ID   LCAT_MICMN              Reviewed;         299 AA.
AC   O35724;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 72.
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   Micromys minutus (European harvest mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Micromys.
OX   NCBI_TaxID=13151;
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; AH005245; AAB58988.1; -; Genomic_DNA.
DR   AlphaFoldDB; O35724; -.
DR   SMR; O35724; -.
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_0000090360"
FT   ACT_SITE        257
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P04180"
FT   ACT_SITE        289
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P04180"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        225..268
FT                   /evidence="ECO:0000250|UniProtKB:P04180"
FT   NON_TER         1
FT   NON_TER         299
SQ   SEQUENCE   299 AA;  34834 MW;  55896C9A38C2482C CRC64;
     FFTIWLDINM FLPLGVDCWI DNTRVVYNRS SGRMSNAPGV QIRVPGFGKT YSVEYLDDNK
     LAGYLHTLVQ NLVNNAYVRD ETVRAAPYDW RLAPSQQDEY YQKLAELVEE MYDAYGKPVF
     LIGHRLGCLH VLHFLLHQSW KGIPIMSNIK LKEEQRITTT SPWMFPAHHV WPEDHVFIST
     PNFNYTGQDF KRFFADLHFE EGWYMFLQSR DLLEGLPAPG VEVYCLYGVG RPTRYTYIYD
     HNFPYKDPVA ILYEDGDETV ATRSTELCGQ WQGRQSQPVY LLPMNGTDHL NMVFSNKTL