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Protein

Phosphatidylcholine-sterol acyltransferase

Gene

LCAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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) (PubMed:10329423, PubMed:19065001, PubMed:26195816). 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 (PubMed:8820107). 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 (PubMed:10722751).6 Publications

Miscellaneous

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

Catalytic activityi

Phosphatidylcholine + a sterol = 1-acylglycerophosphocholine + a sterol ester.PROSITE-ProRule annotation8 Publications

Activity 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
  1. Vmax=8.3 mmol/min/mg enzyme with LDL as substrate1 Publication
  2. Vmax=0.58 mmol/min/mg enzyme with HDL2 as substrate1 Publication
  3. Vmax=2.0 mmol/min/mg enzyme with HDL3 as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei173Determinant for substrate specificity1 Publication1
Active sitei205Nucleophile1 Publication1
Active sitei369Charge relay system1 Publication1
Active sitei401Charge relay system1 Publication1

GO - Molecular functioni

  • apolipoprotein A-I binding Source: BHF-UCL
  • phosphatidylcholine-sterol O-acyltransferase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processCholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

BRENDAi2.3.1.43 2681
ReactomeiR-HSA-8964058 HDL remodeling
SABIO-RKiP04180
SIGNORiP04180

Protein family/group databases

ESTHERihuman-LCAT PC-sterol_acyltransferase

Chemistry databases

SwissLipidsiSLP:000000660

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylcholine-sterol acyltransferase (EC:2.3.1.437 Publications)
Alternative name(s):
Lecithin-cholesterol acyltransferase
Phospholipid-cholesterol acyltransferase
Gene namesi
Name:LCAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000213398.7
HGNCiHGNC:6522 LCAT
MIMi606967 gene
neXtProtiNX_P04180

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Lecithin-cholesterol acyltransferase deficiency (LCATD)15 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:245900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00425117L → LLLPPAAPFWL in LCATD. 1
Natural variantiVAR_03902029N → I in LCATD. 1 Publication1
Natural variantiVAR_03902237T → M in LCATD. 1 PublicationCorresponds to variant dbSNP:rs971887742Ensembl.1
Natural variantiVAR_00425354G → S in LCATD. 1 Publication1
Natural variantiVAR_00425457G → R in LCATD. 1 Publication1
Natural variantiVAR_004255117A → T in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940886EnsemblClinVar.1
Natural variantiVAR_004257159R → W in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28940887EnsemblClinVar.1
Natural variantiVAR_039028164R → C in LCATD. 1 Publication1
Natural variantiVAR_004258164R → H in LCATD; also in a compound heterozygote carrying R-95 with intermediate phenotype between LCATD and FED; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs769485083Ensembl.1
Natural variantiVAR_004259171R → W in LCATD. 2 Publications1
Natural variantiVAR_004260180Y → N in LCATD. Corresponds to variant dbSNP:rs749740660Ensembl.1
Natural variantiVAR_039030205S → N in LCATD. 1 Publication1
Natural variantiVAR_004262233L → P in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28942087EnsemblClinVar.1
Natural variantiVAR_039031242K → N in LCATD. 1 Publication1
Natural variantiVAR_004263252N → K in LCATD. 1 PublicationCorresponds to variant dbSNP:rs121908049EnsemblClinVar.1
Natural variantiVAR_039032268R → H in LCATD. 1 PublicationCorresponds to variant dbSNP:rs780824776Ensembl.1
Natural variantiVAR_039034298T → I in LCATD. 1 Publication1
Natural variantiVAR_004265317M → I in LCATD; partially defective enzyme. 2 PublicationsCorresponds to variant dbSNP:rs121908048EnsemblClinVar.1
Natural variantiVAR_039035331P → S in LCATD. 1 Publication1
Natural variantiVAR_039036333V → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs776035233Ensembl.1
Natural variantiVAR_004266345T → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940888EnsemblClinVar.1
Natural variantiVAR_039038406F → V in LCATD. 1 Publication1
Fish-eye disease (FED)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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').
See also OMIM:136120
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00425234P → L in FED. 1 PublicationCorresponds to variant dbSNP:rs121908051EnsemblClinVar.1
Natural variantiVAR_03902134P → Q in FED. 1 Publication1
Natural variantiVAR_03902370V → E in FED. 1 PublicationCorresponds to variant dbSNP:rs748427834Ensembl.1
Natural variantiVAR_06686299W → S in FED; loss of activity. 1 Publication1
Natural variantiVAR_039026123R → C in FED. 1 PublicationCorresponds to variant dbSNP:rs140068549Ensembl.1
Natural variantiVAR_004256147T → I in FED. 1 PublicationCorresponds to variant dbSNP:rs121908050EnsemblClinVar.1
Natural variantiVAR_039027159R → Q in FED. 1 PublicationCorresponds to variant dbSNP:rs768017317Ensembl.1
Natural variantiVAR_004264276M → K in FED. 1 PublicationCorresponds to variant dbSNP:rs121908054EnsemblClinVar.1
Natural variantiVAR_066867338L → F in FED; results in reduced protein secretion and activity. 1 Publication1
Natural variantiVAR_066868347R → C in FED; results in reduced activity. 1 PublicationCorresponds to variant dbSNP:rs202017590EnsemblClinVar.1
Natural variantiVAR_004267371T → M in FED. 1 PublicationCorresponds to variant dbSNP:rs121908053EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi173E → A: Increased activity towards PAPC. Increased PAPC/POPC activity ratio. 1 Publication1
Mutagenesisi173E → D: Little change in enzyme specific activity nor in PAPC/POPC activity ratio. 1 Publication1
Mutagenesisi173E → K: Decreased enzyme specific activity. Increased PAPC/POPC activity ratio. 1 Publication1
Mutagenesisi173E → L: Increased activity towards PAPC. Increased PAPC/POPC activity ratio. 1 Publication1
Mutagenesisi173E → Q: Decreased enzyme specific activity. Increased PAPC/POPC activity ratio. 1 Publication1

