Prkca
entrez
24680
canonical
uniprot
P05696
canonical
ensembl
ENSRNOG00000003491
resolver
ensembl
ENSRNOG00055029138
resolver
ensembl
ENSRNOG00060013871
resolver
ensembl
ENSRNOG00065019003
resolver
ensp
ENSRNOP00000079110
resolver
ensp
ENSRNOP00055041646
resolver
ensp
ENSRNOP00060018914
resolver
ensp
ENSRNOP00065025598
resolver
enst
ENSRNOT00000100596
resolver
enst
ENSRNOT00055050566
resolver
enst
ENSRNOT00060023763
resolver
enst
ENSRNOT00065032081
resolver
genesymbol
Prkca
resolver
genesymbol_syn
Pkca
resolver
uniprot
A0A8I5ZMR6
resolver
uniprot
B5DFC4
resolver
uniprot_entry
A0A8I5ZMR6_RAT
resolver
uniprot_entry
B5DFC4_RAT
resolver
uniprot_entry
KPCA_RAT
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-497 (activation loop of the kinase domain), Thr-638 (turn motif) and Ser-657 (hydrophobic region), need to be phosphorylated for its full activation.
uniprot
proteins
amino_acid_sequence
MADVYPANDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVTDEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNVELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV
uniprot
proteins
ec_number
2.7.11.13
uniprot
proteins
function
FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascades involving MAPK1/3 (ERK1/2) and RAP1GAP. Depending on the cell type, is involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation. In cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Depending on the cell type, exhibits anti-apoptotic function and protects cells from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, or mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42 (By similarity). Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription (By similarity). Phosphorylates SOCS2 at 'Ser-52' facilitating its ubiquitination and proteasomal degradation (By similarity). Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (By similarity). 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:P17252, ECO:0000250|UniProtKB:P20444, ECO:0000269|PubMed:11076962, ECO:0000269|PubMed:11864993, ECO:0000269|PubMed:15271671, ECO:0000269|PubMed:19176525}.
uniprot
proteins
mass_dalton
76792
uniprot
proteins
mutagenesis
MUTAGEN 195; /note="Y->S: Reduced phosphatidylinositol 4,5-bisphosphate recognition and impaired membrane docking. Loss of phosphatidylinositol 4,5-bisphosphate-binding and strong decrease of membrane docking; when associated with A-209; A-211 and A-245."; /evidence="ECO:0000269|PubMed:19346474"; MUTAGEN 209; /note="K->A: Loss of phosphatidylinositol 4,5-bisphosphate-binding and strong decrease of membrane docking; when associated with S-195; A-211 and A-245."; /evidence="ECO:0000269|PubMed:19346474"; MUTAGEN 211; /note="K->A: Loss of phosphatidylinositol 4,5-bisphosphate-binding and strong decrease of membrane docking; when associated with S-195; A-209 and A-245."; /evidence="ECO:0000269|PubMed:19346474"; MUTAGEN 245; /note="W->A: Reduced phosphatidylinositol 4,5-bisphosphate recognition and impaired membrane docking. Loss of phosphatidylinositol 4,5-bisphosphate-binding and strong decrease of membrane docking; when associated with S-195; A-209 and A-211."; /evidence="ECO:0000269|PubMed:19346474
uniprot
proteins
post_translational_modification
PTM: In response to growth factors, phosphorylated at Thr-631 and Ser-657 by the mTORC2 complex, promoting autophosphorylation and activation of PRKCA. {ECO:0000250|UniProtKB:P17252}.
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
10562545
uniprot
proteins
pubmed
11076962
uniprot
proteins
pubmed
11864993
uniprot
proteins
pubmed
15271671
uniprot
proteins
pubmed
19176525
uniprot
proteins
pubmed
19346474
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
3045562
uniprot
proteins
pubmed
3387228
uniprot
proteins
pubmed
3666147
uniprot
proteins
pubmed
9566962
uniprot
proteins
sequence_length
672
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15271671}. Cell membrane {ECO:0000269|PubMed:15271671, ECO:0000269|PubMed:19346474}; Peripheral membrane protein {ECO:0000305|PubMed:15271671}. Mitochondrion membrane {ECO:0000250|UniProtKB:P17252}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17252}. Nucleus {ECO:0000269|PubMed:15271671}. Note=Translocated to the nucleus upon treatment with PMA or IGF1. {ECO:0000269|PubMed:15271671}.
uniprot
proteins