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P04180

- LCAT_HUMAN

UniProt

P04180 - LCAT_HUMAN

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Protein
Phosphatidylcholine-sterol acyltransferase
Gene
LCAT
Organism
Homo sapiens (Human)
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. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines. 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.1 Publication

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 APOA4.1 Publication

Kineticsi

Affinity for LDL is 2.3 to 4-fold lower than for HDL. Relative reactivities are 16% for HDL3, 1.3% for HDL2 and 6.5% for LDL.

  1. KM=0.97 mM for LDL1 Publication
  2. KM=0.4 mM for HDL2
  3. KM=0.10 mM for HDL3

Vmax=8.3 mmol/min/mg enzyme with LDL as substrate

Vmax=0.58 mmol/min/mg enzyme with HDL2 as substrate

Vmax=2.0 mmol/min/mg enzyme with HDL3 as substrate

Sites

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

GO - Molecular functioni

  1. apolipoprotein A-I binding Source: BHF-UCL
  2. phosphatidylcholine-sterol O-acyltransferase activity Source: UniProtKB
  3. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

BRENDAi2.3.1.43. 2681.
ReactomeiREACT_13621. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:6522. LCAT.

Subcellular locationi

Secreted
Note: Secreted into blood plasma. Produced in astrocytes and secreted into cerebral spinal fluid (CSF).1 Publication

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProt
  4. high-density lipoprotein particle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Lecithin-cholesterol acyltransferase deficiency (LCATD) [MIM:245900]: A disorder of lipoprotein metabolism characterized by inadequate esterification of plasmatic cholesterol. Two clinical forms are recognized: complete LCAT deficiency and fish-eye disease. LCATD is generally referred to the complete form which is associated with absence of both alpha and beta LCAT activities resulting in esterification anomalies involving both HDL (alpha-LCAT activity) and LDL (beta-LCAT activity). It causes a typical triad of diffuse corneal opacities, target cell hemolytic anemia, and proteinuria with renal failure.
Note: The disease is caused by mutations affecting the gene represented in this entry.15 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171L → LLLPPAAPFWL in LCATD.
VAR_004251
Natural varianti29 – 291N → I in LCATD. 1 Publication
VAR_039020
Natural varianti37 – 371T → M in LCATD. 1 Publication
VAR_039022
Natural varianti54 – 541G → S in LCATD. 1 Publication
VAR_004253
Natural varianti57 – 571G → R in LCATD. 1 Publication
VAR_004254
Natural varianti95 – 951G → R in a compound heterozygote carrying H-164; intermediate phenotype between LCATD and FED; reduction of activity. 1 Publication
VAR_039024
Natural varianti117 – 1171A → T in LCATD. 2 Publications
Corresponds to variant rs28940886 [ dbSNP | Ensembl ].
VAR_004255
Natural varianti159 – 1591R → W in LCATD. 1 Publication
Corresponds to variant rs28940887 [ dbSNP | Ensembl ].
VAR_004257
Natural varianti164 – 1641R → C in LCATD. 1 Publication
VAR_039028
Natural varianti164 – 1641R → H in LCATD; also in a compound heterozygote carrying R-95 with intermediate phenotype between LCATD and FED; loss of activity. 2 Publications
VAR_004258
Natural varianti171 – 1711R → W in LCATD. 2 Publications
VAR_004259
Natural varianti180 – 1801Y → N in LCATD.
VAR_004260
Natural varianti205 – 2051S → N in LCATD. 1 Publication
VAR_039030
Natural varianti233 – 2331L → P in LCATD. 1 Publication
Corresponds to variant rs28942087 [ dbSNP | Ensembl ].
VAR_004262
Natural varianti242 – 2421K → N in LCATD. 1 Publication
VAR_039031
Natural varianti252 – 2521N → K in LCATD. 1 Publication
VAR_004263
Natural varianti268 – 2681R → H in LCATD. 1 Publication
VAR_039032
Natural varianti298 – 2981T → A in FED and LCATD. 2 Publications
VAR_039033
Natural varianti298 – 2981T → I in LCATD. 1 Publication
VAR_039034
Natural varianti317 – 3171M → I in LCATD; partially defective enzyme. 2 Publications
VAR_004265
Natural varianti331 – 3311P → S in LCATD. 1 Publication
VAR_039035
Natural varianti333 – 3331V → M in LCATD. 2 Publications
VAR_039036
Natural varianti345 – 3451T → M in LCATD. 2 Publications
Corresponds to variant rs28940888 [ dbSNP | Ensembl ].
VAR_004266
Natural varianti396 – 3961L → R in a patient with LCATD. 2 Publications
VAR_039037
Natural varianti406 – 4061F → V in LCATD. 1 Publication
VAR_039038
Fish-eye disease (FED) [MIM:136120]: A disorder of lipoprotein metabolism due to partial lecithin-cholesterol acyltransferase deficiency that affects only alpha-LCAT activity. FED is characterized by low plasma HDL and corneal opacities due to accumulation of cholesterol deposits in the cornea ('fish-eye').
Note: The disease is caused by mutations affecting the gene represented in this entry.7 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341P → L in FED. 1 Publication
VAR_004252
Natural varianti34 – 341P → Q in FED. 1 Publication
VAR_039021
Natural varianti70 – 701V → E in FED. 1 Publication
VAR_039023
Natural varianti95 – 951G → R in a compound heterozygote carrying H-164; intermediate phenotype between LCATD and FED; reduction of activity. 1 Publication
VAR_039024
Natural varianti99 – 991W → S in FED; loss of activity. 1 Publication
VAR_066862
Natural varianti123 – 1231R → C in FED. 1 Publication
VAR_039026
Natural varianti147 – 1471T → I in FED. 1 Publication
VAR_004256
Natural varianti159 – 1591R → Q in FED. 1 Publication
VAR_039027
Natural varianti164 – 1641R → H in LCATD; also in a compound heterozygote carrying R-95 with intermediate phenotype between LCATD and FED; loss of activity. 2 Publications
VAR_004258
Natural varianti276 – 2761M → K in FED. 1 Publication
VAR_004264
Natural varianti298 – 2981T → A in FED and LCATD. 2 Publications
VAR_039033
Natural varianti338 – 3381L → F in FED; results in reduced protein secretion and activity. 1 Publication
VAR_066867
Natural varianti347 – 3471R → C in FED; results in reduced activity. 1 Publication
VAR_066868
Natural varianti371 – 3711T → M in FED. 1 Publication
VAR_004267

