Prkcg
entrez
18752
canonical
uniprot
P63318
canonical
ensembl
ENSMUSG00000078816
resolver
ensp
ENSMUSP00000097874
resolver
ensp
ENSMUSP00000131351
resolver
enst
ENSMUST00000100301
resolver
enst
ENSMUST00000172109
resolver
genesymbol
Prkcg
resolver
genesymbol_syn
Pkcc
resolver
genesymbol_syn
Pkcg
resolver
genesymbol_syn
Prkcc
resolver
uniprot
F6ZB24
resolver
uniprot
P05697
resolver
uniprot
Q2NKI4
resolver
uniprot
Q3UN66
resolver
uniprot_entry
F6ZB24_MOUSE
resolver
uniprot_entry
KPCG_MOUSE
resolver
uniprot_entry
Q2NKI4_MOUSE
resolver
uniprot_entry
Q3UN66_MOUSE
resolver
uniprot_sec
P05697
resolver
activity_regulation
ACTIVITY REGULATION: Classical (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.
uniprot
proteins
amino_acid_sequence
MAGLGPGGGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTSDEIHITVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTKTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDSKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGSTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIAPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM
uniprot
proteins
ec_number
2.7.11.13
uniprot
proteins
function
FUNCTION: Calcium-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 contribute 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. Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (PubMed:23185022). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (By similarity). Acts as a regulator of dopamine signaling by mediating constitutive phosphorylation of dopamine receptor DRD1, inhibiting G protein-coupled receptor signaling (By similarity). {ECO:0000250|UniProtKB:P05129, ECO:0000269|PubMed:11246146, ECO:0000269|PubMed:11278552, ECO:0000269|PubMed:11356858, ECO:0000269|PubMed:11731061, ECO:0000269|PubMed:17904530, ECO:0000269|PubMed:23185022, ECO:0000269|PubMed:8269509, ECO:0000269|PubMed:9323205}.
uniprot
proteins
mass_dalton
78358
uniprot
proteins
post_translational_modification
PTM: Autophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4. {ECO:0000269|PubMed:17904530}.; PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P05129}.
uniprot
proteins
protein_family
AGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
PKC subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
11246146
uniprot
proteins
pubmed
11278552
uniprot
proteins
pubmed
11356858
uniprot
proteins
pubmed
11731061
uniprot
proteins
pubmed
17114649
uniprot
proteins
pubmed
17904530
uniprot
proteins
pubmed
18473171
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23185022
uniprot
proteins
pubmed
8269509
uniprot
proteins
pubmed
8428669
uniprot
proteins
pubmed
8548809
uniprot
proteins
pubmed
9323205
uniprot
proteins
sequence_length
697
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17904530}. Cytoplasm, perinuclear region {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:17904530, ECO:0000269|PubMed:18473171}; Peripheral membrane protein. Synapse, synaptosome {ECO:0000269|PubMed:18473171}. Cell projection, dendrite {ECO:0000250|UniProtKB:P63319}. Note=Translocates to synaptic membranes on stimulation. {ECO:0000269|PubMed:18473171}.
uniprot
proteins