Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells (PubMed:11907044, PubMed:12713657). Required for early embryonic development (By similarity). Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. Acts as an LRPAP1 alpha-2-macroglobulin receptor (PubMed:26142438, PubMed:1702392). Acts as TAU/MAPT receptor and controls the endocytosis of TAU/MAPT as well as its subsequent spread (PubMed:32296178). May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission (PubMed:12888553). (Microbial infection) Functions as a receptor for Pseudomonas aeruginosa exotoxin A. Heterodimer of an 85-kDa membrane-bound carboxyl subunit and a non-covalently attached 515-kDa N-terminal subunit. Intracellular domain interacts with MAFB (By similarity). Found in a complex with PID1/PCLI1, LRP1 and CUBNI (PubMed:17124247). Interacts with SNX17, PID1/PCLI1, PDGF and CUBN. The intracellular domain interacts with SHC1, GULP1 and DAB1. Can weakly interact (via NPXY motif) with DAB2 (via PID domain); the interaction is enhanced by tyrosine phosphorylation of the NPXY motif. Interacts with MDK; promotes neuronal survival (PubMed:10772929). Interacts with LRPAP1; this interaction is followed by rapid internalization (PubMed:15053742, PubMed:32296178, PubMed:16938309). Interacts with uPA/PLAU and PAI1/SERPINE1, either individually or in complex with each other, leading to rapid endocytosis; this interaction is abolished in the presence of LRPAP1/RAP (PubMed:15053742). Also interacts with tPA/PLAT alone or in complex with SERPINE1 (PubMed:15053742). Interacts with the urokinase receptor PLAUR; this interaction leads to PLAUR internalization and is impaired in the presence of SORL1 (PubMed:14764453). Interacts with PDGFB (PubMed:15053742). Interacts with TAU/MAPT, leading to endocytosis; this interaction is reduced in the presence of LRPAP1/RAP (PubMed:32296178). (Microbial infection) Interacts with bacterial exotoxins. (Microbial infection) Interacts with Rift valley fever virus (RVFV) glycoprotein N; this interaction facilitates virus entry. After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus. Localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation. Most abundant in liver, brain and lung. Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515 kDa large extracellular domain (LRP-515) that remains non-covalently associated. Gamma-secretase-dependent cleavage of LRP-85 releases the intracellular domain from the membrane. The N-terminus is blocked. Phosphorylated on serine and threonine residues. Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1. The disease is caused by variants affecting the gene represented in this entry. Belongs to the LDLR family.