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi173 – 1731E → A: Increased activity towards PAPC. Increased PAPC/POPC activity ratio. 1 Publication
Mutagenesisi173 – 1731E → D: Little change in enzyme specific activity nor in PAPC/POPC activity ratio. 1 Publication
Mutagenesisi173 – 1731E → K: Decreased enzyme specific activity. Increased PAPC/POPC activity ratio. 1 Publication
Mutagenesisi173 – 1731E → L: Increased activity towards PAPC. Increased PAPC/POPC activity ratio. 1 Publication
Mutagenesisi173 – 1731E → Q: Decreased enzyme specific activity. Increased PAPC/POPC activity ratio. 1 Publication

Keywords - Diseasei

Corneal dystrophy, Disease mutation

Organism-specific databases

MIMi136120. phenotype.
245900. phenotype.
Orphaneti79293. Familial LCAT deficiency.
79292. Fish-eye disease.
PharmGKBiPA226.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424
Add
BLAST
Chaini25 – 440416Phosphatidylcholine-sterol acyltransferase
PRO_0000017802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi44 – 441N-linked (GlcNAc...) (complex)2 Publications
Disulfide bondi74 ↔ 981 Publication
Glycosylationi108 – 1081N-linked (GlcNAc...) (complex)1 Publication
Glycosylationi296 – 2961N-linked (GlcNAc...) (complex)2 Publications
Disulfide bondi337 ↔ 3801 Publication
Glycosylationi408 – 4081N-linked (GlcNAc...) (complex)1 Publication
Glycosylationi431 – 4311O-linked (GalNAc...)1 Publication
Glycosylationi433 – 4331O-linked (GalNAc...)1 Publication

Post-translational modificationi

O- and N-glycosylated. O-glycosylation on Thr-431 and Ser-433 consists of sialylated galactose beta 1-->3N-acetylgalactosamine structures. N-glycosylated sites contain sialylated triantennary and/or biantennary complex structures.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP04180.
PaxDbiP04180.
PeptideAtlasiP04180.
PRIDEiP04180.

