SMPD1
SMPD1 (sphingomyelin phosphodiesterase 1, also known as ASM or acid sphingomyelinase) is a lysosomal enzyme that converts sphingomyelin to ceramide. It also has phospholipase C activity, and defects in the SMPD1 gene cause Niemann-Pick disease types A and B. Browse Assay Genie's current range of SMPD1 research reagents below, or read on for the biology behind the target.
SMPD1 encodes a lysosomal acid sphingomyelinase. The enzyme catalyses the conversion of sphingomyelin to ceramide, a reaction classified under EC 3.1.4.12. According to the NCBI Gene summary, the encoded protein also has phospholipase C activity, which is reflected in its second EC assignment, EC 3.1.4.3. Because it acts on a major membrane sphingolipid and generates ceramide, SMPD1 is a natural focus for studies of sphingolipid turnover in the lysosome.
The SMPD1 protein belongs to the acid sphingomyelinase family and sits within the HGNC gene group of saposin B type domain containing proteins. UniProt records its subcellular locations as the lysosome, the lipid droplet and the secreted compartment, including the extracellular space. Multiple transcript variants encoding different isoforms have been identified. UniProt also notes that a form of the protein lacks the residues that bind the cofactor Zn(2+) and has no enzyme activity, so isoform-level detail matters when interpreting results. The mouse ortholog is Smpd1, which is the usual starting point for animal studies.
The gene is also known by the alias ASM and was previously named sphingomyelin phosphodiesterase 1, acid lysosomal. Its clinical relevance is well established: defects in the SMPD1 gene are a cause of Niemann-Pick disease type A (NPA) and Niemann-Pick disease type B (NPB). Researchers therefore study SMPD1 in the context of lysosomal storage disease, ceramide generation and sphingomyelin metabolism, alongside related enzymes such as SMPD2 and SMPDL3A.
SMPD1 hydrolyses sphingomyelin to ceramide, making it a central enzyme for studying how membrane sphingolipids are broken down.
Defects in SMPD1 cause Niemann-Pick disease types A and B, so the enzyme is a key subject in lysosomal disease research.
As a lysosomal acid sphingomyelinase, SMPD1 is investigated as a source of ceramide within cells.
Multiple isoforms and locations, including lysosome, lipid droplet and secreted pools, make SMPD1 a useful model for protein trafficking and variant analysis.
SMPD1 is a lysosomal acid sphingomyelinase that converts sphingomyelin to ceramide. The NCBI Gene summary also reports phospholipase C activity for the encoded protein. UniProt lists its locations as the lysosome, lipid droplet and secreted compartment, including the extracellular space.
SMPD1 is also called ASM, for acid sphingomyelinase, and was previously named sphingomyelin phosphodiesterase 1, acid lysosomal. Multiple transcript variants encoding different isoforms have been identified, and UniProt notes that one form lacks Zn(2+)-binding residues and has no enzyme activity.
Yes. Defects in the SMPD1 gene are a cause of Niemann-Pick disease type A and type B. The mouse ortholog is Smpd1. Researchers working across species should check the datasheet of any product for its validated reactivity.
Other sphingomyelinase family members, sphingolipid-metabolism enzymes and lysosomal storage disease targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P17405; product specifications from Assay Genie datasheets.