LCAT_GERGM
ID LCAT_GERGM Reviewed; 293 AA.
AC O35840;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 78.
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 Gerbilliscus gambianus (Gambian gerbil) (Gerbilliscus kempi gambiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Gerbillinae; Gerbilliscus.
OX NCBI_TaxID=41264;
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; U72298; AAB58989.1; -; Genomic_DNA.
DR EMBL; U72297; AAB58989.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; O35840; -.
DR SMR; O35840; -.
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.
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..>293
FT /note="Phosphatidylcholine-sterol acyltransferase"
FT /id="PRO_0000090362"
FT ACT_SITE 123
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 ACT_SITE 284
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT SITE 91
FT /note="Determinant for substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT CARBOHYD 26
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 293
SQ SEQUENCE 293 AA; 33822 MW; 8CFB4BB7CAA738B7 CRC64;
TIWLDLNMFL SLGVDCWIDN TRVVYNRSSG RVSNAPGVEI RVPGFGKTYS VEYLDDNKLA
EYMHTLVQNL VNNGYVRDET VRAAPYDWRL EPSQQDDYYQ KLAGLIEEMY AAYGKPVFLI
GHSLGCLHVL YFLLRQGIPI MSSIKLREEQ RITTTSPWMF PDRDVWPEDH VFISTPEFNY
TGQDFERFFS DLHFEEGWYM WLQSRDLLAG LPAPGVDVYC LYGVGLPTPH TYIYDHNFPY
KDPVAALYED GDDTVATRST ELCGQWQGRQ SQPVHLLPMN GTEHLNMVFS NKT
