIANT 276
FT /note="M -> K (in FED; dbSNP:rs121908054)"
FT /evidence="ECO:0000269|PubMed:1516702"
FT /id="VAR_004264"
FT VARIANT 298
FT /note="T -> A (in FED and LCATD)"
FT /evidence="ECO:0000269|PubMed:11423760,
FT ECO:0000269|PubMed:15994445"
FT /id="VAR_039033"
FT VARIANT 298
FT /note="T -> I (in LCATD)"
FT /evidence="ECO:0000269|PubMed:15994445"
FT /id="VAR_039034"
FT VARIANT 317
FT /note="M -> I (in LCATD; partially defective enzyme;
FT dbSNP:rs121908048)"
FT /evidence="ECO:0000269|PubMed:1681161,
FT ECO:0000269|PubMed:1859405"
FT /id="VAR_004265"
FT VARIANT 322
FT /note="R -> C (in a patient with low HDL-cholesterol
FT levels; reduced protein secretion; dbSNP:rs1407191796)"
FT /evidence="ECO:0000269|PubMed:21901787"
FT /id="VAR_066866"
FT VARIANT 331
FT /note="P -> S (in LCATD)"
FT /evidence="ECO:0000269|PubMed:9741700"
FT /id="VAR_039035"
FT VARIANT 333
FT /note="V -> M (in LCATD; dbSNP:rs776035233)"
FT /evidence="ECO:0000269|PubMed:15994445,
FT ECO:0000269|PubMed:16051254"
FT /id="VAR_039036"
FT VARIANT 338
FT /note="L -> F (in FED; results in reduced protein secretion
FT and activity; dbSNP:rs1330635214)"
FT /evidence="ECO:0000269|PubMed:21901787"
FT /id="VAR_066867"
FT VARIANT 345
FT /note="T -> M (in LCATD; dbSNP:rs28940888)"
FT /evidence="ECO:0000269|PubMed:12957688,
FT ECO:0000269|PubMed:8432868"
FT /id="VAR_004266"
FT VARIANT 347
FT /note="R -> C (in FED; results in reduced activity;
FT dbSNP:rs202017590)"
FT /evidence="ECO:0000269|PubMed:21901787"
FT /id="VAR_066868"
FT VARIANT 371
FT /note="T -> M (in FED; dbSNP:rs121908053)"
FT /evidence="ECO:0000269|PubMed:1737840"
FT /id="VAR_004267"
FT VARIANT 396
FT /note="L -> R (in a patient with LCATD)"
FT /evidence="ECO:0000269|PubMed:15994445,
FT ECO:0000269|PubMed:16874701"
FT /id="VAR_039037"
FT VARIANT 406
FT /note="F -> V (in LCATD)"
FT /evidence="ECO:0000269|PubMed:12957688"
FT /id="VAR_039038"
FT MUTAGEN 173
FT /note="E->A: Increased activity towards PAPC. Increased
FT PAPC/POPC activity ratio."
FT /evidence="ECO:0000269|PubMed:14636062"
FT MUTAGEN 173
FT /note="E->D: Little change in enzyme specific activity nor
FT in PAPC/POPC activity ratio."
FT /evidence="ECO:0000269|PubMed:14636062"
FT MUTAGEN 173
FT /note="E->K: Decreased enzyme specific activity. Increased
FT PAPC/POPC activity ratio."
FT /evidence="ECO:0000269|PubMed:14636062"
FT MUTAGEN 173
FT /note="E->L: Increased activity towards PAPC. Increased
FT PAPC/POPC activity ratio."
FT /evidence="ECO:0000269|PubMed:14636062"
FT MUTAGEN 173
FT /note="E->Q: Decreased enzyme specific activity. Increased
FT PAPC/POPC activity ratio."
FT /evidence="ECO:0000269|PubMed:14636062"
FT CONFLICT 257
FT /note="I -> H (in Ref. 8; CAB56610/AAA59499)"
FT /evidence="ECO:0000305"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:5BV7"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:5BV7"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:4XWG"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:5BV7"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:5BV7"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 178..195
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 206..217
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:5BV7"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:5BV7"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:5TXF"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:5BV7"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:5TXF"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:5BV7"
FT TURN 322..327
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 335..350
FT /evidence="ECO:0007829|PDB:5BV7"
FT TURN 353..357
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 361..373
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:5BV7"
FT STRAND 391..397
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:5BV7"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:5BV7"
FT HELIX 408..419
FT /evidence="ECO:0007829|PDB:5BV7"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:5BV7"
SQ 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
