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Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase)

 LCAT_MOUSE              Reviewed;         438 AA.
P16301; Q8K139;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 139.
RecName: Full=Phosphatidylcholine-sterol acyltransferase;
EC=2.3.1.43 {ECO:0000269|PubMed:15654758, ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:8820107};
AltName: Full=Lecithin-cholesterol acyltransferase;
AltName: Full=Phospholipid-cholesterol acyltransferase;
Flags: Precursor;
Name=Lcat;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=2600083;
Warden C.H., Langner C.A., Gordon J.I., Taylor B.A., McLean J.W.,
Lusis A.J.;
"Tissue-specific expression, developmental regulation, and chromosomal
mapping of the lecithin: cholesterol acyltransferase gene. Evidence
for expression in brain and testes as well as liver.";
J. Biol. Chem. 264:21573-21581(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
Meroni G., Malgaretti N., Magnaghi P., Taramelli R.;
"Promoter and 5' flanking sequences of the mouse LCAT gene.";
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
[6]
CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=8820107;
Subbaiah P.V., Liu M.;
"Comparative studies on the substrate specificity of
lecithin:cholesterol acyltransferase towards the molecular species of
phosphatidylcholine in the plasma of 14 vertebrates.";
J. Lipid Res. 37:113-122(1996).
[7]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=11809774; DOI=10.1074/jbc.M112320200;
Ng D.S., Maguire G.F., Wylie J., Ravandi A., Xuan W., Ahmed Z.,
Eskandarian M., Kuksis A., Connelly P.W.;
"Oxidative stress is markedly elevated in lecithin:cholesterol
acyltransferase-deficient mice and is paradoxically reversed in the
apolipoprotein E knockout background in association with a reduction
in atherosclerosis.";
J. Biol. Chem. 277:11715-11720(2002).
[8]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=11893779;
Furbee J.W. Jr., Francone O., Parks J.S.;
"In vivo contribution of LCAT to apolipoprotein B lipoprotein
cholesteryl esters in LDL receptor and apolipoprotein E knockout
mice.";
J. Lipid Res. 43:428-437(2002).
[9]
FUNCTION, AND ACTIVITY REGULATION.
PubMed=15654758; DOI=10.1021/bi0481489;
Zhao Y., Thorngate F.E., Weisgraber K.H., Williams D.L., Parks J.S.;
"Apolipoprotein E is the major physiological activator of lecithin-
cholesterol acyltransferase (LCAT) on apolipoprotein B lipoproteins.";
Biochemistry 44:1013-1025(2005).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-397 AND ASN-408.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[11]
DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, ACTIVITY REGULATION,
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=19065001; DOI=10.1194/jlr.M800584-JLR200;
Hirsch-Reinshagen V., Donkin J., Stukas S., Chan J., Wilkinson A.,
Fan J., Parks J.S., Kuivenhoven J.A., Lutjohann D., Pritchard H.,
Wellington C.L.;
"LCAT synthesized by primary astrocytes esterifies cholesterol on
glia-derived lipoproteins.";
J. Lipid Res. 50:885-893(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Liver, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Central enzyme in the extracellular metabolism of plasma
lipoproteins. Synthesized mainly in the liver and secreted into
plasma where it converts cholesterol and phosphatidylcholines
(lecithins) to cholesteryl esters and lysophosphatidylcholines on
the surface of high and low density lipoproteins (HDLs and LDLs)
(PubMed:19065001). The cholesterol ester is then transported back
to the liver. Also produced in the brain by primary astrocytes,
and esterifies free cholesterol on nascent APOE-containing
lipoproteins secreted from glia and influences cerebral spinal
fluid (CSF) APOE- and APOA1 levels (PubMed:19065001). Together
with APOE and the cholesterol transporter ABCA1, plays a key role
in the maturation of glial-derived, nascent lipoproteins
(PubMed:19065001). Required for remodeling high-density
lipoprotein particles into their spherical forms
(PubMed:19065001). Has a preference for plasma 16:0-18:2 or 18:O-
18:2 phosphatidylcholines (PubMed:8820107).
