LCAT_PIG
ID LCAT_PIG Reviewed; 188 AA.
AC P30930;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Phosphatidylcholine-sterol acyltransferase;
DE EC=2.3.1.43 {ECO:0000269|PubMed:8820107};
DE AltName: Full=1-alkyl-2-acetylglycerophosphocholine esterase;
DE EC=3.1.1.47 {ECO:0000250|UniProtKB:P04180};
DE AltName: Full=Lecithin-cholesterol acyltransferase;
DE AltName: Full=Phospholipid-cholesterol acyltransferase;
DE AltName: Full=Platelet-activating factor acetylhydrolase {ECO:0000250|UniProtKB:P04180};
DE Short=PAF acetylhydrolase;
DE Flags: Fragments;
GN Name=LCAT;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Plasma;
RX PubMed=2591200; DOI=10.1016/0305-0491(89)90361-1;
RA Yueksel K.U., Park Y.B., Jung J., Gracy R.W., Lacko A.G.;
RT "Studies on the structure of lecithin:cholesterol acyltransferase (LCAT)
RT -- comparisons of the active site region and secondary structure of the
RT human and the porcine enzymes.";
RL Comp. Biochem. Physiol. 94B:389-394(1989).
RN [2]
RP PROTEIN SEQUENCE OF 97-106 AND 142-154.
RC TISSUE=Plasma;
RX PubMed=3827927; DOI=10.1016/0006-291x(87)90673-5;
RA Park Y.B., Yuksel K.U., Gracy R.W., Lacko A.G.;
RT "The catalytic center of lecithin:cholesterol acyltransferase: isolation
RT and sequence of diisopropyl fluorophosphate-labeled peptides.";
RL Biochem. Biophys. Res. Commun. 143:360-363(1987).
RN [3]
RP CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=8820107;
RA Subbaiah P.V., Liu M.;
RT "Comparative studies on the substrate specificity of lecithin:cholesterol
RT acyltransferase towards the molecular species of phosphatidylcholine in the
RT plasma of 14 vertebrates.";
RL J. Lipid Res. 37:113-122(1996).
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. 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). Has a preference for plasma 16:0-18:2 or 18:O-18:2
CC phosphatidylcholines (PubMed:8820107). Catalyzes the hydrolysis of 1-O-
CC alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-activating factor
CC or PAF) to 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (By
CC similarity). Also catalyzes the transfer of the acetate group from PAF
CC to 1-hexadecanoyl-sn-glycero-3-phosphocholine forming lyso-PAF (By
CC similarity). Catalyzes the esterification of (24S)-hydroxycholesterol
CC (24(S)OH-C), also known as cerebrosterol to produce 24(S)OH-C
CC monoesters (By similarity). {ECO:0000250|UniProtKB:P04180,
CC ECO:0000269|PubMed:8820107}.
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:0000255|PROSITE-ProRule:PRU10037,
CC ECO:0000269|PubMed:8820107};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + 1-hexadecanoyl-2-acyl-sn-glycero-3-
CC phosphocholine = (24S)-24-hydroxycholesterol ester + 1-hexadecanoyl-
CC sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:43216, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:77369, ChEBI:CHEBI:82869;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43217;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphocholine = (24S)-
CC hydroxycholesterol 3-linoleoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine; Xref=Rhea:RHEA:43224, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002, ChEBI:CHEBI:82875;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43225;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate;
CC Xref=Rhea:RHEA:53448, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73003, ChEBI:CHEBI:82751;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53449;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + cholesterol = 1-hexadecanoyl-sn-glycero-3-phosphocholine +
CC cholesteryl (9Z-octadecenoate); Xref=Rhea:RHEA:53456,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:46898, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53457;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(8Z,11Z,14Z-eicosatrienoyl)-sn-glycero-3-
CC phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + cholesteryl (8Z,11Z,14Z)-eicosatrienoate;
CC Xref=Rhea:RHEA:53464, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:84346, ChEBI:CHEBI:86121;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53465;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z-eicosatrienoyl)-sn-glycero-3-
CC phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + cholesteryl (5Z,8Z,11Z)-eicosatrienoate;