PTM databases

PhosphoSiteiP04180.
UniCarbKBiP04180.

Expressioni

Tissue specificityi

Expressed mainly in brain, liver and testes. Secreted into plasma and cerebral spinal fluid. Expressed in Hep-G2 cell line.2 Publications

Gene expression databases

ArrayExpressiP04180.
BgeeiP04180.
CleanExiHS_LCAT.
GenevestigatoriP04180.

Organism-specific databases

HPAiHPA044767.

Interactioni

Protein-protein interaction databases

BioGridi110123. 5 interactions.
DIPiDIP-29620N.
IntActiP04180. 1 interaction.
STRINGi9606.ENSP00000264005.

Structurei

3D structure databases

ProteinModelPortaliP04180.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi426 – 43914Pro-rich
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG322613.
HOGENOMiHOG000238654.
HOVERGENiHBG017055.
InParanoidiP04180.
KOiK00650.
OMAiLRQPQSW.
PhylomeDBiP04180.
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.

P04180-1 [UniParc]FASTAAdd to Basket

« Hide

MGPPGSPWQW VTLLLGLLLP PAAPFWLLNV LFPPHTTPKA ELSNHTRPVI    50
LVPGCLGNQL EAKLDKPDVV NWMCYRKTED FFTIWLDLNM FLPLGVDCWI 100
DNTRVVYNRS SGLVSNAPGV QIRVPGFGKT YSVEYLDSSK LAGYLHTLVQ 150
NLVNNGYVRD ETVRAAPYDW RLEPGQQEEY YRKLAGLVEE MHAAYGKPVF 200
LIGHSLGCLH LLYFLLRQPQ AWKDRFIDGF ISLGAPWGGS IKPMLVLASG 250
DNQGIPIMSS IKLKEEQRIT TTSPWMFPSR MAWPEDHVFI STPSFNYTGR 300
DFQRFFADLH FEEGWYMWLQ SRDLLAGLPA PGVEVYCLYG VGLPTPRTYI 350
YDHGFPYTDP VGVLYEDGDD TVATRSTELC GLWQGRQPQP VHLLPLHGIQ 400
HLNMVFSNLT LEHINAILLG AYRQGPPASP TASPEPPPPE 440
Length:440
Mass (Da):49,578
Last modified:March 20, 1987 - v1
Checksum:iB315EF118AA7A378
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171L → LLLPPAAPFWL in LCATD.
VAR_004251
Natural varianti29 – 291N → I in LCATD. 1 Publication
VAR_039020
Natural varianti34 – 341P → L in FED. 1 Publication
VAR_004252
Natural varianti34 – 341P → Q in FED. 1 Publication
VAR_039021
Natural varianti37 – 371T → M in LCATD. 1 Publication
VAR_039022
Natural varianti54 – 541G → S in LCATD. 1 Publication
VAR_004253
Natural varianti57 – 571G → R in LCATD. 1 Publication
VAR_004254
Natural varianti70 – 701V → E in FED. 1 Publication
VAR_039023
Natural varianti95 – 951G → R in a compound heterozygote carrying H-164; intermediate phenotype between LCATD and FED; reduction of activity. 1 Publication
VAR_039024
Natural varianti99 – 991W → S in FED; loss of activity. 1 Publication
VAR_066862
Natural varianti115 – 1151S → P.1 Publication
VAR_039025
Natural varianti117 – 1171A → T in LCATD. 2 Publications
Corresponds to variant rs28940886 [ dbSNP | Ensembl ].
VAR_004255
Natural varianti123 – 1231R → C in FED. 1 Publication
VAR_039026
Natural varianti134 – 1352EY → DN in a patient with low HDL-cholesterol levels; results in reduced activity.
VAR_066863
Natural varianti147 – 1471T → I in FED. 1 Publication
VAR_004256
Natural varianti159 – 1591R → Q in FED. 1 Publication
VAR_039027
Natural varianti159 – 1591R → W in LCATD. 1 Publication
Corresponds to variant rs28940887 [ dbSNP | Ensembl ].
VAR_004257
Natural varianti164 – 1641R → C in LCATD. 1 Publication
VAR_039028