{ECO:0000250|UniProtKB:P04180, ECO:0000269|PubMed:11809774,
ECO:0000269|PubMed:11893779, ECO:0000269|PubMed:15654758,
ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:8820107}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + a sterol = 1-
acylglycerophosphocholine + a sterol ester. {ECO:0000255|PROSITE-
ProRule:PRU10037, ECO:0000269|PubMed:15654758,
ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:8820107}.
-!- ACTIVITY REGULATION: APOA1 is the most potent activator in plasma.
Also activated by APOE, APOC1 and APOA4.
{ECO:0000269|PubMed:15654758, ECO:0000269|PubMed:19065001}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19065001,
ECO:0000269|PubMed:8820107}. Note=Secreted into blood plasma
(PubMed:8820107). Produced in astrocytes and secreted into
cerebral spinal fluid (CSF) (By similarity). {ECO:0000250,
ECO:0000269|PubMed:8820107}.
-!- TISSUE SPECIFICITY: Detected in blood plasma (PubMed:8820107).
Produced and secreted by astrocytes (at protein level)
(PubMed:19065001). Abundantly expressed in liver, brain and testis
with highest levels in liver. In the brain, found in cerebellum,
cerebral cortex, hippocampus and brain stem. Located to neurons
and neuroglia. {ECO:0000269|PubMed:19065001,
ECO:0000269|PubMed:2600083}.
-!- DEVELOPMENTAL STAGE: In the testis, expressed days 4,8, 14, and 35
of postnatal life with highest levels at day 35. In the brain,
expressed in fetal stages and levels begin to rise after day 4
after birth and continue to increase through suckling and weaning
reaching a peak at postnatal day 24. In the liver, expressed in
fetal life from day 16-21 of gestation with a 3-fold increase in
the four final days of gestation. {ECO:0000269|PubMed:2600083}.
-!- DISRUPTION PHENOTYPE: Null mice exhibit a 7-fold increase in the
cholesteryl ester fatty acid CEFA ratio of APOB lipoprotein CEs.
There is also a 3.6 increase in vascular ring O(2) production and
plasma phospholipid (PL)-bound-F2-isoprostane levels. This effect
is paradoxically reversed in the APOE knockout background.
{ECO:0000269|PubMed:11809774, ECO:0000269|PubMed:11893779,
ECO:0000269|PubMed:19065001}.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; J05154; AAA39419.1; -; mRNA.
EMBL; AK149476; BAE28903.1; -; mRNA.
EMBL; AC159265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC028861; AAH28861.1; -; mRNA.
EMBL; X54095; CAA38029.1; -; Genomic_DNA.
CCDS; CCDS22622.1; -.
PIR; A34158; XXMSN.
RefSeq; NP_032516.2; NM_008490.2.
UniGene; Mm.1593; -.
ProteinModelPortal; P16301; -.
SMR; P16301; -.
STRING; 10090.ENSMUSP00000038232; -.
SwissLipids; SLP:000001729; -.
ESTHER; mouse-lcat; PC-sterol_acyltransferase.
iPTMnet; P16301; -.
PhosphoSitePlus; P16301; -.
MaxQB; P16301; -.
PaxDb; P16301; -.
PeptideAtlas; P16301; -.
PRIDE; P16301; -.
Ensembl; ENSMUST00000038896; ENSMUSP00000038232; ENSMUSG00000035237.
GeneID; 16816; -.
KEGG; mmu:16816; -.
UCSC; uc009neq.2; mouse.
CTD; 3931; -.
MGI; MGI:96755; Lcat.
eggNOG; KOG2369; Eukaryota.
eggNOG; ENOG410Y9CF; LUCA.
GeneTree; ENSGT00390000004902; -.
HOVERGEN; HBG017055; -.
InParanoid; P16301; -.
KO; K00650; -.
OMA; TYGKPVF; -.
OrthoDB; EOG091G07S3; -.
TreeFam; TF313258; -.
Reactome; R-MMU-8964058; HDL remodeling.
PRO; PR:P16301; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000035237; Expressed in 162 organ(s), highest expression level in liver.
