An N-terminal region of the acid sphingomyelinase sequence (residues 89-165) is shown to be homologous to saposin-type sequences. By analogy with the known functions of saposins, this sphingomyelinase saposin-type domain may possess lipid-binding and/or sphingomyelinase-activator properties. This finding may prove to be important in the understanding of Niemann-Pick disease, which results from sphingomyelinase deficiency.
- Amino Acid Sequence
- Entamoeba histolytica
- Molecular Sequence Data
- Sequence Alignment
- Sequence Homology, Amino Acid
- Sphingolipid Activator Proteins
- Sphingomyelin Phosphodiesterase