LCAT_RAT
ID LCAT_RAT Reviewed; 440 AA.
AC P18424; O35849;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Phosphatidylcholine-sterol acyltransferase;
DE EC=2.3.1.43 {ECO:0000269|PubMed:14636062, ECO:0000269|PubMed:8820107, ECO:0000269|PubMed:9219904};
DE AltName: Full=1-alkyl-2-acetylglycerophosphocholine esterase;
DE EC=3.1.1.47 {ECO:0000250|UniProtKB:P04180};
DE AltName: Full=Lecithin-cholesterol acyltransferase {ECO:0000303|PubMed:14636062};
DE AltName: Full=Phospholipid-cholesterol acyltransferase;
DE AltName: Full=Platelet-activating factor acetylhydrolase {ECO:0000250|UniProtKB:P04180};
DE Short=PAF acetylhydrolase;
DE Flags: Precursor;
GN Name=Lcat;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2402469; DOI=10.1093/nar/18.17.5308;
RA Meroni G., Malgaretti N., Magnaghi P., Taramelli R.;
RT "Nucleotide sequence of the cDNA for lecithin-cholesterol acyl transferase
RT (LCAT) from the rat.";
RL Nucleic Acids Res. 18:5308-5308(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley, and Wistar; TISSUE=Liver;
RX PubMed=9219904; DOI=10.1016/s0005-2760(97)00055-6;
RA Wang J., Gebre A.K., Anderson R.A., Parks J.S.;
RT "Cloning and in vitro expression of rat lecithin:cholesterol
RT acyltransferase.";
RL Biochim. Biophys. Acta 1346:207-211(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [6]
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 [7]
RP CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF ALA-173.
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).
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). The cholesterol ester is
CC then transported back to the liver. Also produced in the brain by
CC primary astrocytes, and esterifies free cholesterol on nascent APOE-
CC 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 (By
CC similarity). Has a preference for plasma 16:0-18:2 or 18:O-18:2
CC phosphatidylcholines (PubMed:8820107, PubMed:14636062). Catalyzes the
CC hydrolysis of 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-
CC activating factor or PAF) to 1-O-alkyl-sn-glycero-3-phosphocholine
CC (lyso-PAF) (By similarity). Also catalyzes the transfer of the acetate
CC group from PAF to 1-hexadecanoyl-sn-glycero-3-phosphocholine forming
CC lyso-PAF (By similarity). Catalyzes the esterification of (24S)-
CC hydroxycholesterol (24(S)OH-C), also known as cerebrosterol to produce
CC 24(S)OH-C monoesters (By similarity). {ECO:0000250|UniProtKB:P04180,
CC ECO:0000269|PubMed:14636062, 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:14636062, ECO:0000269|PubMed:8820107,
CC ECO:0000269|PubMed:9219904};
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:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000250|UniProtKB:P04180};
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-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=(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:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43217;
CC Evidence={ECO:0000250|UniProtKB:P04180};
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:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43225;
CC Evidence={ECO:0000250|UniProtKB:P04180};
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:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53465;
CC Evidence={ECO:0000250|UniProtKB:P04180};
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:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53461;
CC Evidence={ECO:0000250|UniProtKB:P04180};
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:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53469;
CC Evidence={ECO:0000250|UniProtKB:P04180};
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:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53473;
CC Evidence={ECO:0000250|UniProtKB:P04180};
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:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53477;
CC Evidence={ECO:0000250|UniProtKB:P04180};
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:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53517;
CC Evidence={ECO:0000250|UniProtKB:P04180};
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:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53521;
CC Evidence={ECO:0000250|UniProtKB:P04180};
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:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53637;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14636062,
CC ECO:0000269|PubMed:8820107, ECO:0000269|PubMed:9219904}. Note=Secreted
CC into blood plasma (PubMed:8820107). Produced in astrocytes and secreted
CC into cerebral spinal fluid (CSF) (By similarity).
CC {ECO:0000250|UniProtKB:P04180, ECO:0000269|PubMed:8820107}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level)
CC (PubMed:8820107). {ECO:0000269|PubMed:8820107}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; X54096; CAA38030.1; -; mRNA.
DR EMBL; U62803; AAB65771.1; -; mRNA.
DR EMBL; AC121465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473972; EDL92424.1; -; Genomic_DNA.
DR EMBL; BC091155; AAH91155.1; -; mRNA.
DR PIR; S11214; XXRTN.
DR RefSeq; NP_058720.2; NM_017024.2.