CC Xref=Rhea:RHEA:53460, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:86119, ChEBI:CHEBI:88752;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53461;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl)-sn-
CC glycero-3-phosphocholine + cholesterol = (5Z,8Z,11Z,14Z,17Z-
CC eicosapentaenoyl)-cholesterol + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine; Xref=Rhea:RHEA:53468, ChEBI:CHEBI:16113,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:84969, ChEBI:CHEBI:86137;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53469;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + cholesterol = 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + cholesteryl (9Z,12Z)-octadecadienoate;
CC Xref=Rhea:RHEA:53472, ChEBI:CHEBI:16113, ChEBI:CHEBI:41509,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53473;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(6Z,9Z,12Z-octadecatrienoyl)-sn-glycero-3-
CC phosphocholine + cholesterol = (6Z,9Z,12Z-octadecatrienoyl)-
CC cholesterol + 1-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:53476, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:84786, ChEBI:CHEBI:88756;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53477;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(11Z,14Z,17Z-eicosatrienoyl)-sn-glycero-3-
CC phosphocholine + cholesterol = (11Z,14Z,17Z-eicosatrienoyl)-
CC cholesterol + 1-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:53516, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:137411, ChEBI:CHEBI:137412;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53517;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-
CC phosphocholine + cholesterol = (9Z,12Z,15Z-octadecatrienoyl)-
CC cholesterol + 1-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:53520, ChEBI:CHEBI:16113, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:84341, ChEBI:CHEBI:84789;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53521;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + a 1-O-alkyl-2-
CC acetyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-acetyl-sn-
CC glycero-3-phosphocholine + 1-O-alkyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:53636, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75219;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53637;
CC Evidence={ECO:0000250|UniProtKB:P04180};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8820107}.
CC Note=Secreted into blood plasma (PubMed:8820107). Produced in
CC astrocytes and secreted into cerebral spinal fluid (CSF) (By
CC similarity). {ECO:0000250|UniProtKB:P04180,
CC ECO:0000269|PubMed:8820107}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level)
CC (PubMed:8820107). {ECO:0000269|PubMed:8820107}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; PL0153; PL0153.
DR PeptideAtlas; P30930; -.
DR InParanoid; P30930; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISS:UniProtKB.
DR GO; GO:0004607; F:phosphatidylcholine-sterol O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047179; F:platelet-activating factor acetyltransferase 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:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 3.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR Pfam; PF02450; LCAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cholesterol metabolism; Direct protein sequencing;
KW Glycoprotein; Hydrolase; Lipid metabolism; Reference proteome; Secreted;
KW Steroid metabolism; Sterol metabolism; Transferase.
FT CHAIN 1..>188
FT /note="Phosphatidylcholine-sterol acyltransferase"
FT /id="PRO_0000090361"
FT ACT_SITE 169
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT NON_CONS 34..35
FT /evidence="ECO:0000305"
FT NON_CONS 44..45
FT /evidence="ECO:0000305"
FT NON_CONS 60..61
FT /evidence="ECO:0000305"
FT NON_CONS 66..67
FT /evidence="ECO:0000305"
FT NON_CONS 77..78
FT /evidence="ECO:0000305"
FT NON_CONS 84..85
FT /evidence="ECO:0000305"
FT NON_CONS 96..97
FT /evidence="ECO:0000305"
FT NON_CONS 106..107
FT /evidence="ECO:0000305"
FT NON_CONS 115..116
FT /evidence="ECO:0000305"
FT NON_CONS 154..155
FT /evidence="ECO:0000305"
FT NON_TER 188
SQ SEQUENCE 188 AA; 21238 MW; A2A25EDB015EAB48 CRC64;
FWLLNVLFPP HTTPKAELSN HTRPVILVPG CLGNPDVVNW MCYRFTIWLD LNMFLPLGVD
VPGFGKTYSV EYLDNSKAAP YDWRLEPSQQ EEYYLKISLG APWGGSDLHF EEGWYDLLAG
LPAPGVEVYC LYGVGLPTPR XYIFDXGFPY XDPVQQQPVH LLPLPGTQHL NMVFSXQTLE
XINAILLG
