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P16301

- LCAT_MOUSE

UniProt

P16301 - LCAT_MOUSE

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Protein
Phosphatidylcholine-sterol acyltransferase
Gene
Lcat
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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). 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. Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins. Required for remodeling high-density lipoprotein particles into their spherical forms By similarity. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines.4 Publications

Catalytic activityi

Phosphatidylcholine + a sterol = 1-acylglycerophosphocholine + a sterol ester.

Enzyme regulationi

APOA1 is the most potent activator in plasma. Also activated by APOE, APOC1 and APOA4.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei173 – 1731Determinant for substrate specificity
Active sitei205 – 2051Charge relay system By similarity

GO - Molecular functioni

  1. phosphatidylcholine-sterol O-acyltransferase activity Source: MGI

GO - Biological processi

  1. cholesterol esterification Source: Ensembl
  2. cholesterol homeostasis Source: Ensembl
  3. cholesterol metabolic process Source: MGI
  4. cholesterol transport Source: MGI
  5. high-density lipoprotein particle remodeling Source: Ensembl
  6. lipoprotein biosynthetic process Source: MGI
  7. phosphatidylcholine biosynthetic process Source: Ensembl
  8. regulation of high-density lipoprotein particle assembly Source: UniProtKB
  9. reverse cholesterol transport Source: Ensembl
  10. very-low-density lipoprotein particle remodeling Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

ReactomeiREACT_213857. HDL-mediated lipid transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylcholine-sterol acyltransferase (EC:2.3.1.43)
Alternative name(s):
Lecithin-cholesterol acyltransferase
Phospholipid-cholesterol acyltransferase
Gene namesi
Name:Lcat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:96755. Lcat.

Subcellular locationi

Secreted
Note: Secreted into blood plasma. Produced in astrocytes and secreted into cerebral spinal fluid (CSF) By similarity.

GO - Cellular componenti

  1. extracellular space Source: MGI
  2. high-density lipoprotein particle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

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 O2 production and plasma phospholipid (PL)-bound-F2-isoprostane levels. This effect is paradoxically reversed in the APOE knockout background.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424
Add
BLAST
Chaini25 – 438414Phosphatidylcholine-sterol acyltransferase
PRO_0000017804Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi44 – 441N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi74 ↔ 98 By similarity
Glycosylationi108 – 1081N-linked (GlcNAc...) Reviewed prediction
Glycosylationi296 – 2961N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi337 ↔ 380 By similarity
Glycosylationi397 – 3971N-linked (GlcNAc...)1 Publication
Glycosylationi408 – 4081N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP16301.
PRIDEiP16301.

PTM databases

PhosphoSiteiP16301.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiP16301.
CleanExiMM_LCAT.
GenevestigatoriP16301.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000038232.

Structurei

3D structure databases

ProteinModelPortaliP16301.
SMRiP16301. Positions 196-239.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi425 – 43713Pro-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG322613.
GeneTreeiENSGT00390000004902.
HOVERGENiHBG017055.
InParanoidiQ8K139.
KOiK00650.
OMAiLRQPQSW.
OrthoDBiEOG73BVD0.
TreeFamiTF313258.

Family and domain databases

Gene3Di3.40.50.1820. 3 hits.
InterProiIPR029058. AB_hydrolase.
IPR003386. LACT/PDAT_acylTrfase.
[Graphical view]
PfamiPF02450. LCAT. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16301-1 [UniParc]FASTAAdd to Basket

« Hide

MGLPGSPWQR VLLLLGLLLP PATPFWLLNV LFPPHTTPKA ELSNHTRPVI    50
LVPGCLGNRL EAKLDKPDVV NWMCYRKTED FFTIWLDFNL FLPLGVDCWI 100
DNTRIVYNHS SGRVSNAPGV QIRVPGFGKT ESVEYVDDNK LAGYLHTLVQ 150
NLVNNGYVRD ETVRAAPYDW RLAPHQQDEY YKKLAGLVEE MYAAYGKPVF 200
LIGHSLGCLH VLHFLLRQPQ SWKDHFIDGF ISLGAPWGGS IKAMRILASG 250
DNQGIPILSN IKLKEEQRIT TTSPWMLPAP HVWPEDHVFI STPNFNYTVQ 300
DFERFFTDLH FEEGWHMFLQ SRDLLERLPA PGVEVYCLYG VGRPTPHTYI 350
YDHNFPYKDP VAALYEDGDD TVATRSTELC GQWQGRQSQP VHLLPMNETD 400
HLNMVFSNKT LEHINAILLG AYRTPKSPAA SPSPPPPE 438
Length:438
Mass (Da):49,747
Last modified:July 27, 2011 - v2
Checksum:i2FDD571853523136
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti411 – 4111L → M in AAA39419. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05154 mRNA. Translation: AAA39419.1.
AK149476 mRNA. Translation: BAE28903.1.
AC159265 Genomic DNA. No translation available.
BC028861 mRNA. Translation: AAH28861.1.
X54095 Genomic DNA. Translation: CAA38029.1.
CCDSiCCDS22622.1.
PIRiA34158. XXMSN.
RefSeqiNP_032516.2. NM_008490.2.
UniGeneiMm.1593.

