AlphaFold predicted structure
LPL · P06858
Mean pLDDT
91.1/ 100
Very high
475 residues
Confidence breakdown
- Very high(≥ 90)81%
- Confident(70–90)7%
- Low(50–70)9%
- Very low(< 50)3%
Open interactive 3D viewer
AlphaFold (Jumper et al., 2021) · CC BY 4.0
LPL
Chr 8p21.3lipoprotein lipase
- MANE:
- ENST00000650287.1
Annotations refreshed 1 month ago.
Predicted protein structure
Clinical relevance (Genomics England PanelApp)
Diagnostic Grade (Green)
Familial chylomicronaemia syndrome (FCS)
BOTH monoallelic and biallelic, autosomal or pseudoautosomalLikely inborn error of metabolism
BOTH monoallelic and biallelic, autosomal or pseudoautosomalSevere hypertriglyceridaemia
BOTH monoallelic and biallelic, autosomal or pseudoautosomalUndiagnosed metabolic disorders
BOTH monoallelic and biallelic, autosomal or pseudoautosomalChildhood onset dystonia, chorea or related movement disorder
Familial hypercholesterolaemia
Neonatal diabetes
BIALLELIC, autosomal or pseudoautosomal
Disease associations (Open Targets)
familial lipoprotein lipase deficiency
0.88Hyperlipoproteinemia type 1
0.81Combined hyperlipidemia
0.77coronary artery disorder
0.65metabolic syndrome
0.60type 2 diabetes mellitus
0.59myocardial infarction
0.58Hypercholesterolemia
0.58metabolic disease
0.58familial hyperlipidemia
0.57
Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.
Protein function (UniProt)
Lipoprotein lipase
Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:11342582, PubMed:27578112, PubMed:8675619). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (PubMed:12032167, PubMed:7592706). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:11342582, PubMed:27811232)
Diseases associated with LPL
Curated MONDO disease pages that list LPL among their top associated genes.