| IED ID | IndEnz0010001294 |
| Enzyme Type ID | esterase001294 |
| Protein Name |
Phosphatidylcholine-sterol acyltransferase EC 2.3.1.43 Lecithin-cholesterol acyltransferase Phospholipid-cholesterol acyltransferase |
| Gene Name | LCAT |
| Organism | Papio anubis (Olive baboon) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Cercopithecoidea Cercopithecidae (Old World monkeys) Cercopithecinae Papio (baboons) Papio anubis (Olive baboon) |
| Enzyme Sequence | MGPPGSPWQWVPLLLGLLLPPAAPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQLEAKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEYYHKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGSIKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSRLAWPEDHVFISTPSFNYTGRDFQRFFADLHFEEGWYMWLQSRDLLAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYTDPVDVLYEDGDDTVATRSTELCGLWQGRQPQPVHLLPLRGIQHLNMVFSNQTLEHINAILLGAYRQGPPASLTASPEPPPPE |
| Enzyme Length | 440 |
| Uniprot Accession Number | Q08758 |
| 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 | ACTIVITY REGULATION: APOA1 is the most potent activator in plasma. Also activated by APOE, APOC1 and APOA4 (By similarity). {ECO:0000250}. |
| 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:0000250|UniProtKB:P04180, ECO:0000255|PROSITE-ProRule:PRU10037}; |
| DNA Binding | |
| EC Number | 2.3.1.43 |
| 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. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines. 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). {ECO:0000250|UniProtKB:P04180}. |
| 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;Lipid metabolism;Reference proteome;Secreted;Signal;Steroid metabolism;Sterol metabolism;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04180}. Note=Secreted into blood plasma. Produced in astrocytes and secreted into cerebral spinal fluid (CSF) (By similarity). {ECO:0000250|UniProtKB:P04180}. |
| 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 | 49,645 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21204 |
| Cross Reference Brenda |