Acid sphingomyelinase possesses a domain homologous to its activator proteins: saposins B and D.
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.
Ponting
C P
CP
Department of Biochemistry, University of Oxford, United Kingdom.
D000595:Amino Acid Sequence; D000818:Animals; D004748:Entamoeba histolytica / Q000201:enzymology; D006023:Glycoproteins / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D049231:Saposins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D049128:Sphingolipid Activator Proteins; D013108:Sphingomyelin Phosphodiesterase / Q000737:chemistry*
D006023:Glycoproteins; C483345:PSAP protein, human; D049231:Saposins; D049128:Sphingolipid Activator Proteins; D013108:Sphingomyelin Phosphodiesterase