LMPD Database

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LMP000308

UniProt Annotations

Entry Information
Gene Nameprotein kinase C, gamma
Protein EntryKPCG_HUMAN
UniProt IDP05129
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P05129-1; Sequence=Displayed; Name=2; IsoId=P05129-2; Sequence=VSP_056467, VSP_056468, VSP_056469; Note=No experimental confirmation available.;
Catalytic ActivityATP + a protein = ADP + a phosphoprotein.
CofactorName=Ca(2+); Xref=ChEBI
DiseaseSpinocerebellar ataxia 14 (SCA14) [MIM
Enzyme RegulationClassical (or conventional) PKCs (PRKCA, PRKCB and PRKCG) are activated by calcium and diacylglycerol (DAG) in the presence of phosphatidylserine. Three specific sites; Thr-514 (activation loop of the kinase domain), Thr-655 (turn motif) and Thr-674 (hydrophobic region), need to be phosphorylated for its full activation.
FunctionCalcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress (By similarity). Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage.
PtmAutophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4.
PtmUbiquitinated.
SimilarityBelongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
SimilarityContains 1 AGC-kinase C-terminal domain.
SimilarityContains 1 C2 domain. {ECO
SimilarityContains 1 protein kinase domain.
SimilarityContains 2 phorbol-ester/DAG-type zinc fingers.
Subcellular LocationCytoplasm . Cytoplasm, perinuclear region {ECO
SubunitInteracts with GRIA4 (By similarity). Interacts with CDCP1. Interacts with TP53INP1 and p53/TP53. {ECO
Tissue SpecificityExpressed in Purkinje cells of the cerebellar cortex.
Web ResourceName=Mutations of the PRKCG gene; Note=Retina International's Scientific Newsletter; URL="http://www.retina-international.org/files/sci-news/prkcgmut.htm";