Natural varianti164 – 1641R → H in LCATD; also in a compound heterozygote carrying R-95 with intermediate phenotype between LCATD and FED; loss of activity. 2 Publications
VAR_004258
Natural varianti165 – 1651A → T.1 Publication
VAR_039029
Natural varianti171 – 1711R → W in LCATD. 2 Publications
VAR_004259
Natural varianti180 – 1801Y → N in LCATD.
VAR_004260
Natural varianti182 – 1821R → C.2 Publications
VAR_004261
Natural varianti205 – 2051S → N in LCATD. 1 Publication
VAR_039030
Natural varianti232 – 2321S → T.3 Publications
Corresponds to variant rs4986970 [ dbSNP | Ensembl ].
VAR_017030
Natural varianti233 – 2331L → P in LCATD. 1 Publication
Corresponds to variant rs28942087 [ dbSNP | Ensembl ].
VAR_004262
Natural varianti242 – 2421K → N in LCATD. 1 Publication
VAR_039031
Natural varianti246 – 2461V → F in a patient with low HDL-cholesterol levels; the mutant is hardly secreted and is catalytically inactive. 1 Publication
VAR_066864
Natural varianti252 – 2521N → K in LCATD. 1 Publication
VAR_004263
Natural varianti268 – 2681R → C in a patient with low HDL-cholesterol levels; the mutant is hardly secreted and is catalytically inactive. 1 Publication
VAR_066865
Natural varianti268 – 2681R → H in LCATD. 1 Publication
VAR_039032
Natural varianti276 – 2761M → K in FED. 1 Publication
VAR_004264
Natural varianti298 – 2981T → A in FED and LCATD. 2 Publications
VAR_039033
Natural varianti298 – 2981T → I in LCATD. 1 Publication
VAR_039034
Natural varianti317 – 3171M → I in LCATD; partially defective enzyme. 2 Publications
VAR_004265
Natural varianti322 – 3221R → C in a patient with low HDL-cholesterol levels; reduced protein secretion. 1 Publication
VAR_066866
Natural varianti331 – 3311P → S in LCATD. 1 Publication
VAR_039035
Natural varianti333 – 3331V → M in LCATD. 2 Publications
VAR_039036
Natural varianti338 – 3381L → F in FED; results in reduced protein secretion and activity. 1 Publication
VAR_066867
Natural varianti345 – 3451T → M in LCATD. 2 Publications
Corresponds to variant rs28940888 [ dbSNP | Ensembl ].
VAR_004266
Natural varianti347 – 3471R → C in FED; results in reduced activity. 1 Publication
VAR_066868
Natural varianti371 – 3711T → M in FED. 1 Publication
VAR_004267
Natural varianti396 – 3961L → R in a patient with LCATD. 2 Publications
VAR_039037
Natural varianti406 – 4061F → V in LCATD. 1 Publication
VAR_039038

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571I → H in CAB56610. 1 Publication
Sequence conflicti257 – 2571I → H in AAA59499. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04981 Genomic DNA. Translation: CAA28651.1.
M12625 mRNA. Translation: AAA59498.1.
AY422210 Genomic DNA. Translation: AAR03499.1.
BT009748 mRNA. Translation: AAP88750.1.
AC040162 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83190.1.
BC014781 mRNA. Translation: AAH14781.1.
M26268 mRNA. Translation: AAA59499.1.
X06537 mRNA. Translation: CAB56610.1.
M17959 Genomic DNA. Translation: AAA59500.1.
CCDSiCCDS10854.1.
PIRiA00571. XXHUN.
RefSeqiNP_000220.1. NM_000229.1.
UniGeneiHs.387239.

