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Protein

Phosphatidylcholine-sterol acyltransferase

Gene

LCAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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) (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

Catalytic activityi

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

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
  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

  • cholesterol esterification Source: UniProtKB
  • cholesterol homeostasis Source: BHF-UCL
  • cholesterol metabolic process Source: UniProtKB
  • cholesterol transport Source: MGI
  • high-density lipoprotein particle remodeling Source: UniProtKB
  • lipoprotein biosynthetic process Source: Ensembl
  • lipoprotein metabolic process Source: Reactome
  • phosphatidylcholine biosynthetic process Source: BHF-UCL
  • phosphatidylcholine metabolic process Source: UniProtKB
  • phospholipid metabolic process Source: BHF-UCL
  • regulation of high-density lipoprotein particle assembly Source: Ensembl
  • reverse cholesterol transport Source: BHF-UCL
  • 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

BioCyciZFISH:HS02453-MONOMER.
BRENDAi2.3.1.43. 2681.
ReactomeiR-HSA-194223. HDL-mediated lipid transport.
SABIO-RKP04180.

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

HGNCiHGNC:6522. LCAT.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • high-density lipoprotein particle Source: BHF-UCL
Complete GO annotation...

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 Publication1
Natural variantiVAR_00425354G → S in LCATD. 1 Publication1
Natural variantiVAR_00425457G → R in LCATD. 1 Publication1
Natural variantiVAR_03902495G → R in a compound heterozygote carrying H-164; intermediate phenotype between LCATD and FED; reduction of activity. 1 Publication1
Natural variantiVAR_004255117A → T in LCATD. 2 PublicationsCorresponds to variant rs28940886dbSNPEnsembl.1
Natural variantiVAR_004257159R → W in LCATD. 1 PublicationCorresponds to variant rs28940887dbSNPEnsembl.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 rs769485083dbSNPEnsembl.1
Natural variantiVAR_004259171R → W in LCATD. 2 Publications1
Natural variantiVAR_004260180Y → N in LCATD. Corresponds to variant rs749740660dbSNPEnsembl.1
Natural variantiVAR_039030205S → N in LCATD. 1 Publication1
Natural variantiVAR_004262233L → P in LCATD. 1 PublicationCorresponds to variant rs28942087dbSNPEnsembl.1
Natural variantiVAR_039031242K → N in LCATD. 1 Publication1
Natural variantiVAR_004263252N → K in LCATD. 1 PublicationCorresponds to variant rs121908049dbSNPEnsembl.1
Natural variantiVAR_039032268R → H in LCATD. 1 PublicationCorresponds to variant rs780824776dbSNPEnsembl.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 rs121908048dbSNPEnsembl.1
Natural variantiVAR_039035331P → S in LCATD. 1 Publication1
Natural variantiVAR_039036333V → M in LCATD. 2 PublicationsCorresponds to variant rs776035233dbSNPEnsembl.1
Natural variantiVAR_004266345T → M in LCATD. 2 PublicationsCorresponds to variant rs28940888dbSNPEnsembl.1
Natural variantiVAR_039037396L → R in a patient with LCATD. 2 Publications1
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 rs121908051dbSNPEnsembl.1
Natural variantiVAR_03902134P → Q in FED. 1 Publication1
Natural variantiVAR_03902370V → E in FED. 1 PublicationCorresponds to variant rs748427834dbSNPEnsembl.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_039026123R → C in FED. 1 PublicationCorresponds to variant rs140068549dbSNPEnsembl.1
Natural variantiVAR_004256147T → I in FED. 1 PublicationCorresponds to variant rs121908050dbSNPEnsembl.1
Natural variantiVAR_039027159R → Q in FED. 1 PublicationCorresponds to variant rs768017317dbSNPEnsembl.1
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 rs769485083dbSNPEnsembl.1
Natural variantiVAR_004264276M → K in FED. 1 PublicationCorresponds to variant rs121908054dbSNPEnsembl.1
Natural variantiVAR_039033298T → A in FED and LCATD. 2 Publications1
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 rs202017590dbSNPEnsembl.1
Natural variantiVAR_004267371T → M in FED. 1 PublicationCorresponds to variant rs121908053dbSNPEnsembl.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)2 Publications1
Disulfide bondi74 ↔ 98Combined sources2 Publications
Glycosylationi108N-linked (GlcNAc...) (complex)Combined sources2 Publications1
Glycosylationi296N-linked (GlcNAc...) (complex)Combined sources3 Publications1
Disulfide bondi337 ↔ 380Combined sources2 Publications
Glycosylationi408N-linked (GlcNAc...) (complex)Combined sources2 Publications1
Glycosylationi431O-linked (GalNAc...)1 Publication1
Glycosylationi433O-linked (GalNAc...)1 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.

PTM databases

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.
CleanExiHS_LCAT.
ExpressionAtlasiP04180. baseline and differential.
GenevisibleiP04180. HS.

Organism-specific databases

HPAiHPA044767.

