Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphatidylcholine-sterol acyltransferase

Gene

Lcat

Organism
Rattus norvegicus (Rat)
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). The cholesterol ester is then transported back to the liver. Also produced in the brain by primary astrocytes, and esterifies free cholesterol on nascent APOE-containing lipoproteins secreted from glia and influences cerebral spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins. Required for remodeling high-density lipoprotein particles into their spherical forms (By similarity). Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines (PubMed:8820107, PubMed:14636062).By similarity2 Publications

Catalytic activityi

Phosphatidylcholine + a sterol = 1-acylglycerophosphocholine + a sterol ester.PROSITE-ProRule annotation2 Publications

Enzyme regulationi

APOA1 is the most potent activator in plasma. Also activated by APOE, APOC1 and APOA4 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei173Determinant for substrate specificity1 Publication1
Active sitei205NucleophileBy similarity1
Active sitei369Charge relay systemBy similarity1
Active sitei401Charge relay systemBy similarity1

GO - Molecular functioni

  • phosphatidylcholine-sterol O-acyltransferase activity Source: RGD
  • phospholipase A2 activity Source: RGD

GO - Biological processi

  • cholesterol esterification Source: UniProtKB
  • cholesterol metabolic process Source: RGD
  • lipoprotein metabolic process Source: RGD
  • phosphatidylcholine metabolic process Source: UniProtKB
  • response to copper ion Source: RGD
  • response to glucocorticoid Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Protein family/group databases

ESTHERiratno-lcat. PC-sterol_acyltransferase.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylcholine-sterol acyltransferase (EC:2.3.1.432 Publications)
Alternative name(s):
Lecithin-cholesterol acyltransferase1 Publication
Phospholipid-cholesterol acyltransferase
Gene namesi
Name:Lcat
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2993. Lcat.

Subcellular locationi

  • Secreted 2 Publications

  • Note: Secreted into blood plasma (PubMed:8820107). Produced in astrocytes and secreted into cerebral spinal fluid (CSF) (By similarity).By similarity1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi173A → E: Reduced activity with 20-carbon phophatidylcholine as substrate. Little change with 18-carbon phophatidylcholine as substrate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24By similarityAdd BLAST24
ChainiPRO_000001780625 – 440Phosphatidylcholine-sterol acyltransferaseAdd BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi44N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi74 ↔ 98By similarity
Glycosylationi108N-linked (GlcNAc...)Sequence analysis1
Glycosylationi296N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi337 ↔ 380By similarity
Glycosylationi397N-linked (GlcNAc...)Sequence analysis1
Glycosylationi408N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP18424.
PRIDEiP18424.

Expressioni

Tissue specificityi

Detected in blood plasma (at protein level) (PubMed:8820107).1 Publication

Interactioni

Protein-protein interaction databases

IntActiP18424. 1 interactor.
STRINGi10116.ENSRNOP00000026583.

Structurei

3D structure databases

ProteinModelPortaliP18424.
SMRiP18424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi423 – 438Pro-richAdd BLAST16

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2369. Eukaryota.
ENOG410Y9CF. LUCA.
HOGENOMiHOG000238654.
HOVERGENiHBG017055.
InParanoidiP18424.
PhylomeDBiP18424.

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.

P18424-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLPGSPWQW VLLLLGLLLP PATSFWLLNV LFPPHTTPKA ELSNHTRPVI
60 70 80 90 100
LVPGCMGNRL EAKLDKPNVV NWLCYRKTED FFTIWLDFNM FLPLGVDCWI
110 120 130 140 150
DNTRVVYNRS SGHMSNAPGV QIRVPGFGKT YSVEYLDDNK LAGYLNTLVQ
160 170 180 190 200
NLVNNGYVRD ETVRAAPYDW RLAPRQQDEY YQKLAGLVEE MYAAYGKPVF
210 220 230 240 250
LIGHSLGCLH VLHFLLRQPQ SWKDHFIDGF ISLGAPWGGS IKPMRILASG
260 270 280 290 300
DNQGIPIMSN IKLREEQRIT TTSPWMFPAH HVWPEDHVFI STPNFNYTGQ
310 320 330 340 350
DFERFFADLH FEEGWHMFLQ SRDLLAGLPA PGVEVYCLYG VGMPTAHTYI
360 370 380 390 400
YDHNFPYKDP VAALYEDGDD TVATRSTELC GQVQGRQSQG VHLLRMNGTD
410 420 430 440
HLNMVFSNKT LEHINAILLG AYPHGTPKSP TASLGPPPTE
Length:440
Mass (Da):49,727
Last modified:November 1, 1990 - v1
Checksum:i65E39212168A8885
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54096 mRNA. Translation: CAA38030.1.
PIRiS11214. XXRTN.
UniGeneiRn.10481.

Genome annotation databases

UCSCiRGD:2993. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54096 mRNA. Translation: CAA38030.1.
PIRiS11214. XXRTN.
UniGeneiRn.10481.

3D structure databases

ProteinModelPortaliP18424.
SMRiP18424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP18424. 1 interactor.
STRINGi10116.ENSRNOP00000026583.

Protein family/group databases

ESTHERiratno-lcat. PC-sterol_acyltransferase.

Proteomic databases

PaxDbiP18424.
PRIDEiP18424.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2993. rat.

Organism-specific databases

RGDi2993. Lcat.

Phylogenomic databases

eggNOGiKOG2369. Eukaryota.
ENOG410Y9CF. LUCA.
HOGENOMiHOG000238654.
HOVERGENiHBG017055.
InParanoidiP18424.
PhylomeDBiP18424.

Miscellaneous databases

PROiP18424.

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_RAT
AccessioniPrimary (citable) accession number: P18424
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.