PROSITE documentation PDOC50007 [for PROSITE entry PS50008]

Phosphatidylinositol-specific phospholipase C profiles





Description

Phosphatidylinositol-specific phospholipase C (EC 3.1.4.11), an eukaryotic intracellular enzyme, plays an important role in signal transduction processes [1]. It catalyzes the hydrolysis of 1-phosphatidyl-D-myo-inositol-4,5-diphosphate into the second messenger molecules diacylglycerol and inositol-1,4,5-triphosphate. This catalytic process is tightly regulated by reversible phosphorylation and binding of regulatory proteins [2,3,4].

In mammals, there are at least 6 different isoforms of PI-PLC, they differ in their domain structure, their regulation, and their tissue distribution. Lower eukaryotes also possess multiple isoforms of PI-PLC.

All eukaryotic PI-PLCs contain two regions of homology, sometimes referred to as 'X-box' and 'Y-box'. The order of these two regions is always the same (NH2-X-Y-COOH), but the spacing is variable. In most isoforms, the distance between these two regions is only 50-100 residues but in the γ isoforms one PH domain, two SH2 domains, and one SH3 domain are inserted between the two PLC-specific domains. The two conserved regions have been shown to be important for the catalytic activity. At the C-terminal of the Y-box, there is a C2 domain (see <PDOC00380>) possibly involved in Ca-dependent membrane attachment.

By profile analysis, we could show that sequences with significant similarity to the X-box domain occur also in prokaryotic and trypanosome PI-specific phospholipases C. Apart from this region, the prokaryotic enzymes show no similarity to their eukaryotic counterparts.

We developed two profiles, one covering the X-box, the other the Y-box.

Last update:

July 2003 / Text revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

PIPLC_Y_DOMAIN, PS50008; Phosphatidylinositol-specific phospholipase Y-box domain profile  (MATRIX)

PIPLC_X_DOMAIN, PS50007; Phosphatidylinositol-specific phospholipase X-box domain profile  (MATRIX)


References

1AuthorsMeldrum E., Parker P.J., Carozzi A.
TitleThe PtdIns-PLC superfamily and signal transduction.
SourceBiochim. Biophys. Acta 1092:49-71(1991).
PubMed ID1849017

2AuthorsRhee S.G., Choi K.D.
TitleMultiple forms of phospholipase C isozymes and their activation mechanisms.
SourceAdv. Second Messenger Phosphoprotein Res. 26:35-61(1992).
PubMed ID1419362

3AuthorsRhee S.G., Choi K.D.
TitleRegulation of inositol phospholipid-specific phospholipase C isozymes.
SourceJ. Biol. Chem. 267:12393-12396(1992).
PubMed ID1319994

4AuthorsSternweis P.C., Smrcka A.V.
TitleRegulation of phospholipase C by G proteins.
SourceTrends Biochem. Sci. 17:502-506(1992).
PubMed ID1335185



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)