Phospholipase C, phosphatidylinositol-specific, Y domain
IPR001711
Definition
Phosphatidylinositol-specific phospholipase C ([ec:3.1.4.11]), an eukaryotic intracellular enzyme, plays an important role in signal transduction processes PMID:1849017 (see [interpro:IPR001192]). It catalyzes the hydrolysis of 1-phosphatidyl-D-myo-inositol-3,4,5-triphosphate 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 [[cite:PMID:1419362], [cite:PMID:1319994], [cite:PMID:1335185]]. 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' (see [interpro:IPR000909]) 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 gamma 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 [interpro:IPR000008]) possibly involved in Ca-dependent membrane attachment.
15 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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