LCAT_PAPAN
ID LCAT_PAPAN Reviewed; 440 AA.
AC Q08758;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 104.
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: Precursor;
GN Name=LCAT;
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8514197; DOI=10.1016/0378-1119(93)90578-q;
RA Hixson J.E., Driscoll D.M., Birnbaum S., Britten M.L.;
RT "Baboon lecithin cholesterol acyltransferase (LCAT): cDNA sequences of two
RT alleles, evolution, and gene expression.";
RL Gene 128:295-299(1993).
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 -!- TISSUE SPECIFICITY: Most abundant in liver and cerebellum.
CC {ECO:0000269|PubMed:8514197}.
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; L08633; AAA35388.1; -; mRNA.
DR RefSeq; NP_001106083.1; NM_001112613.1.
DR AlphaFoldDB; Q08758; -.
DR SMR; Q08758; -.
DR STRING; 9555.ENSPANP00000012215; -.
DR ESTHER; papan-lcat; PC-sterol_acyltransferase.
DR Ensembl; ENSPANT00000017150; ENSPANP00000012215; ENSPANG00000022341.
DR GeneID; 100126664; -.
DR KEGG; panu:100126664; -.
DR CTD; 3931; -.
DR eggNOG; KOG2369; Eukaryota.
DR GeneTree; ENSGT00940000160052; -.
DR HOGENOM; CLU_037070_1_0_1; -.
DR OMA; WEDTKNL; -.
DR OrthoDB; 828056at2759; -.
DR Proteomes; UP000028761; Chromosome 18.
DR Bgee; ENSPANG00000022341; Expressed in aorta and 64 other tissues.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:Ensembl.
DR GO; GO:0034186; F:apolipoprotein A-I binding; IEA:Ensembl.
DR GO; GO:0004607; F:phosphatidylcholine-sterol O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047179; F:platelet-activating factor acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0034435; P:cholesterol esterification; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:Ensembl.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
DR GO; GO:0090107; P:regulation of high-density lipoprotein particle assembly; IEA:Ensembl.
DR GO; GO:0043691; P:reverse cholesterol transport; IEA:Ensembl.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IEA:Ensembl.
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.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cholesterol metabolism; Disulfide bond; Glycoprotein;
KW Lipid metabolism; Reference proteome; Secreted; Signal; Steroid metabolism;
KW Sterol metabolism; Transferase.
FT SIGNAL 1..24
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT CHAIN 25..440
FT /note="Phosphatidylcholine-sterol acyltransferase"
FT /id="PRO_0000017803"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 369
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT ACT_SITE 401
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT SITE 173
FT /note="Determinant for substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..98
FT /evidence="ECO:0000250|UniProtKB:P04180"
FT DISULFID 337..380
FT /evidence="ECO:0000250|UniProtKB:P04180"
SQ SEQUENCE 440 AA; 49645 MW; E06B0BC8300BA9D9 CRC64;
MGPPGSPWQW VPLLLGLLLP PAAPFWLLNV LFPPHTTPKA ELSNHTRPVI LVPGCLGNQL
EAKLDKPDVV NWMCYRKTED FFTIWLDLNM FLPLGVDCWI DNTRVVYNRS SGLVSNAPGV
QIRVPGFGKT YSVEYLDSSK LAGYLHTLVQ NLVNNGYVRD ETVRAAPYDW RLEPGQQEEY
YHKLAGLVEE MHAAYGKPVF LIGHSLGCLH LLYFLLRQPQ AWKDRFIDGF ISLGAPWGGS
IKPMLVLASG DNQGIPIMSS IKLKEEQRIT TTSPWMFPSR LAWPEDHVFI STPSFNYTGR
DFQRFFADLH FEEGWYMWLQ SRDLLAGLPA PGVEVYCLYG VGLPTPRTYI YDHGFPYTDP
VDVLYEDGDD TVATRSTELC GLWQGRQPQP VHLLPLRGIQ HLNMVFSNQT LEHINAILLG
AYRQGPPASL TASPEPPPPE