Genome annotation databases

EnsembliENST00000264005; ENSP00000264005; ENSG00000213398.
GeneIDi3931.
KEGGihsa:3931.
UCSCiuc002euy.1. human.

Polymorphism databases

DMDMi125993.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Lecithin-cholesterol acyltransferase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04981 Genomic DNA. Translation: CAA28651.1 .
M12625 mRNA. Translation: AAA59498.1 .
AY422210 Genomic DNA. Translation: AAR03499.1 .
BT009748 mRNA. Translation: AAP88750.1 .
AC040162 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83190.1 .
BC014781 mRNA. Translation: AAH14781.1 .
M26268 mRNA. Translation: AAA59499.1 .
X06537 mRNA. Translation: CAB56610.1 .
M17959 Genomic DNA. Translation: AAA59500.1 .
CCDSi CCDS10854.1.
PIRi A00571. XXHUN.
RefSeqi NP_000220.1. NM_000229.1.
UniGenei Hs.387239.

3D structure databases

ProteinModelPortali P04180.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110123. 5 interactions.
DIPi DIP-29620N.
IntActi P04180. 1 interaction.
STRINGi 9606.ENSP00000264005.

Chemistry

ChEMBLi CHEMBL5942.

PTM databases

PhosphoSitei P04180.
UniCarbKBi P04180.

Polymorphism databases

DMDMi 125993.

Proteomic databases

MaxQBi P04180.
PaxDbi P04180.
PeptideAtlasi P04180.
PRIDEi P04180.

Protocols and materials databases

DNASUi 3931.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264005 ; ENSP00000264005 ; ENSG00000213398 .
GeneIDi 3931.
KEGGi hsa:3931.
UCSCi uc002euy.1. human.

Organism-specific databases

CTDi 3931.
GeneCardsi GC16M067973.
H-InvDB HIX0134431.
HGNCi HGNC:6522. LCAT.
HPAi HPA044767.
MIMi 136120. phenotype.
245900. phenotype.
606967. gene.
neXtProti NX_P04180.
Orphaneti 79293. Familial LCAT deficiency.
79292. Fish-eye disease.
PharmGKBi PA226.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322613.
HOGENOMi HOG000238654.
HOVERGENi HBG017055.
InParanoidi P04180.
KOi K00650.
OMAi LRQPQSW.
PhylomeDBi P04180.
TreeFami TF313258.

Enzyme and pathway databases

BRENDAi 2.3.1.43. 2681.
Reactomei REACT_13621. HDL-mediated lipid transport.

Miscellaneous databases

GeneWikii Lecithin%E2%80%94cholesterol_acyltransferase.
GenomeRNAii 3931.
NextBioi 15437.
PROi P04180.
SOURCEi Search...

Gene expression databases

ArrayExpressi P04180.
Bgeei P04180.
CleanExi HS_LCAT.
Genevestigatori P04180.