Keywords - Diseasei

Corneal dystrophy, Disease mutation

Organism-specific databases

DisGeNETi3931
MalaCardsiLCAT
MIMi136120 phenotype
245900 phenotype
OpenTargetsiENSG00000213398
Orphaneti79293 Familial LCAT deficiency
79292 Fish-eye disease
PharmGKBiPA226

Chemistry databases

ChEMBLiCHEMBL5942

Polymorphism and mutation databases

BioMutaiLCAT
DMDMi125993

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000001780225 – 440Phosphatidylcholine-sterol acyltransferaseAdd BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi44N-linked (GlcNAc...) (complex) asparagine2 Publications1
Disulfide bondi74 ↔ 98Combined sources2 Publications
Glycosylationi108N-linked (GlcNAc...) (complex) asparagineCombined sources2 Publications1
Glycosylationi296N-linked (GlcNAc...) (complex) asparagineCombined sources3 Publications1
Disulfide bondi337 ↔ 380Combined sources2 Publications
Glycosylationi408N-linked (GlcNAc...) (complex) asparagineCombined sources2 Publications1
Glycosylationi431O-linked (GalNAc...) threonine1 Publication1
Glycosylationi433O-linked (GalNAc...) serine1 Publication1

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
ProteomicsDBi51671

PTM databases

GlyConnecti495
iPTMnetiP04180
PhosphoSitePlusiP04180
UniCarbKBiP04180

Expressioni

Tissue specificityi

Detected in blood plasma (PubMed:3458198, PubMed:8820107, PubMed:10222237). Detected in cerebral spinal fluid (at protein level) (PubMed:10222237). Detected in liver (PubMed:3797244, PubMed:3458198). Expressed mainly in brain, liver and testes.4 Publications

Gene expression databases

BgeeiENSG00000213398 Expressed in 136 organ(s), highest expression level in right lobe of liver
CleanExiHS_LCAT
ExpressionAtlasiP04180 baseline and differential
GenevisibleiP04180 HS

Organism-specific databases

HPAiHPA044767

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
APOA1P026472EBI-9104464,EBI-701692

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110123, 6 interactors
DIPiDIP-29620N
IntActiP04180, 1 interactor
STRINGi9606.ENSP00000264005

Chemistry databases

BindingDBiP04180

Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP04180
SMRiP04180
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi426 – 439Pro-richAdd BLAST14

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2369 Eukaryota
ENOG410Y9CF LUCA
GeneTreeiENSGT00390000004902
HOGENOMiHOG000238654
HOVERGENiHBG017055
InParanoidiP04180
KOiK00650
OMAiFEDGWYM
OrthoDBiEOG091G07S3
PhylomeDBiP04180
TreeFamiTF313258

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR003386 LACT/PDAT_acylTrfase
PfamiView protein in Pfam
PF02450 LCAT, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00120 LIPASE_SER, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All

