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P04180

- LCAT_HUMAN

UniProt

P04180 - LCAT_HUMAN

Protein

Phosphatidylcholine-sterol acyltransferase

Gene

LCAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 1 (20 Mar 1987)
      Previous versions | rss
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    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.PROSITE-ProRule annotation

    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 HDL21 Publication
    3. KM=0.10 mM for HDL31 Publication

    Vmax=8.3 mmol/min/mg enzyme with LDL as substrate1 Publication

    Vmax=0.58 mmol/min/mg enzyme with HDL2 as substrate1 Publication

    Vmax=2.0 mmol/min/mg enzyme with HDL3 as substrate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei173 – 1731Determinant for substrate specificity
    Active sitei205 – 2051Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

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

    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

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

    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

    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.15 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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').7 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 – 2424Add
    BLAST
    Chaini25 – 440416Phosphatidylcholine-sterol acyltransferasePRO_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.2 Publications

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. Lipase family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti257 – 2571I → H in CAB56610. (PubMed:2823898)Curated
    Sequence conflicti257 – 2571I → H in AAA59499. (PubMed:2823898)Curated

    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 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...
    MobiDBi 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

    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: October 1, 2014
    This is version 158 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