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. "Human lecithin-cholesterol acyltransferase gene: complete gene sequence and sites of expression."
    McLean J., Wion K., Drayna D., Fielding C., Lawn R.
    Nucleic Acids Res. 14:9397-9406(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  2. "Cloning and expression of human lecithin-cholesterol acyltransferase cDNA."
    McLean J., Fielding C., Drayna D., Dieplinger H., Baer B., Kohr W., Henzel W., Lawn R.
    Proc. Natl. Acad. Sci. U.S.A. 83:2335-2339(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Nickerson D.A., Smith J.D., Fullerton S.M., Clark A.G., Stengard J.H., Salomaa V., Boerwinkle E., Sing C.F., Weiss K.M.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Brain.
  8. "The isolation and characterisation of cDNA and genomic clones for human lecithin: cholesterol acyltransferase."
    Tata F., Chaves M.E., Markham A.F., Scrace G.D., Waterfield M.D., McIntyre N., Williamson R., Humphries S.E.
    Biochim. Biophys. Acta 910:142-148(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-440.
  9. "The isolation and characterisation of a cDNA clone for human lecithin:cholesterol acyl transferase and its use to analyse the genes in patients with LCAT deficiency and fish eye disease."
    Rogne S., Skretting G., Larsen F., Myklebost O., Mevag B., Carlson L.A., Holmquist L., Gjone E., Prydz H.
    Biochem. Biophys. Res. Commun. 148:161-169(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-440.
  10. "Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme."
    Yang C., Manoogian D., Pao Q., Lee F., Knapp R.D., Gotto A.M. Jr., Pownall H.J.
    J. Biol. Chem. 262:3086-3091(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
  11. "Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion."
    Schindler P.A., Settineri C.A., Collet X., Fielding C.J., Burlingame A.L.
    Protein Sci. 4:791-803(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-44; ASN-108; ASN-296; ASN-408; THR-431 AND SER-433, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "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.
  13. "Secretion of lecithin:cholesterol acyltransferase by brain neuroglial cell lines."
    Collet X., Francone O., Besnard F., Fielding C.J.
    Biochem. Biophys. Res. Commun. 258:73-76(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  14. "Binding affinity and reactivity of lecithin cholesterol acyltransferase with native lipoproteins."
    Kosek A.B., Durbin D., Jonas A.
    Biochem. Biophys. Res. Commun. 258:548-551(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  15. "Formation of spherical, reconstituted high density lipoproteins containing both apolipoproteins A-I and A-II is mediated by lecithin:cholesterol acyltransferase."
    Clay M.A., Pyle D.H., Rye K.A., Barter P.J.
    J. Biol. Chem. 275:9019-9025(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HIGH-DENSITY LIPOPROTEIN PARTICLE REMODELING.
  16. "Negative charge at amino acid 149 is the molecular determinant for substrate specificity of lecithin: cholesterol acyltransferase for phosphatidylcholine containing 20-carbon sn-2 fatty acyl chains."
    Zhao Y., Wang J., Gebre A.K., Chisholm J.W., Parks J.S.
    Biochemistry 42:13941-13949(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY, MUTAGENESIS OF GLU-173.
  17. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44 AND ASN-296.
    Tissue: Plasma.
  18. "Relationship of endogenous hyperleptinemia to serum paraoxonase 1, cholesteryl ester transfer protein, and lecithin cholesterol acyltransferase in obese individuals."
    Bajnok L., Seres I., Varga Z., Jeges S., Peti A., Karanyi Z., Juhasz A., Csongradi E., Mezosi E., Nagy E.V., Paragh G.
    Metabolism 56:1542-1549(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH OBESITY.
  19. "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: ENZYME REGULATION, SUBCELLULAR LOCATION.
  20. "An amino acid exchange in exon I of the human lecithin: cholesterol acyltransferase (LCAT) gene is associated with fish eye disease."
    Skretting G., Prydz H.
    Biochem. Biophys. Res. Commun. 182:583-587(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FED LEU-34.
