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Proteins with EGF-like domains often consist of more than 1,000 amino acids, have multiple copies of the EGF-like domain, and contain additional domains known to be involved in specific protein-protein interactions. The predicted partial LRP4 protein contains 2 EGF-like domains, a calcium binding-type EGF-like domain, 3 LDL receptor-type EGF-like domains, 4 YWTD spacer regions, a transmembrane domain, a cytoplasmic NPXY motif, which is required for clustering and internalization of LDL receptors, and a cytoplasmic tSXV motif, which anchors proteins with a PDZ domain. The sequence and domain organization of LRP4 shows significant similarities to those of members of the LDL receptor family. Northern blot analysis detected rat Megf7 expression in several regions of the brain.
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