background:
Low density lipoprotein receptor-related protein (also known as low density LRP, LRP1, alpha-2-macroglobulin receptor or Apolipoprotein E receptor) is an endocytotic receptor that is involved both in endocytosis and in phagocytosis of apoptotic cells. It is required for early embryonic development, is involved in cellular lipid homeostasis, and may play a role in APP metabolism, kinase-dependent intracellular signalling, neuronal calcium signalling and neurotransmission. Low density LRP also plays a role in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha-2-macroglobulin), and is involved in the local metabolism of complexes of plasminogen activators and their endogenous ligands. Low density LPR is postulated to be one of the major players in host resistance to HIV. The precursor low density LRP molecule is cleaved post-translationally to form a 85 kDa membrane-spanning subunit (LRP-85) and a 515 kDa large extracellular domain (LRP-515), which remains non-covalently associated with LRP-85. Following cleavage, the intracellular domain (LPRICD) is present in both the cytoplasm and the nucleus.
Function:
Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. 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. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission.
Functions as a receptor for Pseudomonas aeruginosa exotoxin A.
Subcellular Location:
Cell membrane. Membrane, coated pit and Cytoplasm. Nucleus. After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus.
Tissue Specificity:
Most abundant in liver, brain and lung.
Post-translational modifications:
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.
Similarity:
Belongs to the LDLR family.
Contains 22 EGF-like domains.
Contains 31 LDL-receptor class A domains.
Contains 34 LDL-receptor class B repeats.
Database links:
Entrez Gene: 4035 Human
Entrez Gene: 16971 Mouse
Entrez Gene: 100009547 Rabbit
Entrez Gene: 299858 Rat
Omim: 107770 Human
SwissProt: Q07954 Human
SwissProt: Q91ZX7 Mouse
Unigene: 162757 Human
Unigene: 271854 Mouse
Unigene: 22436 Rat
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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