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Protein Science, Vol 3, Issue 2 359-361, Copyright © 1994 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Acid sphingomyelinase possesses a domain homologous to its activator proteins: Saposins B and D

C. P. PONTING
Laboratory of Molecular Biophysics, University of Oxford, Department of Biochemistry, Rex Richards Building, South Parks Road, Oxford OX1 3QU, United Kingdom

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.
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