LCAT_CHICK
ID LCAT_CHICK Reviewed; 413 AA.
AC P53760;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Phosphatidylcholine-sterol acyltransferase;
DE EC=2.3.1.43 {ECO:0000269|PubMed:7592817, ECO:0000269|PubMed:8820107};
DE AltName: Full=Lecithin-cholesterol acyltransferase;
DE AltName: Full=Phospholipid-cholesterol acyltransferase;
DE Flags: Precursor; Fragment;
GN Name=LCAT;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=White leghorn;
RX PubMed=7592817; DOI=10.1074/jbc.270.44.26139;
RA Hengstschlaeger-Ottnad E., Kuchler K., Schneider W.J.;
RT "Chicken lecithin-cholesterol acyltransferase. Molecular characterization
RT reveals unusual structure and expression pattern.";
RL J. Biol. Chem. 270:26139-26145(1995).
RN [2]
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). {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:0000269|PubMed:7592817, ECO:0000269|PubMed:8820107};
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:0000269|PubMed:7592817,
CC ECO:0000269|PubMed:8820107}. Note=Secreted into blood plasma
CC (PubMed:7592817, PubMed:8820107). {ECO:0000269|PubMed:7592817,
CC ECO:0000269|PubMed:8820107}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma (at protein level)
CC (PubMed:7592817, PubMed:8820107). Expressed in liver, brain and adrenal
CC glands. Lower expression in testes. In laying hens, expressed higher in
CC brain than in liver. In roosters, higher levels in liver than in brain
CC (PubMed:7592817). {ECO:0000269|PubMed:7592817,
CC ECO:0000269|PubMed:8820107}.
CC -!- DEVELOPMENTAL STAGE: Expressed in liver during embryogenesis. Levels
CC higher in liver than in brain up to 15 weeks after hatching. In the
CC brain, first detected at 11 weeks after hatching and increasing levels
CC from 15 weeks to maturity (25 weeks). Expression in the liver is much
CC lower throughout these later stages of hatching.
CC {ECO:0000269|PubMed:7592817}.
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 EMBL; X91011; CAA62493.1; -; mRNA.
DR PIR; I50662; I50662.
DR RefSeq; NP_001280023.1; NM_001293094.1.
DR AlphaFoldDB; P53760; -.
DR SMR; P53760; -.
DR STRING; 9031.ENSGALP00000043323; -.
DR ESTHER; chick-lcat; PC-sterol_acyltransferase.
DR PRIDE; P53760; -.
DR GeneID; 396136; -.
DR KEGG; gga:396136; -.
DR CTD; 3931; -.
DR VEuPathDB; HostDB:geneid_396136; -.
DR eggNOG; KOG2369; Eukaryota.
DR InParanoid; P53760; -.
DR OrthoDB; 828056at2759; -.
DR PhylomeDB; P53760; -.
DR BRENDA; 2.3.1.43; 1306.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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: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.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cholesterol metabolism; Disulfide bond; Glycoprotein;
KW Lipid metabolism; Reference proteome; Secreted; Signal; Steroid metabolism;
KW Sterol metabolism; Transferase.
FT SIGNAL <1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..413
FT /note="Phosphatidylcholine-sterol acyltransferase"
FT /id="PRO_0000017807"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 203
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 367
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 399
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..96
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT DISULFID 335..378
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT NON_TER 1
SQ SEQUENCE 413 AA; 47804 MW; 3DE6B6BF4897EABA CRC64;
GRTGAGFTLL TLLLLLPQPT SQFWLFNVLF PPTTTPEAPP TNSTPPWCLV PGFLGNQLEA
KLDKPDVVNW MCYRKTEDYF TIWLNLNTFL PVGVDCWIDN TRVVYNRTAR KMTNAPGVHI
RVPGFGKTYS VEYLDQSKLA GYLHTLVQNL VNNGYVRDQT VRAAPYDWRV GPQEQPEYFQ
NLKALIEEMH DEYQQRVFLI GHSMGNLNVL YFLLQQKQAW KDQYIGGFIS LGAPWGGSVK
PLRVLASGDN QGIPLMSNIK LREEQRMTTT SPWMFPTSLA WPEDHVFIST PSYNYTYRDY
QRFFTDVNLE DGWYMWEDMK DLLKGLPPPG VDTYCLYGTG YPTVETYIYD EHFPYEDPVD
MIYGDGDDTV NKRSSELCKR WRNQQKQKVH VQELRGIDHL NMVFSNLTLT LHQ
