Detail Information for IndEnz0005000263
IED ID IndEnz0005000263
Enzyme Type ID lipase000263
Protein Name Phosphatidylcholine-sterol acyltransferase
EC 2.3.1.43
1-alkyl-2-acetylglycerophosphocholine esterase
EC 3.1.1.47
Lecithin-cholesterol acyltransferase
Phospholipid-cholesterol acyltransferase
Platelet-activating factor acetylhydrolase
PAF acetylhydrolase
Gene Name LCAT
Organism Oryctolagus cuniculus (Rabbit)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit)
Enzyme Sequence MGPPGSPWQWVLLLLGLLLPPAAPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQLEAKLDKPSVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNRSSGRVVISPGVQIRVPGFGKTYSVEYLDNNKLAGYMHTLVQNLVNNGYVRDETVRAAPYDWRLEPSQQEEYYGKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQSWKDRFIDGFISLGAPWGGSIKPMLVLASGDNQGIPLMSSIKLREEQRITTTSPWMFPSQGVWPEDHVFISTPSFNYTGRDFKRFFEDLHFEEGWYMWLQSRDLLAGLPAPGVEVYCLYGIGLPTPHTYIYDHGFPYTDPVGVLYEDGDDTVATSSTDLCGLWRGRQPQPVHLLPLHETEHLNMVFSNQTLEHINAILLGAYRSGTPASPTASPGSPPPE
Enzyme Length 440
Uniprot Accession Number P53761
Absorption
Active Site ACT_SITE 205; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P04180; ACT_SITE 369; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P04180; ACT_SITE 401; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P04180
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a sterol = a 1-acyl-sn-glycero-3-phosphocholine + a sterol ester; Xref=Rhea:RHEA:21204, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=2.3.1.43; Evidence={ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:8820107}; CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=(24S)-hydroxycholesterol + 1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine = (24S)-24-hydroxycholesterol ester + 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:43216, ChEBI:CHEBI:34310, ChEBI:CHEBI:72998, ChEBI:CHEBI:77369, ChEBI:CHEBI:82869; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43217; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=(24S)-hydroxycholesterol + 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine = (24S)-hydroxycholesterol 3-linoleoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:43224, ChEBI:CHEBI:34310, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002, ChEBI:CHEBI:82875; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43225; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-phosphocholine + cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:53448, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003, ChEBI:CHEBI:82751; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53449; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-phosphocholine + cholesteryl (9Z-octadecenoate); Xref=Rhea:RHEA:53456, ChEBI:CHEBI:16113, ChEBI:CHEBI:46898, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53457; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(8Z,11Z,14Z-eicosatrienoyl)-sn-glycero-3-phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-phosphocholine + cholesteryl (8Z,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:53464, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998, ChEBI:CHEBI:84346, ChEBI:CHEBI:86121; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53465; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z-eicosatrienoyl)-sn-glycero-3-phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-phosphocholine + cholesteryl (5Z,8Z,11Z)-eicosatrienoate; Xref=Rhea:RHEA:53460, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998, ChEBI:CHEBI:86119, ChEBI:CHEBI:88752; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53461; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl)-sn-glycero-3-phosphocholine + cholesterol = (5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl)-cholesterol + 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:53468, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998, ChEBI:CHEBI:84969, ChEBI:CHEBI:86137; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53469; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-phosphocholine + cholesteryl (9Z,12Z)-octadecadienoate; Xref=Rhea:RHEA:53472, ChEBI:CHEBI:16113, ChEBI:CHEBI:41509, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53473; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(6Z,9Z,12Z-octadecatrienoyl)-sn-glycero-3-phosphocholine + cholesterol = (6Z,9Z,12Z-octadecatrienoyl)-cholesterol + 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:53476, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998, ChEBI:CHEBI:84786, ChEBI:CHEBI:88756; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53477; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(11Z,14Z,17Z-eicosatrienoyl)-sn-glycero-3-phosphocholine + cholesterol = (11Z,14Z,17Z-eicosatrienoyl)-cholesterol + 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:53516, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998, ChEBI:CHEBI:137411, ChEBI:CHEBI:137412; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53517; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphocholine + cholesterol = (9Z,12Z,15Z-octadecatrienoyl)-cholesterol + 1-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:53520, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998, ChEBI:CHEBI:84341, ChEBI:CHEBI:84789; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53521; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000250|UniProtKB:P04180}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + 1-O-alkyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:53636, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707, ChEBI:CHEBI:72998, ChEBI:CHEBI:75219; Evidence={ECO:0000250|UniProtKB:P04180};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53637; Evidence={ECO:0000250|UniProtKB:P04180};
DNA Binding
EC Number 2.3.1.43; 3.1.1.47
Enzyme Function 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). The cholesterol ester is then transported back to the liver. 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 (By similarity). Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines (PubMed:8820107). Catalyzes the hydrolysis of 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-activating factor or PAF) to 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (By similarity). Also catalyzes the transfer of the acetate group from PAF to 1-hexadecanoyl-sn-glycero-3-phosphocholine forming lyso-PAF (By similarity). Catalyzes the esterification of (24S)-hydroxycholesterol (24(S)OH-C), also known as cerebrosterol to produce 24(S)OH-C monoesters (By similarity). {ECO:0000250|UniProtKB:P04180, ECO:0000269|PubMed:8820107}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (2); Glycosylation (4); Signal peptide (1); Site (1)
Keywords Acyltransferase;Cholesterol metabolism;Disulfide bond;Glycoprotein;Hydrolase;Lipid metabolism;Reference proteome;Secreted;Signal;Steroid metabolism;Sterol metabolism;Transferase
Interact With
Induction INDUCTION: Levels increase up to 3-fold on a 6-week cholesterol-enriched diet. {ECO:0000269|PubMed:8827532}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8820107}. Note=Secreted into blood plasma (PubMed:8820107). Produced in astrocytes and secreted into cerebral spinal fluid (CSF) (By similarity). {ECO:0000250|UniProtKB:P04180, ECO:0000269|PubMed:8820107}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000250|UniProtKB:P04180
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 49,560
Kinetics
Metal Binding
Rhea ID RHEA:21204; RHEA:17777; RHEA:17778; RHEA:43216; RHEA:43217; RHEA:43224; RHEA:43225; RHEA:53448; RHEA:53449; RHEA:53456; RHEA:53457; RHEA:53464; RHEA:53465; RHEA:53460; RHEA:53461; RHEA:53468; RHEA:53469; RHEA:53472; RHEA:53473; RHEA:53476; RHEA:53477; RHEA:53516; RHEA:53517; RHEA:53520; RHEA:53521; RHEA:40811; RHEA:40812; RHEA:40427; RHEA:40428; RHEA:53636; RHEA:53637
Cross Reference Brenda