ID   LCAT_ELIQU              Reviewed;         299 AA.
AC   O35573;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Phosphatidylcholine-sterol acyltransferase;
DE            EC=2.3.1.43 {ECO:0000250|UniProtKB:P04180};
DE   AltName: Full=Lecithin-cholesterol acyltransferase;
DE   AltName: Full=Phospholipid-cholesterol acyltransferase;
DE   Flags: Fragment;
GN   Name=LCAT;
OS   Eliomys quercinus (Garden dormouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Gliridae;
OC   Leithiinae; Eliomys.
OX   NCBI_TaxID=53277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9417899; DOI=10.1006/mpev.1997.0424;
RA   Robinson M., Catzeflis F., Briolay J., Mouchiroud D.;
RT   "Molecular phylogeny of rodents, with special emphasis on murids: evidence
RT   from nuclear gene LCAT.";
RL   Mol. Phylogenet. Evol. 8:423-434(1997).
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. Has a preference for plasma 16:0-
CC       18:2 or 18:O-18:2 phosphatidylcholines. 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). {ECO:0000250|UniProtKB:P04180}.
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:0000250|UniProtKB:P04180};
CC   -!- ACTIVITY REGULATION: APOA1 is the most potent activator in plasma. Also
CC       activated by APOE, APOC1 and APOA4 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04180}.
CC       Note=Secreted into blood plasma. Produced in astrocytes and secreted
CC       into cerebral spinal fluid (CSF) (By similarity).
CC       {ECO:0000250|UniProtKB:P04180}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AH005254; AAB58999.1; -; Genomic_DNA.
DR   AlphaFoldDB; O35573; -.
DR   SMR; O35573; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004607; F:phosphatidylcholine-sterol O-acyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0034435; P:cholesterol esterification; ISS:UniProtKB.
DR   GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR   Gene3D; 3.40.50.1820; -; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR   Pfam; PF02450; LCAT; 2.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cholesterol metabolism; Disulfide bond; Glycoprotein;
KW   Lipid metabolism; Secreted; Steroid metabolism; Sterol metabolism;
KW   Transferase.
FT   CHAIN           <1..>299
FT                   /note="Phosphatidylcholine-sterol acyltransferase"
FT                   /id="PRO_0000090359"
FT   ACT_SITE        127
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P04180"
FT   ACT_SITE        258
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P04180"
FT   ACT_SITE        290
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P04180"
FT   SITE            95
FT                   /note="Determinant for substrate specificity"
FT                   /evidence="ECO:0000250|UniProtKB:P04180"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        226..269
FT                   /evidence="ECO:0000250|UniProtKB:P04180"
FT   NON_TER         1
FT   NON_TER         299
SQ   SEQUENCE   299 AA;  34653 MW;  9C2041F7E79A2CEF CRC64;
     EDCFTIWLDL NIFLSLGVDC WIDNTRVIYN RSSGYMSNAP GVQIRVPGFG KTYSIEYLDD
     NKLAGYMHTL VQNLVNNAYV RDETVRAPPY DWRLEPRHQE EYYLKLAGLV EEMYATYGKP
     VFLIGHSLGF CHLLYFLLLQ PQGIPIMSSI KLVEEQRITT TSPWMFPSHQ VWPEDHVFIS
     TPNFNYTFSD FQRFFADLHF EDGWYMWLQS RDLLAGLPAP GVEVYCLYGV GLPTPHTYMY
     DHGFPYTDPV GIIYEDGDDT VTTHSIELCS HWQGRQPQPV HLLPLRGTQH LNMVFSNKT