ID   LCAT_MYOGA              Reviewed;         291 AA.
AC   O35502;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 73.
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   Myodes glareolus (Bank vole) (Clethrionomys glareolus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Arvicolinae; Myodes.
OX   NCBI_TaxID=447135;
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, ECO:0000255|PROSITE-
CC         ProRule:PRU10037};
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; AH005247; AAB58990.1; -; Genomic_DNA.
DR   AlphaFoldDB; O35502; -.
DR   SMR; O35502; -.
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; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR   Pfam; PF02450; LCAT; 2.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 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..>291
FT                   /note="Phosphatidylcholine-sterol acyltransferase"
FT                   /id="PRO_0000090358"
FT   ACT_SITE        125
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P04180"
FT   ACT_SITE        252
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P04180"
FT   SITE            93
FT                   /note="Determinant for substrate specificity"
FT                   /evidence="ECO:0000250|UniProtKB:P04180"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        220..263
FT                   /evidence="ECO:0000250|UniProtKB:P04180"
FT   NON_TER         1
FT   NON_TER         291
SQ   SEQUENCE   291 AA;  33536 MW;  B1F7E9D89201219D CRC64;
     FFTIFLDLNM FLALGVNCWI DNTRVVYNRS SGRMSNAPCV QIRVPGFGKT YSVEYLDDNK
     LAGYMHTLVQ NLVNNGYVRD ETVLAAPYDW RLEPSQQEEY YQKLAGLVEE MHAAYGKPVF
     LIGHSVGCLH VLYFNQGIPI MSSIKLREEQ RITTTSPWMF PARRVWPEDH VFISTPNFNY
     TGQDFKRFFE DLYFEEGWYM WLQSRDLLAG LPAPGVEVYC LYGVGLPTPS TYIYDHSFPY
     KDPVAALYED GDDTVATRST ELCGQVQGSQ SQPVHWLPMN WTEQLNMLFS N