Chaperone specifically assisting the folding of beta-propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wnt pathway through chaperoning the coreceptors of the canonical Wnt pathway, LRP5 and LRP6, to the plasma membrane. Essential for specification of embryonic polarity and mesoderm induction.
Belongs to the MESD family.
The chaperone domain provides a folding template for proper folding of the beta-propeller (BP) domains of LRP5/6. The escort domain ensures LRP5/6 safe-trafficking from the ER to the Golgi by preventing premature ligand-binding.