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InterPro: IPR017766 Sphingomyelinase C/phospholipase C

Protein matchesHelp
UniProtKB
Matches:
162 proteins
AccessionHelp IPR017766 Sphingomyelinase/phospholipase
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR005135 Endonuclease/exonuclease/phosphatase
GO Term annotationHelp
Function GO:0008081 phosphoric diester hydrolase activity
Component GO:0005576 extracellular region
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This entry represents the proteins sphingomyelinase C (EC:3.1.4.12) and phospholipase C (EC:3.1.4.3). Sphingomyelinase (also known as sphingomyelin phosphodiesterase) is a hydrolase enzyme involved in sphingolipid metabolism, breaking down sphingomyelin to phosphocholine and ceramide [1]. However, some of these enzymes act as haemolysins, virulence factors that promotes intracellular proliferation by mediating the disruption of the phagocytic vacuole and the release of bacteria into the host cell cytosol. It may act in concert with the phospholipases PlcA and PlcB and the hemolysin Hly to mediate efficient escape from the vacuole [2]. Phospholipase C is a bacterial haemolysin, which are exotoxins that attack blood cell membranes and cause cell rupture. Beta-haemolysin is a phospholipase C with specific activity toward sphingomyelins, and has a high specificity for sphingomyelin [3].

Structural linksHelp
SCOP: d.151.1.3
Database linksHelp
Enzyme: EC:3.1.4

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR017766 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P11889 Sphingomyelinase C

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Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR017766 Sphingomyelinase C/phospholipase C
IPR005135 Endonuclease/exonuclease/phosphatase
PDB Chain
ModBase
SCOP Domain

PublicationsHelp
1. Katerov VE, Golubkov VI, Totolian AA, Shalen K, Ensen L, Mikula I, Smola I.
[The cloning and expression of the gene for Staphylococcus aureus beta-hemolysin]
Zh. Mikrobiol. Epidemiol. Immunobiol. 28-33 1994 [PubMed: 7941863]
2. Montes LR, Lopez DJ, Sot J, Bagatolli LA, Stonehouse MJ, Vasil ML, Wu BX, Hannun YA, Goni FM, Alonso A.
Ceramide-enriched membrane domains in red blood cells and the mechanism of sphingomyelinase-induced hot-cold hemolysis.
Biochemistry 47 11222-30 2008 [PubMed: 18826261]
http://dx.doi.org/10.1021/bi801139z
3. Orgun NN, Way SS.
A critical role for phospholipase C in protective immunity conferred by listeriolysin O-deficient Listeria monocytogenes.
Microb. Pathog. 44 159-63 2008 [PubMed: 17888620]
http://dx.doi.org/10.1016/j.micpath.2007.08.002

Additional ReadingHelp
Openshaw AE, Race PR, Monzo HJ, Vazquez-Boland JA, Banfield MJ.
Crystal structure of SmcL, a bacterial neutral sphingomyelinase C from Listeria.
J. Biol. Chem. 280 2005 35011-7 [PubMed: 16093240]
http://dx.doi.org/10.1074/jbc.M506800200
Segers RP, van der Drift A, de Nijs A, Corcione P, van der Zeijst BA, Gaastra W.
Molecular analysis of a sphingomyelinase C gene from Leptospira interrogans serovar hardjo.
Infect. Immun. 58 1990 2177-85 [PubMed: 2163985]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=2163985
Ago H, Oda M, Takahashi M, Tsuge H, Ochi S, Katunuma N, Miyano M, Sakurai J.
Structural basis of the sphingomyelin phosphodiesterase activity in neutral sphingomyelinase from Bacillus cereus.
J. Biol. Chem. 281 2006 16157-67 [PubMed: 16595670]
http://dx.doi.org/10.1074/jbc.M601089200
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InterPro 23.1