Neutral Sphingomyelinase (NSMASE)

SMPD2; N-SMase; ISC1; Neutral Sphingomyelin Phosphodiesterase; Sphingomyelin Phosphodiesterase 2,Neutral Membrane; Lyso-platelet-activating factor-phospholipase C

SPN	T726
HGNC	11121
MGI	1278330
PubMed	20378533
RGD	619753
UniProt	O60906
Wiki	SMPD2

SMPD2 isa protein which was initially identified as a sphingomyelinase based on sequence similarity between bacterial sphingomyelinases and a yeast protein. Subsequent studies showed that its biological function is less likely to be as a sphingomyelinase and instead as a lysophospholipase.

Neutral sphingomyelinase (N-SMase) activity was first described in fibroblasts from patients with Niemann-Pick disease – a lysosomal storage disease characterized by deficiencies in acid SMase . Subsequent study found that this enzyme was the product of a distinct gene, had an optimum pH of 7.4, was dependent on Mg2+ ions for activity, and was particularly enriched in brain .

Reference

"Cloned mammalian neutral sphingomyelinase: functions in sphingolipid signaling?"
Proc. Natl. Acad. Sci. U.S.A. 95:3638-3643(1998) [PubMed] [Europe PMC] [Abstract]

"The DNA sequence and analysis of human chromosome 6."
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Function of the cloned putative neutral sphingomyelinase as lyso-platelet activating factor-phospholipase C."
J. Biol. Chem. 274:38131-38139(1999) [PubMed] [Europe PMC] [Abstract]