P04180-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGPPGSPWQW VTLLLGLLLP PAAPFWLLNV LFPPHTTPKA ELSNHTRPVI
60 70 80 90 100
LVPGCLGNQL EAKLDKPDVV NWMCYRKTED FFTIWLDLNM FLPLGVDCWI
110 120 130 140 150
DNTRVVYNRS SGLVSNAPGV QIRVPGFGKT YSVEYLDSSK LAGYLHTLVQ
160 170 180 190 200
NLVNNGYVRD ETVRAAPYDW RLEPGQQEEY YRKLAGLVEE MHAAYGKPVF
210 220 230 240 250
LIGHSLGCLH LLYFLLRQPQ AWKDRFIDGF ISLGAPWGGS IKPMLVLASG
260 270 280 290 300
DNQGIPIMSS IKLKEEQRIT TTSPWMFPSR MAWPEDHVFI STPSFNYTGR
310 320 330 340 350
DFQRFFADLH FEEGWYMWLQ SRDLLAGLPA PGVEVYCLYG VGLPTPRTYI
360 370 380 390 400
YDHGFPYTDP VGVLYEDGDD TVATRSTELC GLWQGRQPQP VHLLPLHGIQ
410 420 430 440
HLNMVFSNLT LEHINAILLG AYRQGPPASP TASPEPPPPE
Length:440
Mass (Da):49,578
Last modified:March 20, 1987 - v1
Checksum:iB315EF118AA7A378
GO

Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
I3L0J6I3L0J6_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
80Annotation score:
J3QSE5J3QSE5_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
255Annotation score:
J3QKT0J3QKT0_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
138Annotation score:
I3L1Q6I3L1Q6_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
107Annotation score:
I3L3R0I3L3R0_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
93Annotation score:
I3L215I3L215_HUMAN
Phosphatidylcholine-sterol acyltran...
LCAT
61Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti257I → H in CAB56610 (PubMed:2823898).Curated1
Sequence conflicti257I → H in AAA59499 (PubMed:2823898).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00425117L → LLLPPAAPFWL in LCATD. 1
Natural variantiVAR_03902029N → I in LCATD. 1 Publication1
Natural variantiVAR_00425234P → L in FED. 1 PublicationCorresponds to variant dbSNP:rs121908051EnsemblClinVar.1
Natural variantiVAR_03902134P → Q in FED. 1 Publication1
Natural variantiVAR_03902237T → M in LCATD. 1 PublicationCorresponds to variant dbSNP:rs971887742Ensembl.1
Natural variantiVAR_00425354G → S in LCATD. 1 Publication1
Natural variantiVAR_00425457G → R in LCATD. 1 Publication1
Natural variantiVAR_03902370V → E in FED. 1 PublicationCorresponds to variant dbSNP:rs748427834Ensembl.1
Natural variantiVAR_03902495G → R in a compound heterozygote carrying H-164; intermediate phenotype between LCATD and FED; reduction of activity. 1 Publication1
Natural variantiVAR_06686299W → S in FED; loss of activity. 1 Publication1
Natural variantiVAR_039025115S → P1 PublicationCorresponds to variant dbSNP:rs1412883954Ensembl.1
Natural variantiVAR_004255117A → T in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940886EnsemblClinVar.1
Natural variantiVAR_039026123R → C in FED. 1 PublicationCorresponds to variant dbSNP:rs140068549Ensembl.1
Natural variantiVAR_066863134 – 135EY → DN in a patient with low HDL-cholesterol levels; results in reduced activity. 1 Publication2
Natural variantiVAR_004256147T → I in FED. 1 PublicationCorresponds to variant dbSNP:rs121908050EnsemblClinVar.1
Natural variantiVAR_039027159R → Q in FED. 1 PublicationCorresponds to variant dbSNP:rs768017317Ensembl.1
Natural variantiVAR_004257159R → W in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28940887EnsemblClinVar.1
Natural variantiVAR_039028164R → C in LCATD. 1 Publication1
Natural variantiVAR_004258164R → H in LCATD; also in a compound heterozygote carrying R-95 with intermediate phenotype between LCATD and FED; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs769485083Ensembl.1
Natural variantiVAR_039029165A → T1 PublicationCorresponds to variant dbSNP:rs1369994093Ensembl.1
Natural variantiVAR_004259171R → W in LCATD. 2 Publications1
Natural variantiVAR_004260180Y → N in LCATD. Corresponds to variant dbSNP:rs749740660Ensembl.1
Natural variantiVAR_004261182R → C2 PublicationsCorresponds to variant dbSNP:rs387906300EnsemblClinVar.1
Natural variantiVAR_039030205S → N in LCATD. 1 Publication1
Natural variantiVAR_017030232S → T3 PublicationsCorresponds to variant dbSNP:rs4986970Ensembl.1
Natural variantiVAR_004262233L → P in LCATD. 1 PublicationCorresponds to variant dbSNP:rs28942087EnsemblClinVar.1
Natural variantiVAR_039031242K → N in LCATD. 1 Publication1
Natural variantiVAR_066864246V → F in a patient with low HDL-cholesterol levels; the mutant is hardly secreted and is catalytically inactive. 1 Publication1
Natural variantiVAR_004263252N → K in LCATD. 1 PublicationCorresponds to variant dbSNP:rs121908049EnsemblClinVar.1
Natural variantiVAR_066865268R → C in a patient with low HDL-cholesterol levels; the mutant is hardly secreted and is catalytically inactive. 1 PublicationCorresponds to variant dbSNP:rs745320775Ensembl.1
Natural variantiVAR_039032268R → H in LCATD. 1 PublicationCorresponds to variant dbSNP:rs780824776Ensembl.1
Natural variantiVAR_004264276M → K in FED. 1 PublicationCorresponds to variant dbSNP:rs121908054EnsemblClinVar.1
Natural variantiVAR_039033298T → A in FED and LCATD. 2 Publications1
Natural variantiVAR_039034298T → I in LCATD. 1 Publication1
Natural variantiVAR_004265317M → I in LCATD; partially defective enzyme. 2 PublicationsCorresponds to variant dbSNP:rs121908048EnsemblClinVar.1
Natural variantiVAR_066866322R → C in a patient with low HDL-cholesterol levels; reduced protein secretion. 1 Publication1
Natural variantiVAR_039035331P → S in LCATD. 1 Publication1
Natural variantiVAR_039036333V → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs776035233Ensembl.1
Natural variantiVAR_066867338L → F in FED; results in reduced protein secretion and activity. 1 Publication1
Natural variantiVAR_004266345T → M in LCATD. 2 PublicationsCorresponds to variant dbSNP:rs28940888EnsemblClinVar.1
Natural variantiVAR_066868347R → C in FED; results in reduced activity. 1 PublicationCorresponds to variant dbSNP:rs202017590EnsemblClinVar.1
Natural variantiVAR_004267371T → M in FED. 1 PublicationCorresponds to variant dbSNP:rs121908053EnsemblClinVar.1
Natural variantiVAR_039037396L → R in a patient with LCATD. 2 Publications1
Natural variantiVAR_039038406F → V in LCATD. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Wikipedia