  21. "Two different allelic mutations in the lecithin-cholesterol acyltransferase gene associated with the fish eye syndrome. Lecithin-cholesterol acyltransferase (Thr123-->Ile) and lecithin-cholesterol acyltransferase (Thr347-->Met)."
    Klein H.-G., Lohse P., Pritchard P.H., Bojanovski D., Schmidt H., Brewer H.B. Jr.
    J. Clin. Invest. 89:499-506(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FED ILE-147 AND MET-371.
  22. "Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele."
    Taramelli R., Pontoglio M., Candiani G., Ottolenghi S., Dieplinger H., Catapano A., Albers J., Vergani C., McLean J.
    Hum. Genet. 85:195-199(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LCATD TRP-171.
  23. "Differential phenotypic expression by three mutant alleles in familial lecithin:cholesterol acyltransferase deficiency."
    Gotoda T., Yamada N., Murase T., Sakuma M., Murayama N., Shimano H., Kozaki K., Albers J.J., Yazaki Y., Akanuma Y.
    Lancet 338:778-781(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LCATD LYS-252 AND ILE-317.
  24. "The genetic defect of the original Norwegian lecithin:cholesterol acyltransferase deficiency families."
    Skretting G., Blomhoff J.P., Solheim J., Prydz H.
    FEBS Lett. 309:307-310(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FED LYS-276.
  25. "Lecithin-cholesterol acyltransferase (LCAT) deficiency with a missense mutation in exon 6 of the LCAT gene."
    Maeda E., Naka Y., Matozaki T., Sakuma M., Akanuma Y., Yoshino G., Kasuga M.
    Biochem. Biophys. Res. Commun. 178:460-466(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LCATD ILE-317.
  26. "Genetic and phenotypic heterogeneity in familial lecithin: cholesterol acyltransferase (LCAT) deficiency. Six newly identified defective alleles further contribute to the structural heterogeneity in this disease."
    Funke H., von Eckardstein A., Pritchard P.H., Hornby A.E., Wiebusch H., Motti C., Hayden M.R., Dachet C., Jacotot B., Gerdes U., Faergeman O., Albers J.J., Colleoni N., Catapano A., Frohlich J., Assmann G.
    J. Clin. Invest. 91:677-683(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LCATD THR-117; TRP-159; PRO-233 AND MET-345, VARIANT CYS-182.
  27. "Lecithin:cholesterol acyltransferase deficiency: identification of a causative gene mutation and a co-inherited protein polymorphism."
    Hill J.S., O K., Wang X., Pritchard P.H.
    Biochim. Biophys. Acta 1181:321-323(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LCATD THR-117, VARIANT CYS-182.
  28. "A single G to A nucleotide transition in exon IV of the lecithin: cholesterol acyltransferase (LCAT) gene results in an Arg140 to His substitution and causes LCAT-deficiency."
    Steyrer E., Haubenwallner S., Hoerl G., Giessauf W., Kostner G.M., Zechner R.
    Hum. Genet. 96:105-109(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LCATD HIS-164, CHARACTERIZATION OF VARIANT LCATD HIS-164.
  29. "Deficiency of lecithin:cholesterol acyltransferase due to compound heterozygosity of two novel mutations (Gly33Arg and 30 bp ins) in the LCAT gene."
    Wiebusch H., Cullen P., Owen J.S., Collins D., Sharp P.S., Funke H., Assmann G.
    Hum. Mol. Genet. 4:143-145(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LCATD ARG-57 AND LEU-LEU-PRO-PRO-ALA-ALA-PRO-PHE-TRP-LEU-17 INS.
  30. Cited for: VARIANTS FED GLN-34 AND GLN-159.
  31. "Complete deficiency of plasma lecithin-cholesterol acyltransferase (LCAT) activity due to a novel homozygous mutation (Gly-30-Ser) in the LCAT gene."
    Owen J.S., Wiebusch H., Cullen P., Watts G.F., Lima V.L.M., Funke H., Assmann G.
    Hum. Mutat. 8:79-82(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LCATD SER-54.
  32. "A novel missense mutation (Asn5-->Ile) in lecithin: cholesterol acyltransferase (LCAT) gene in a Japanese patient with LCAT deficiency."
    Okubo M., Aoyama Y., Shio H., Albers J.J., Murase T.
    Int. J. Clin. Lab. Res. 26:250-254(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LCATD ILE-29.
  33. "Molecular basis of fish-eye disease in a patient from Spain. Characterization of a novel mutation in the LCAT gene and lipid analysis of the cornea."