Interactioni

GO - Molecular functioni

  • apolipoprotein A-I binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110123. 5 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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi49 – 52Combined sources4
Beta strandi60 – 63Combined sources4
Beta strandi82 – 86Combined sources5
Helixi88 – 91Combined sources4
Helixi95 – 103Combined sources9
Beta strandi105 – 107Combined sources3
Turni109 – 111Combined sources3
Beta strandi114 – 117Combined sources4
Beta strandi121 – 123Combined sources3
Turni125 – 128Combined sources4
Helixi131 – 134Combined sources4
Beta strandi135 – 137Combined sources3
Beta strandi142 – 145Combined sources4
Helixi146 – 153Combined sources8
Turni154 – 156Combined sources3
Turni160 – 162Combined sources3
Beta strandi163 – 165Combined sources3
Helixi174 – 176Combined sources3
Helixi178 – 195Combined sources18
Beta strandi199 – 204Combined sources6
Helixi206 – 217Combined sources12
Helixi220 – 226Combined sources7
Beta strandi227 – 234Combined sources8
Helixi242 – 248Combined sources7
Turni250 – 252Combined sources3
Turni255 – 257Combined sources3
Beta strandi270 – 272Combined sources3
Helixi274 – 276Combined sources3
Turni280 – 282Combined sources3
Beta strandi288 – 291Combined sources4
Beta strandi296 – 298Combined sources3
Helixi302 – 308Combined sources7
Helixi312 – 321Combined sources10
Turni322 – 327Combined sources6
Beta strandi335 – 350Combined sources16
Turni353 – 357Combined sources5
Beta strandi361 – 373Combined sources13
Helixi374 – 377Combined sources4
Helixi378 – 383Combined sources6
Beta strandi386 – 389Combined sources4
Beta strandi391 – 397Combined sources7
Helixi401 – 403Combined sources3
Turni404 – 406Combined sources3
Helixi408 – 419Combined sources12
Turni420 – 422Combined sources3

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[»]
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.
OMAiTHSTELC.
OrthoDBiEOG091G07S3.
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

        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

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 rs121908051dbSNPEnsembl.1
Natural variantiVAR_03902134P → Q in FED. 1 Publication1
Natural variantiVAR_03902237T → M in LCATD. 1 Publication1
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 rs748427834dbSNPEnsembl.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 → P.1 Publication1
Natural variantiVAR_004255117A → T in LCATD. 2 PublicationsCorresponds to variant rs28940886dbSNPEnsembl.1
Natural variantiVAR_039026123R → C in FED. 1 PublicationCorresponds to variant rs140068549dbSNPEnsembl.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 rs121908050dbSNPEnsembl.1
Natural variantiVAR_039027159R → Q in FED. 1 PublicationCorresponds to variant rs768017317dbSNPEnsembl.1
Natural variantiVAR_004257159R → W in LCATD. 1 PublicationCorresponds to variant rs28940887dbSNPEnsembl.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 rs769485083dbSNPEnsembl.1
Natural variantiVAR_039029165A → T.1 Publication1
Natural variantiVAR_004259171R → W in LCATD. 2 Publications1
Natural variantiVAR_004260180Y → N in LCATD. Corresponds to variant rs749740660dbSNPEnsembl.1
Natural variantiVAR_004261182R → C.2 PublicationsCorresponds to variant rs387906300dbSNPEnsembl.1
Natural variantiVAR_039030205S → N in LCATD. 1 Publication1
Natural variantiVAR_017030232S → T.3 PublicationsCorresponds to variant rs4986970dbSNPEnsembl.1
Natural variantiVAR_004262233L → P in LCATD. 1 PublicationCorresponds to variant rs28942087dbSNPEnsembl.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 rs121908049dbSNPEnsembl.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 rs745320775dbSNPEnsembl.1
Natural variantiVAR_039032268R → H in LCATD. 1 PublicationCorresponds to variant rs780824776dbSNPEnsembl.1
Natural variantiVAR_004264276M → K in FED. 1 PublicationCorresponds to variant rs121908054dbSNPEnsembl.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 rs121908048dbSNPEnsembl.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 rs776035233dbSNPEnsembl.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 rs28940888dbSNPEnsembl.1
Natural variantiVAR_066868347R → C in FED; results in reduced activity. 1 PublicationCorresponds to variant rs202017590dbSNPEnsembl.1
Natural variantiVAR_004267371T → M in FED. 1 PublicationCorresponds to variant rs121908053dbSNPEnsembl.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

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[»]
ProteinModelPortaliP04180.
SMRiP04180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110123. 5 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

iPTMnetiP04180.
PhosphoSitePlusiP04180.
UniCarbKBiP04180.

Polymorphism and mutation databases

BioMutaiLCAT.
DMDMi125993.

Proteomic databases

MaxQBiP04180.
PaxDbiP04180.
PeptideAtlasiP04180.
PRIDEiP04180.

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.
GeneCardsiLCAT.
H-InvDBHIX0134431.
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.
OMAiTHSTELC.
OrthoDBiEOG091G07S3.
PhylomeDBiP04180.
TreeFamiTF313258.

Enzyme and pathway databases

BioCyciZFISH:HS02453-MONOMER.
BRENDAi2.3.1.43. 2681.
ReactomeiR-HSA-194223. HDL-mediated lipid transport.
SABIO-RKP04180.

Miscellaneous databases

ChiTaRSiLCAT. human.
GeneWikiiLecithin%E2%80%94cholesterol_acyltransferase.
GenomeRNAii3931.
PROiP04180.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000213398.
CleanExiHS_LCAT.
ExpressionAtlasiP04180. baseline and differential.
GenevisibleiP04180. HS.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 177 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.