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VLDLR

Binds VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Binding to Reelin induces tyrosine phosphorylation of Dab1 and modulation of Tau phosphorylation (By similarity).
Protein class

Disease related genes, Human disease related genes

Predicted location

Intracellular, Membrane (different isoforms)

Single cell type specificity

Cell type enhanced (Cone photoreceptor cells, Cardiomyocytes, Oligodendrocytes)

Immune cell specificity

Immune cell enriched (eosinophil)

Cell line specificity

Cell line enhanced (BEWO, JURKAT, THP-1)

Interaction

Homooligomer (PubMed:30873003). Binds to the extracellular matrix protein Reelin/RELN (PubMed:30873003). Interacts with LRP8 (PubMed:30873003). Interacts with LDLRAP1 (By similarity). Interacts with SNX17 (By similarity). Interacts with DAB1. Interacts with PCSK9. Interacts with PAFAH1B3 and PAFAH1B2, the catalytic complex of (PAF-AH (I)) heterotetrameric enzyme; these interactions may modulate the Reelin pathway (PubMed:17330141). Interacts with STX5; this interaction mediates VLDLR translocation from the endoplasmic reticulum to the plasma membrane (PubMed:23701949). Interacts with CLU (PubMed:24381170). (Microbial infection) Interacts with protein VP1 of the minor-group human rhinoviruses (HRVs) through the second and third LDL-receptor class A domains. (Microbial infection) Interacts with Semliki Forest virus E2-E1 heterodimer; this interaction mediates viral entry to host cell.

Molecular function

Receptor

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For Research Use Only. Not For Clinical Use.

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