    Blanco-Vaca F., Qu S.J., Fiol C., Fan H.Z., Pao Q., Marzal-Casacuberta A., Albers J.J., Hurtado I., Gracia V., Pinto X., Marti T., Pownall H.J.
    Arterioscler. Thromb. Vasc. Biol. 17:1382-1391(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FED CYS-123.
  34. "Transmission of two novel mutations in a pedigree with familial lecithin:cholesterol acyltransferase deficiency: structure-function relationships and studies in a compound heterozygous proband."
    Argyropoulos G., Jenkins A., Klein R.L., Lyons T., Wagenhorst B., St Armand J., Marcovina S.M., Albers J.J., Pritchard P.H., Garvey W.T.
    J. Lipid Res. 39:1870-1876(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LCATD MET-37 AND SER-331.
  35. "Hypocomplementemic type II membranoproliferative glomerulonephritis in a male patient with familial lecithin-cholesterol acyltransferase deficiency due to two different allelic mutations."
    Sessa A., Battini G., Meroni M., Daidone G., Carnera I., Brambilla P.L., Vigano G., Giordano F., Pallotti F., Torri Tarelli L., Calabresi L., Rolleri M., Bertolini S.
    Nephron 88:268-272(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LCATD ALA-298.
  36. "A novel LCAT mutation (Phe382-->Val) in a kindred with familial LCAT deficiency and defective apolipoprotein B-100."
    Nanjee M.N., Stocks J., Cooke C.J., Molhuizen H.O., Marcovina S., Crook D., Kastelein J.P., Miller N.E.
    Atherosclerosis 170:105-113(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS LCATD MET-345 AND VAL-406, VARIANT THR-232.
  37. "Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors."
    Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., Alvin G.B., Das K., Gilliam T.C.
    Hum. Mol. Genet. 12:2733-2743(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT THR-232.
  38. Cited for: VARIANTS FED GLU-70 AND ALA-298, VARIANTS LCATD CYS-164; TRP-171; ASN-205; ASN-242; HIS-268; ILE-298 AND MET-333, VARIANTS PRO-115; THR-165 AND ARG-396.
  39. "Familial lecithin-cholesterol acyltransferase deficiency: biochemical characteristics and molecular analysis of a new LCAT mutation in a Polish family."
    Idzior-Walus B., Sieradzki J., Kostner G., Malecki M.T., Klupa T., Wesolowska T., Rostworowski W., Hartwich J., Walus M., Kiec A.D., Naruszewicz M.
    Atherosclerosis 185:413-420(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LCATD MET-333.
  40. "Compound heterozygosity (G71R/R140H) in the lecithin:cholesterol acyltransferase (LCAT) gene results in an intermediate phenotype between LCAT-deficiency and fish-eye disease."
    Hoerl G., Kroisel P.M., Wagner E., Tiran B., Petek E., Steyrer E.
    Atherosclerosis 187:101-109(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-95, VARIANT LCATD HIS-164, CHARACTERIZATION OF VARIANT ARG-95.
  41. "LCAT deficiency: molecular and phenotypic characterization of an Italian family."
    Gigante M., Ranieri E., Cerullo G., Calabresi L., Iolascon A., Assmann G., Morrone L., Pisciotta L., Schena F.P., Gesualdo L.
    J. Nephrol. 19:375-381(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-232 AND ARG-396.
  42. "High prevalence of mutations in LCAT in patients with low HDL cholesterol levels in The Netherlands: identification and characterization of eight novel mutations."
    Holleboom A.G., Kuivenhoven J.A., Peelman F., Schimmel A.W., Peter J., Defesche J.C., Kastelein J.J., Hovingh G.K., Stroes E.S., Motazacker M.M.
    Hum. Mutat. 32:1290-1298(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS 134-GLU-TYR-135 DELINS ASP-ASN; PHE-246; CYS-268 AND CYS-322, VARIANTS FED SER-99; PHE-338 AND CYS-347, CHARACTERIZATION OF VARIANTS 134-GLU-TYR-135 DELINS ASP-ASN; PHE-246; CYS-268 AND CYS-322, CHARACTERIZATION OF VARIANTS FED SER-99; PHE-338 CYS-347 AND CYS-347.

Entry informationi

Entry nameiLCAT_HUMAN
AccessioniPrimary (citable) accession number: P04180
Secondary accession number(s): Q53XQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: September 3, 2014
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Levels of LCAT activity correlates inversely with leptin levels as well as with obesity for a wide range of BMI values.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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