Signal peptide(a) |
Y |
Secretome P(b) |
0.781 |
Function |
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. . |
GO - Molecular function |
- apolipoprotein binding : ISO:MGI
- heparin binding : ISS:UniProtKB
- lipoprotein lipase activity : IDA:MGI
- signaling receptor binding : ISO:MGI
- triglyceride binding : ISO:MGI
- triglyceride lipase activity : IDA:BHF-UCL
|
GO - Biological process |
- cholesterol homeostasis : ISO:MGI
- fatty acid biosynthetic process : ISO:MGI
- lipid catabolic process : ISO:MGI
- low-density lipoprotein particle mediated signaling : ISO:MGI
- positive regulation of chemokine secretion : ISO:MGI
- positive regulation of cholesterol storage : ISO:MGI
- positive regulation of macrophage derived foam cell differentiation : IGI:BHF-UCL
- positive regulation of sequestering of triglyceride : ISO:MGI
- response to cold : IEA:Ensembl
- response to drug : IEA:Ensembl
- triglyceride biosynthetic process : ISS:UniProtKB
- triglyceride catabolic process : IDA:BHF-UCL
- triglyceride homeostasis : ISO:MGI
- very-low-density lipoprotein particle remodeling : ISO:MGI
|