CleanEx; MM_LCAT; -.
Genevisible; P16301; MM.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0034364; C:high-density lipoprotein particle; ISO:MGI.
GO; GO:0034186; F:apolipoprotein A-I binding; ISO:MGI.
GO; GO:0004607; F:phosphatidylcholine-sterol O-acyltransferase activity; IDA:MGI.
GO; GO:0004623; F:phospholipase A2 activity; ISO:MGI.
GO; GO:0034435; P:cholesterol esterification; ISS:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI.
GO; GO:0030301; P:cholesterol transport; ISO:MGI.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:MGI.
GO; GO:0042158; P:lipoprotein biosynthetic process; IDA:MGI.
GO; GO:0042157; P:lipoprotein metabolic process; ISO:MGI.
GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:MGI.
GO; GO:0046470; P:phosphatidylcholine metabolic process; ISS:UniProtKB.
GO; GO:0006644; P:phospholipid metabolic process; ISO:MGI.
GO; GO:0090107; P:regulation of high-density lipoprotein particle assembly; IDA:UniProtKB.
GO; GO:0046688; P:response to copper ion; ISO:MGI.
GO; GO:0051384; P:response to glucocorticoid; ISO:MGI.
GO; GO:0043691; P:reverse cholesterol transport; ISO:MGI.
GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; ISO:MGI.
Gene3D; 3.40.50.1820; -; 3.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR003386; LACT/PDAT_acylTrfase.
Pfam; PF02450; LCAT; 1.
SUPFAM; SSF53474; SSF53474; 2.
PROSITE; PS00120; LIPASE_SER; 1.
1: Evidence at protein level;
Acyltransferase; Cholesterol metabolism; Complete proteome;
Disulfide bond; Glycoprotein; Lipid metabolism; Reference proteome;
Secreted; Signal; Steroid metabolism; Sterol metabolism; Transferase.
SIGNAL 1 24 {ECO:0000250|UniProtKB:P04180}.
CHAIN 25 438 Phosphatidylcholine-sterol
acyltransferase.
/FTId=PRO_0000017804.
COMPBIAS 425 437 Pro-rich.
ACT_SITE 205 205 Nucleophile.
{ECO:0000250|UniProtKB:P04180}.
ACT_SITE 369 369 Charge relay system.
{ECO:0000250|UniProtKB:P04180}.
ACT_SITE 401 401 Charge relay system.
{ECO:0000250|UniProtKB:P04180}.
SITE 173 173 Determinant for substrate specificity.
{ECO:0000250|UniProtKB:P04180}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 108 108 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
DISULFID 74 98 {ECO:0000250|UniProtKB:P04180}.
DISULFID 337 380 {ECO:0000250|UniProtKB:P04180}.
CONFLICT 411 411 L -> M (in Ref. 1; AAA39419).
{ECO:0000305}.
SEQUENCE 438 AA; 49747 MW; 2FDD571853523136 CRC64;
MGLPGSPWQR VLLLLGLLLP PATPFWLLNV LFPPHTTPKA ELSNHTRPVI LVPGCLGNRL
EAKLDKPDVV NWMCYRKTED FFTIWLDFNL FLPLGVDCWI DNTRIVYNHS SGRVSNAPGV
QIRVPGFGKT ESVEYVDDNK LAGYLHTLVQ NLVNNGYVRD ETVRAAPYDW RLAPHQQDEY
YKKLAGLVEE MYAAYGKPVF LIGHSLGCLH VLHFLLRQPQ SWKDHFIDGF ISLGAPWGGS
IKAMRILASG DNQGIPILSN IKLKEEQRIT TTSPWMLPAP HVWPEDHVFI STPNFNYTVQ
DFERFFTDLH FEEGWHMFLQ SRDLLERLPA PGVEVYCLYG VGRPTPHTYI YDHNFPYKDP
VAALYEDGDD TVATRSTELC GQWQGRQSQP VHLLPMNETD HLNMVFSNKT LEHINAILLG
AYRTPKSPAA SPSPPPPE


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