Enables calcium,diacylglycerol-dependent serine/threonine kinase activity. Involved in several processes, including long-term synaptic potentiation; response to angiotensin; and response to psychosocial stress. Located in several cellular components, including dendrite; perinuclear region of cytoplasm; and synaptic membrane. Is active in postsynaptic cytosol. Human ortholog(s) of this gene implicated in spinocerebellar ataxia type 14. Orthologous to human PRKCG (protein kinase C gamma); PARTICIPATES IN eicosanoid signaling pathway; endothelin signaling pathway; insulin signaling pathway; INTERACTS WITH (+)-pilocarpine; (S)-alpha-methyl-4-carboxyphenylglycine; 2-amino-5-phosphonopentanoic acid.
MGC105487; PKC; PKC-gamma; PKCI; Prkc; Prkcc; protein kinase C gamma type; Protein kinase C type I (gamma type); Protein kinase C, type I (gamma type); RATPKCI
Celecoxib inhibits the reaction [deoxynivalenol affects the localization of PRKCG protein] and Ro 31-8220 inhibits the reaction [deoxynivalenol affects the localization of PRKCG protein]
[Tetradecanoylphorbol Acetate co-treated with Calcium] inhibits the reaction [Zinc promotes the reaction [OPRM1 protein binds to PRKCG protein]] more ...
[Tetradecanoylphorbol Acetate co-treated with Calcium] inhibits the reaction [Zinc promotes the reaction [OPRM1 protein binds to PRKCG protein]] more ...
[Tetradecanoylphorbol Acetate co-treated with Calcium] inhibits the reaction [Zinc promotes the reaction [OPRM1 protein binds to PRKCG protein]] more ...
Protein kinase C gamma associates directly with the GluR4 alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor subunit. Effect on receptor phosphorylation.
Exposure to chronic psychosocial stress and corticosterone in the rat: effects on spatial discrimination learning and hippocampal protein kinase Cgamma immunoreactivity.
Selective changes in protein kinase C isoforms and phosphorylation of endogenous substrate proteins in rat cerebral cortex during pre- and postnatal ethanol exposure.
Protein kinase C-gamma and calcium/calmodulin-dependent protein kinase II-alpha are persistently translocated to cell membranes of the rat brain during and after middle cerebral artery occlusion.