LMPD Database

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LMP006674

UniProt Annotations

Entry Information
Gene Namephospholipase C, delta 3
Protein EntryPLCD3_HUMAN
UniProt IDQ8N3E9
SpeciesHuman
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=105.3 uM for PIP2 ; Vmax=28.5 umol/min/mg enzyme ;
Catalytic Activity1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
CofactorName=Ca(2+); Xref=ChEBI
DomainThe C2 domain is a Ca(2+)-dependent membrane-targeting module.
DomainThe PH domain mediates interaction with the surface membrane by binding to PIP2.
Enzyme RegulationStrongly activated by phosphatidic acid. Inhibited by phosphatidylethanolamine (PtdEtn), phosphatidylcholine (PtdCho), sphingomyelin and phosphatidylserine (PtdSer). {ECO
FunctionHydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow.
InductionDown-regulated by Ca(2+) and cAMP.
SimilarityContains 1 C2 domain. {ECO
SimilarityContains 1 PH domain.
SimilarityContains 1 PI-PLC X-box domain. {ECO
SimilarityContains 1 PI-PLC Y-box domain. {ECO
SimilarityContains 3 EF-hand domains.
Subcellular LocationMembrane; Peripheral membrane protein. Cytoplasm. Cleavage furrow. Note=Localizes at the cleavage furrow during cytokinesis.
Tissue SpecificityPresent in corneal epithelial cells (at protein level).