Lecithin-cholesterol acyltransferase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4X96X-ray8.69A/B/C/D45-421[»]
4XWGX-ray2.65A25-440[»]
4XX1X-ray3.60A/B/J25-440[»]
5BV7X-ray2.45A25-440[»]
5TXFX-ray3.10A/B/C/D25-440[»]
ProteinModelPortaliP04180
SMRiP04180
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110123, 6 interactors
DIPiDIP-29620N
IntActiP04180, 1 interactor
STRINGi9606.ENSP00000264005

Chemistry databases

BindingDBiP04180
ChEMBLiCHEMBL5942
SwissLipidsiSLP:000000660

Protein family/group databases

ESTHERihuman-LCAT PC-sterol_acyltransferase

PTM databases

GlyConnecti495
iPTMnetiP04180
PhosphoSitePlusiP04180
UniCarbKBiP04180

Polymorphism and mutation databases

BioMutaiLCAT
DMDMi125993

Proteomic databases

MaxQBiP04180
PaxDbiP04180
PeptideAtlasiP04180
PRIDEiP04180
ProteomicsDBi51671

Protocols and materials databases

DNASUi3931
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264005; ENSP00000264005; ENSG00000213398
GeneIDi3931
KEGGihsa:3931
UCSCiuc002euy.2 human

Organism-specific databases

CTDi3931
DisGeNETi3931
EuPathDBiHostDB:ENSG00000213398.7
GeneCardsiLCAT
H-InvDBiHIX0134431
HGNCiHGNC:6522 LCAT
HPAiHPA044767
MalaCardsiLCAT
MIMi136120 phenotype
245900 phenotype
606967 gene
neXtProtiNX_P04180
OpenTargetsiENSG00000213398
Orphaneti79293 Familial LCAT deficiency
79292 Fish-eye disease
PharmGKBiPA226
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2369 Eukaryota
ENOG410Y9CF LUCA
GeneTreeiENSGT00390000004902
HOGENOMiHOG000238654
HOVERGENiHBG017055
InParanoidiP04180
KOiK00650
OMAiFEDGWYM
OrthoDBiEOG091G07S3
PhylomeDBiP04180
TreeFamiTF313258

Enzyme and pathway databases

BRENDAi2.3.1.43 2681
ReactomeiR-HSA-8964058 HDL remodeling
SABIO-RKiP04180
SIGNORiP04180

Miscellaneous databases

ChiTaRSiLCAT human
GeneWikiiLecithin%E2%80%94cholesterol_acyltransferase
GenomeRNAii3931
PROiPR:P04180
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000213398 Expressed in 136 organ(s), highest expression level in right lobe of liver
CleanExiHS_LCAT
ExpressionAtlasiP04180 baseline and differential
GenevisibleiP04180 HS

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR003386 LACT/PDAT_acylTrfase
PfamiView protein in Pfam
PF02450 LCAT, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00120 LIPASE_SER, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiLCAT_HUMAN
AccessioniPrimary (citable) accession number: P04180
Secondary accession number(s): Q53XQ3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: November 7, 2018
This is version 194 of the entry and version 1 of the sequence. See 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
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