Genome annotation databases

EnsembliENSMUST00000038896; ENSMUSP00000038232; ENSMUSG00000035237.
GeneIDi16816.
KEGGimmu:16816.
UCSCiuc009neq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05154 mRNA. Translation: AAA39419.1 .
AK149476 mRNA. Translation: BAE28903.1 .
AC159265 Genomic DNA. No translation available.
BC028861 mRNA. Translation: AAH28861.1 .
X54095 Genomic DNA. Translation: CAA38029.1 .
CCDSi CCDS22622.1.
PIRi A34158. XXMSN.
RefSeqi NP_032516.2. NM_008490.2.
UniGenei Mm.1593.

3D structure databases

ProteinModelPortali P16301.
SMRi P16301. Positions 196-239.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000038232.

PTM databases

PhosphoSitei P16301.

Proteomic databases

PaxDbi P16301.
PRIDEi P16301.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000038896 ; ENSMUSP00000038232 ; ENSMUSG00000035237 .
GeneIDi 16816.
KEGGi mmu:16816.
UCSCi uc009neq.2. mouse.

Organism-specific databases

CTDi 3931.
MGIi MGI:96755. Lcat.

Phylogenomic databases

eggNOGi NOG322613.
GeneTreei ENSGT00390000004902.
HOVERGENi HBG017055.
InParanoidi Q8K139.
KOi K00650.
OMAi LRQPQSW.
OrthoDBi EOG73BVD0.
TreeFami TF313258.

Enzyme and pathway databases

Reactomei REACT_213857. HDL-mediated lipid transport.

Miscellaneous databases

NextBioi 290700.
PROi P16301.
SOURCEi Search...

Gene expression databases

Bgeei P16301.
CleanExi MM_LCAT.
Genevestigatori P16301.

Family and domain databases

Gene3Di 3.40.50.1820. 3 hits.
InterProi IPR029058. AB_hydrolase.
IPR003386. LACT/PDAT_acylTrfase.
[Graphical view ]
Pfami PF02450. LCAT. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 2 hits.
PROSITEi PS00120. LIPASE_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Warden C.H., Langner C.A., Gordon J.I., Taylor B.A., McLean J.W., Lusis A.J.
    J. Biol. Chem. 264:21573-21581(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  5. "Promoter and 5' flanking sequences of the mouse LCAT gene."
    Meroni G., Malgaretti N., Magnaghi P., Taramelli R.
    Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
  6. "Comparative studies on the substrate specificity of lecithin:cholesterol acyltransferase towards the molecular species of phosphatidylcholine in the plasma of 14 vertebrates."
    Subbaiah P.V., Liu M.
    J. Lipid Res. 37:113-122(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY.
  7. "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."
    Ng D.S., Maguire G.F., Wylie J., Ravandi A., Xuan W., Ahmed Z., Eskandarian M., Kuksis A., Connelly P.W.
    J. Biol. Chem. 277:11715-11720(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  8. "In vivo contribution of LCAT to apolipoprotein B lipoprotein cholesteryl esters in LDL receptor and apolipoprotein E knockout mice."
    Furbee J.W. Jr., Francone O., Parks J.S.
    J. Lipid Res. 43:428-437(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  9. "Apolipoprotein E is the major physiological activator of lecithin-cholesterol acyltransferase (LCAT) on apolipoprotein B lipoproteins."
    Zhao Y., Thorngate F.E., Weisgraber K.H., Williams D.L., Parks J.S.
    Biochemistry 44:1013-1025(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  10. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-397 AND ASN-408.
    Strain: C57BL/6.
    Tissue: Plasma.
  11. "LCAT synthesized by primary astrocytes esterifies cholesterol on glia-derived lipoproteins."
    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.
    J. Lipid Res. 50:885-893(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, ENZYME REGULATION, FUNCTION.

Entry informationi

Entry nameiLCAT_MOUSE
AccessioniPrimary (citable) accession number: P16301
Secondary accession number(s): Q8K139
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi