Sphingomyelin phosphodiesterase 1

Sphingomyelin phosphodiesterase 1, acid lysosomal

Identifiers

SMPD1; ASM; ASMASE; NPD

External IDs

OMIM: 607608 MGI: 98325 HomoloGene: 457 GeneCards: SMPD1 Gene

3.1.4.12

Gene Ontology
Molecular function	• sphingomyelin phosphodiesterase activity • hydrolase activity, acting on glycosyl bonds
Cellular component	• extracellular space • lysosome • lamellar body
Biological process	• sphingomyelin metabolic process • sphingomyelin catabolic process • signal transduction • nervous system development • metabolic process • cell death • response to cocaine • response to drug • positive regulation of apoptosis • ceramide biosynthetic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
6.41 – 6.42 Mb

Chr 7:
112.7 – 112.71 Mb

PubMed search

[1]

[2]

Sphingomyelin phosphodiesterase 1 also known as acid sphingomyelinase is an enzyme that in humans is encoded by the SMPD1 gene.

Sphingomyelin phosphodiesterase 1 belongs to the sphingomyelin phosphodiesterase family.^[1] Defects in SMPD1 gene cause Niemann-Pick disease, SMPD1-associated.

References

^ "Entrez Gene: SMPD1 sphingomyelin phosphodiesterase 1, acid lysosomal (acid sphingomyelinase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6609.

Stoffel W (2000). "Functional analysis of acid and neutral sphingomyelinases in vitro and in vivo.". Chem. Phys. Lipids 102 (1–2): 107–21. doi:10.1016/S0009-3084(99)00079-1. PMID 11001565.
Newrzella D, Stoffel W (1993). "Molecular cloning of the acid sphingomyelinase of the mouse and the organization and complete nucleotide sequence of the gene". Biol. Chem. Hoppe-Seyler 373 (12): 1233–8. PMID 1292508.
Takahashi T, Desnick RJ, Takada G, Schuchman EH (1993). "Identification of a missense mutation (S436R) in the acid sphingomyelinase gene from a Japanese patient with type B Niemann-Pick disease". Hum. Mutat. 1 (1): 70–1. doi:10.1002/humu.1380010111. PMID 1301192.
Levran O, Desnick RJ, Schuchman EH (1992). "Identification and expression of a common missense mutation (L302P) in the acid sphingomyelinase gene of Ashkenazi Jewish type A Niemann-Pick disease patients". Blood 80 (8): 2081–7. PMID 1391960.
Takahashi T, Suchi M, Desnick RJ et al. (1992). "Identification and expression of five mutations in the human acid sphingomyelinase gene causing types A and B Niemann-Pick disease. Molecular evidence for genetic heterogeneity in the neuronopathic and non-neuronopathic forms". J. Biol. Chem. 267 (18): 12552–8. PMID 1618760.
Schuchman EH, Levran O, Suchi M, Desnick RJ (1991). "An MspI polymorphism in the human acid sphingomyelinase gene (SMPD1)". Nucleic Acids Res. 19 (11): 3160. doi:10.1093/nar/19.11.3160. PMC 328296. PMID 1711683. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=328296.
Ferlinz K, Hurwitz R, Sandhoff K (1991). "Molecular basis of acid sphingomyelinase deficiency in a patient with Niemann-Pick disease type A". Biochem. Biophys. Res. Commun. 179 (3): 1187–91. doi:10.1016/0006-291X(91)91697-B. PMID 1718266.
Schuchman EH, Levran O, Pereira LV, Desnick RJ (1992). "Structural organization and complete nucleotide sequence of the gene encoding human acid sphingomyelinase (SMPD1)". Genomics 12 (2): 197–205. doi:10.1016/0888-7543(92)90366-Z. PMID 1740330.
Schuchman EH, Suchi M, Takahashi T et al. (1991). "Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs". J. Biol. Chem. 266 (13): 8531–9. PMID 1840600.
Levran O, Desnick RJ, Schuchman EH (1991). "Niemann-Pick type B disease. Identification of a single codon deletion in the acid sphingomyelinase gene and genotype/phenotype correlations in type A and B patients". J. Clin. Invest. 88 (3): 806–10. doi:10.1172/JCI115380. PMC 295465. PMID 1885770. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=295465.
da Veiga Pereira L (1991). "Regional assignment of the human acid sphingomyelinase gene (SMPD1) by PCR analysis of somatic cell hybrids and in situ hybridization to 11p15.1----p15.4". Genomics 9 (2): 229–34. doi:10.1016/0888-7543(91)90246-B. PMID 2004772.
Levran O, Desnick RJ, Schuchman EH (1991). "Niemann-Pick disease: a frequent missense mutation in the acid sphingomyelinase gene of Ashkenazi Jewish type A and B patients". Proc. Natl. Acad. Sci. U.S.A. 88 (9): 3748–52. doi:10.1073/pnas.88.9.3748. PMC 51530. PMID 2023926. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=51530.
Quintern LE, Schuchman EH, Levran O et al. (1989). "Isolation of cDNA clones encoding human acid sphingomyelinase: occurrence of alternatively processed transcripts". EMBO J. 8 (9): 2469–73. PMC 401234. PMID 2555181. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=401234.
Horinouchi K, Erlich S, Perl DP et al. (1995). "Acid sphingomyelinase deficient mice: a model of types A and B Niemann-Pick disease". Nat. Genet. 10 (3): 288–93. doi:10.1038/ng0795-288. PMID 7670466.
Sperl W, Bart G, Vanier MT et al. (1994). "A family with visceral course of Niemann-Pick disease, macular halo syndrome and low sphingomyelin degradation rate". J. Inherit. Metab. Dis. 17 (1): 93–103. doi:10.1007/BF00735404. PMID 8051942.
Ida H, Rennert OM, Eto Y, Chan WY (1993). "Cloning of a human acid sphingomyelinase cDNA with a new mutation that renders the enzyme inactive". J. Biochem. 114 (1): 15–20. PMID 8407868.
Ida H, Rennert OM, Maekawa K, Eto Y (1996). "Identification of three novel mutations in the acid sphinogomyelinase gene of Japanese patients with Niemann-Pick disease type A and B". Hum. Mutat. 7 (1): 65–7. doi:10.1002/(SICI)1098-1004(1996)7:1<65::AID-HUMU10>3.0.CO;2-Q. PMID 8664904.
Schuchman EH (1996). "Two new mutations in the acid sphingomyelinase gene causing type a Niemann-pick disease: N389T and R441X". Hum. Mutat. 6 (4): 352–4. doi:10.1002/humu.1380060412. PMID 8680412.
Takahashi T, Suchi M, Sato W et al. (1996). "Identification and expression of a missense mutation (Y446C) in the acid sphingomyelinase gene from a Japanese patient with type A Niemann-Pick disease". Tohoku J. Exp. Med. 177 (2): 117–23. doi:10.1620/tjem.177.117. PMID 8693491.
Ferlinz K, Hurwitz R, Moczall H et al. (1997). "Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis". Eur. J. Biochem. 243 (1–2): 511–7. doi:10.1111/j.1432-1033.1997.511_1a.x. PMID 9030779.

External Links

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic ester hydrolases

Cholinesterase (Acetylcholinesterase, Butyrylcholinesterase) · Pectinesterase · 6-phosphogluconolactonase · PAF acetylhydrolase

Lipase (Bile salt-dependent, Gastric/Lingual, Pancreatic, Lysosomal, Hormone-sensitive, Endothelial, Hepatic, Lipoprotein, Monoacylglycerol, Diacylglycerol)

Phospholipase (A1, A2, B)

3.1.2: Thioesterase

Palmitoyl protein thioesterase · Ubiquitin carboxy-terminal hydrolase L1

3.1.3: Phosphatase

Alkaline phosphatase (ALPI, ALPL, ALPP) · Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases · Nucleotidase · Glucose 6-phosphatase · Fructose 1,6-bisphosphatase · Calcineurin · Phosphoprotein phosphatase (PP2A) · OCRL · Pyruvate dehydrogenase phosphatase · Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase · PTEN · Phytase · Inositol-phosphate phosphatase (IMPA1)

Phosphoprotein phosphatase: Protein tyrosine phosphatase · Protein serine/threonine phosphatase · Dual-specificity phosphatase

3.1.4: Phosphodiesterase

Autotaxin · Phospholipase (C, D) · Sphingomyelin phosphodiesterase (1) · PDE1 · PDE2 · PDE3 · PDE4A/PDE4B · PDE5 · Lecithinase (Clostridium perfringens alpha toxin) · Cyclic nucleotide phosphodiesterase

3.1.6: Sulfatase

arylsulfatase (Arylsulfatase A, Arylsulfatase B, Arylsulfatase E, Steroid sulfatase) · Galactosamine-6 sulfatase · Iduronate-2-sulfatase · N-acetylglucosamine-6-sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I · Deoxyribonuclease II · Deoxyribonuclease IV · Restriction enzyme · UvrABC endonuclease

Endoribonuclease	RNase III · RNase H (1, 2A, 2B, 2C) · RNase P · RNase A (1, 2, 3, 4/5) · RNase T1 · RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 · Micrococcal nuclease

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

Metabolism: lipid metabolism · glycolipid enzymes

Sphingolipid

To glycosphingolipid	Glycosyltransferase · Sulfotransferase

To ceramide	From ganglioside: Beta-galactosidase · Hexosaminidase A · Neuraminidase · Glucocerebrosidase From globoside: Hexosaminidase B · Alpha-galactosidase · Beta-galactosidase · Glucocerebrosidase From sphingomyelin: Sphingomyelin phosphodiesterase (Sphingomyelin phosphodiesterase 1) From sulfatide: Arylsulfatase A · Galactosylceramidase

To sphingosine	Ceramidase (ACER1, ACER2, ACER3, ASAH1, ASAH2, ASAH2B, ASAH2C)

Other	Sphingosine kinase

NCL

Palmitoyl protein thioesterase · Tripeptidyl peptidase I · CLN3 · CLN5 · CLN6 · CLN8

Ceramide synthesis

Serine C-palmitoyltransferase (SPTLC1) · Ceramide glucosyltransferase (UGCG)

M: MET

mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m

k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon

m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)

Sphingomyelin phosphodiesterase 1

References

Further reading

External Links