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Protein Page:
LPL (human)

LPL The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium. Defects in LPL are the cause of lipoprotein lipase deficiency (LPL deficiency); also known as familial chylomicronemia or hyperlipoproteinemia type I. LPL deficiency chylomicronemia is a recessive disorder usually manifesting in childhood. On a normal diet, patients often present with abdominal pain, hepatosplenomegaly, lipemia retinalis, eruptive xanthomata, and massive hypertriglyceridemia, sometimes complicated with acute pancreatitis. Belongs to the AB hydrolase superfamily. Lipase family. Note: This description may include information from UniProtKB.
Protein type: EC; Lipid Metabolism - glycerolipid; Membrane protein, GPI anchor; Phospholipase
Chromosomal Location of Human Ortholog: 8p22
Cellular Component: extracellular region; extracellular space
Molecular Function: apolipoprotein binding; heparin binding; lipoprotein lipase activity; phospholipase activity; protein binding; receptor binding; triacylglycerol lipase activity
Biological Process: cholesterol homeostasis; fatty acid biosynthetic process; lipoprotein metabolic process; phospholipid metabolic process; positive regulation of inflammatory response; response to glucose stimulus; retinoid metabolic process; triacylglycerol catabolic process; triacylglycerol metabolic process
Disease: Hyperlipidemia, Familial Combined; Hyperlipoproteinemia, Type I
Reference #:  P06858 (UniProtKB)
Alt. Names/Synonyms: HDLCQ11; LIPD; LIPL; Lipoprotein lipase; LPL
Gene Symbols: LPL
Molecular weight: 53,162 Da
Basal Isoelectric point: 8.37  Predict pI for various phosphorylation states
Select Structure to View Below


Protein Structure Not Found.

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