DR AlphaFoldDB; P18424; -.
DR SMR; P18424; -.
DR IntAct; P18424; 1.
DR STRING; 10116.ENSRNOP00000026583; -.
DR SwissLipids; SLP:000001728; -.
DR ESTHER; ratno-lcat; PC-sterol_acyltransferase.
DR GlyGen; P18424; 5 sites.
DR PaxDb; P18424; -.
DR GeneID; 24530; -.
DR KEGG; rno:24530; -.
DR UCSC; RGD:2993; rat.
DR CTD; 3931; -.
DR RGD; 2993; Lcat.
DR VEuPathDB; HostDB:ENSRNOG00000019573; -.
DR eggNOG; KOG2369; Eukaryota.
DR HOGENOM; CLU_037070_1_0_1; -.
DR InParanoid; P18424; -.
DR OMA; WEDTKNL; -.
DR OrthoDB; 828056at2759; -.
DR PhylomeDB; P18424; -.
DR TreeFam; TF313258; -.
DR BRENDA; 2.3.1.43; 5301.
DR Reactome; R-RNO-8964058; HDL remodeling.
DR PRO; PR:P18424; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Proteomes; UP000234681; Chromosome 19.
DR Bgee; ENSRNOG00000019573; Expressed in liver and 20 other tissues.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:RGD.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISO:RGD.
DR GO; GO:0034186; F:apolipoprotein A-I binding; ISO:RGD.
DR GO; GO:0004607; F:phosphatidylcholine-sterol O-acyltransferase activity; IDA:RGD.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:RGD.
DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; ISO:RGD.
DR GO; GO:0034435; P:cholesterol esterification; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; IDA:RGD.
DR GO; GO:0030301; P:cholesterol transport; ISO:RGD.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; ISO:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; IDA:RGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:RGD.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:RGD.
DR GO; GO:0090107; P:regulation of high-density lipoprotein particle assembly; ISO:RGD.
DR GO; GO:0046688; P:response to copper ion; IDA:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IDA:RGD.
DR GO; GO:0043691; P:reverse cholesterol transport; ISO:RGD.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; ISO:RGD.
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 Acyltransferase; Cholesterol metabolism; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid metabolism; Reference proteome; Secreted; Signal;
KW Steroid metabolism; Sterol metabolism; Transferase.
FT SIGNAL 1..24
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT CHAIN 25..440
FT /note="Phosphatidylcholine-sterol acyltransferase"
FT /id="PRO_0000017806"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 369
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 401
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT SITE 173
FT /note="Determinant for substrate specificity"
FT /evidence="ECO:0000305|PubMed:14636062"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..98
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT DISULFID 337..380
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT MUTAGEN 173
FT /note="A->E: Reduced activity with 20-carbon
FT phosphatidylcholine as substrate. Little change with 18-
FT carbon phosphatidylcholine as substrate."
FT /evidence="ECO:0000269|PubMed:14636062"
FT CONFLICT 146
FT /note="H -> N (in Ref. 1; CAA38030)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="W -> V (in Ref. 1; CAA38030)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="A -> G (in Ref. 1; CAA38030)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="P -> R (in Ref. 1; CAA38030)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="R -> P (in Ref. 1; CAA38030)"
FT /evidence="ECO:0000305"
FT CONFLICT 438..439
FT /note="TK -> PT (in Ref. 1; CAA38030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 49882 MW; 836BB2D589F72B63 CRC64;
MGLPGSPWQW VLLLLGLLLP PATSFWLLNV LFPPHTTPKA ELSNHTRPVI LVPGCMGNRL
EAKLDKPNVV NWLCYRKTED FFTIWLDFNM FLPLGVDCWI DNTRVVYNRS SGHMSNAPGV
QIRVPGFGKT YSVEYLDDNK LAGYLHTLVQ NLVNNGYVRD ETVRAAPYDW RLAPRQQDEY
YQKLAGLVEE MYAAYGKPVF LIGHSLGCLH VLHFLLRQPQ SWKDHFIDGF ISLGAPWGGS
IKPMRILASG DNQGIPIMSN IKLREEQRIT TTSPWMFPAH HVWPEDHVFI STPNFNYTGQ
DFERFFADLH FEEGWHMFLQ SRDLLAGLPA PGVEVYCLYG VGMPTAHTYI YDHNFPYKDP
VAALYEDGDD TVATRSTELC GQWQGRQSQA VHLLPMNGTD HLNMVFSNKT LEHINAILLG
AYRHGTPKSP TASLGPPTKE
