Phosphoinositide phospholipase C
| Phosphatidylinositol-specific phospholipase C | |||||||||
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Phospholipase Cδ-1 | |||||||||
| Identifiers | |||||||||
| Symbol | PI-PLC-X | ||||||||
| Pfam | PF00388 | ||||||||
| Pfam clan | CL0384 | ||||||||
| InterPro | IPR000909 | ||||||||
| SMART | PLCXc | ||||||||
| PROSITE | PDOC50007 | ||||||||
| SCOP2 | 1gym / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 118 | ||||||||
| OPM protein | 1djx | ||||||||
| CDD | cd00137 | ||||||||
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| phosphoinositide phospholipase C | |||||||||
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1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2 monomer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 3.1.4.11 | ||||||||
| CAS no. | 37213-51-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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Phosphoinositide phospholipase C (PLC, EC 3.1.4.11, triphosphoinositide phosphodiesterase, phosphoinositidase C, 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase, monophosphatidylinositol phosphodiesterase, phosphatidylinositol phospholipase C, PI-PLC, 1-phosphatidyl-D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase; systematic name 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase) is a family of eukaryotic intracellular enzymes that play an important role in signal transduction processes. These enzymes belong to a larger superfamily of Phospholipase C. Other families of phospholipase C enzymes have been identified in bacteria and trypanosomes. Phospholipases C are phosphodiesterases.
Phospholipase Cs participate in phosphatidylinositol 4,5-bisphosphate (PIP2) metabolism and lipid signaling pathways in a calcium-dependent manner. At present, the family consists of six sub-families comprising a total of 13 separate isoforms that differ in their mode of activation, expression levels, catalytic regulation, cellular localization, membrane binding avidity and tissue distribution. All are capable of catalyzing the hydrolysis of PIP2 into two important second messenger molecules, which go on to alter cell responses such as proliferation, differentiation, apoptosis, cytoskeleton remodeling, vesicular trafficking, ion channel conductance, endocrine function and neurotransmission.