GPIHBP1
Domain
The N-terminal acidic region is intrinsically disordered (PubMed:26725083). This region contributes to LPL binding, stabilizes LPL and protects LPL against loss of activity (PubMed:26725083, PubMed:27929370).
Function
Mediates the transport of lipoprotein lipase LPL from the basolateral to the apical surface of endothelial cells in capillaries (By similarity). Anchors LPL on the surface of endothelial cells in the lumen of blood capillaries (By similarity). Protects LPL against loss of activity, and against ANGPTL4-mediated unfolding (PubMed:27929370, PubMed:29899144). Thereby, plays an important role in lipolytic processing of chylomicrons by LPL, triglyceride metabolism and lipid homeostasis (PubMed:19304573, PubMed:21314738). Binds chylomicrons and phospholipid particles that contain APOA5 (PubMed:17997385, PubMed:19304573). Binds high-density lipoprotein (HDL) and plays a role in the uptake of lipids from HDL (By similarity).
Involvement in disease
Hyperlipoproteinemia 1D
HLPP1D
An autosomal recessive disorder characterized by hyperlipoproteinemia, decreased plasma LPL levels in some patients, high plasma triglyceride levels, and refractory fasting chylomicronemia.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
Glycosylation of Asn-78 is critical for cell surface localization.
Sulfation of a Tyr in the N-terminal acidic region increases the affinity for LPL.
Cellular localization
- Apical cell membrane
- Lipid-anchor
- GPI-anchor
- Basolateral cell membrane
- Lipid-anchor
- GPI-anchor
- Cell membrane
- Lipid-anchor
- GPI-anchor
Alternative names
HBP1, GPIHBP1, Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1, GPI-HBP1, GPI-anchored HDL-binding protein 1, High density lipoprotein-binding protein 1