LLPS-Mum-2125
Prkca

▼ OVERVIEW

Status: Reviewed
Protein Name: Protein kinase C alpha type
Gene Name: Prkca, Pkca
Ensembl Gene: ENSMUSG00000050965.14
Ensembl Protein: ENSMUSP00000097875.3
Organism: Mus musculus
Taxa ID: 10090
LLPS Type: Client


▼ PROPERTY


——— Disorder propensity (calculated by IUPred2A)

▼ Classification

Condensates:
CondensateDescriptionTissue/CellPMIDs
Stress granule, Postsynaptic densityPredicted from orthologsN/A(View)

▼ 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.

▼ SEQUENCE

Protein Sequence (FASTA)
1     MADVYPANDS  TASQDVANRF  ARKGALRQKN  VHEVKDHKFI  ARFFKQPTFC  SHCTDFIWGF  60
61    GKQGFQCQVC  CFVVHKRCHE  FVTFSCPGAD  KGPDTDDPRS  KHKFKIHTYG  SPTFCDHCGS  120
121   LLYGLIHQGM  KCDTCDMNVH  KQCVINVPSL  CGMDHTEKRG  RIYLKAEVTD  EKLHVTVRDA  180
181   KNLIPMDPNG  LSDPYVKLKL  IPDPKNESKQ  KTKTIRSTLN  PQWNESFTFK  LKPSDKDRRL  240
241   SVEIWDWDRT  TRNDFMGSLS  FGVSELMKMP  ASGWYKLLNQ  EEGEYYNVPI  PEGDEEGNME  300
301   LRQKFEKAKL  GPAGNKVISP  SEDRKQPSNN  LDRVKLTDFN  FLMVLGKGSF  GKVMLADRKG  360
361   TEELYAIKIL  KKDVVIQDDD  VECTMVEKRV  LALLDKPPFL  TQLHSCFQTV  DRLYFVMEYV  420
421   NGGDLMYHIQ  QVGKFKEPQA  VFYAAEISIG  LFFLHKRGII  YRDLKLDNVM  LDSEGHIKIA  480
481   DFGMCKEHMM  DGVTTRTFCG  TPDYIAPEII  AYQPYGKSVD  WWAYGVLLYE  MLAGQPPFDG  540
541   EDEDELFQSI  MEHNVSYPKS  LSKEAVSICK  GLMTKHPAKR  LGCGPEGERD  VREHAFFRRI  600
601   DWEKLENREI  QPPFKPKVCG  KGAENFDKFF  TRGQPVLTPP  DQLVIANIDQ  SDFEGFSYVN  660
661   PQFVHPILQS  AV  672
Nucleotide CDS Sequence (FASTA)
1     ATGGCTGACG  TTTACCCGGC  CAACGACTCC  ACGGCGTCTC  AGGACGTGGC  CAACCGCTTC  60
61    GCCCGCAAAG  GGGCGCTGAG  GCAGAAGAAC  GTGCATGAGG  TGAAAGACCA  CAAATTCATC  120
121   GCCCGCTTCT  TCAAGCAACC  CACCTTCTGC  AGCCACTGCA  CCGACTTCAT  CTGGGGGTTT  180
181   GGGAAACAAG  GCTTCCAGTG  CCAAGTTTGC  TGTTTTGTGG  TTCATAAGAG  GTGCCATGAG  240
241   TTCGTTACGT  TCTCTTGTCC  GGGTGCGGAT  AAGGGACCTG  ACACTGACGA  CCCCAGGAGC  300
301   AAGCACAAGT  TCAAAATCCA  CACATACGGA  AGCCCTACCT  TCTGTGATCA  CTGTGGGTCC  360
361   CTGCTCTATG  GACTTATCCA  CCAAGGGATG  AAATGTGACA  CCTGCGACAT  GAATGTTCAC  420
421   AAGCAGTGTG  TGATCAATGT  CCCTAGCCTC  TGCGGAATGG  ATCACACAGA  GAAGAGGGGG  480
481   CGGATTTATC  TGAAGGCTGA  GGTCACTGAT  GAAAAGCTCC  ACGTCACGGT  ACGAGATGCA  540
541   AAAAATCTAA  TCCCTATGGA  TCCAAATGGG  CTTTCGGATC  CTTATGTGAA  GCTGAAACTT  600
601   ATCCCTGACC  CCAAGAATGA  GAGCAAACAG  AAAACCAAAA  CCATCCGCTC  CACACTGAAT  660
661   CCTCAGTGGA  ATGAGTCCTT  CACGTTCAAA  TTAAAACCTT  CAGACAAAGA  CCGGCGACTG  720
721   TCTGTAGAAA  TCTGGGACTG  GGATCGGACG  ACTCGGAATG  ACTTCATGGG  ATCCCTTTCC  780
781   TTTGGTGTCT  CAGAGCTAAT  GAAGATGCCG  GCCAGTGGAT  GGTATAAACT  GCTCAACCAA  840
841   GAAGAGGGCG  AATACTACAA  TGTGCCCATT  CCAGAAGGAG  ATGAAGAAGG  CAACATGGAA  900
901   CTCAGGCAGA  AGTTTGAGAA  AGCCAAGCTA  GGCCCTGCTG  GTAACAAAGT  CATCAGCCCT  960
961   TCAGAAGACA  GAAAGCAACC  ATCCAACAAC  CTGGACAGAG  TGAAACTCAC  AGACTTCAAC  1020
1021  TTCCTCATGG  TGCTGGGGAA  GGGGAGTTTT  GGGAAGGTGA  TGCTTGCTGA  CAGGAAGGGA  1080
1081  ACGGAGGAAC  TGTACGCCAT  CAAGATCCTG  AAGAAGGACG  TGGTGATCCA  GGACGACGAC  1140
1141  GTGGAGTGCA  CCATGGTGGA  GAAGCGCGTG  CTGGCCCTGC  TGGACAAGCC  GCCATTTCTG  1200
1201  ACACAGCTGC  ACTCCTGCTT  CCAGACAGTG  GACCGGCTGT  ACTTCGTCAT  GGAATACGTC  1260
1261  AACGGCGGGG  ACCTCATGTA  CCACATTCAG  CAAGTCGGGA  AATTTAAGGA  GCCACAAGCA  1320
1321  GTATTCTACG  CAGCCGAGAT  CTCCATCGGA  CTGTTCTTCC  TTCATAAAAG  AGGGATCATT  1380
1381  TACAGGGATC  TGAAGCTGGA  CAATGTCATG  CTGGACTCAG  AAGGGCACAT  CAAAATCGCC  1440
1441  GACTTTGGGA  TGTGCAAGGA  ACACATGATG  GATGGAGTCA  CGACCAGGAC  CTTCTGTGGG  1500
1501  ACTCCGGACT  ACATTGCCCC  AGAGATAATC  GCTTACCAGC  CGTACGGGAA  GTCTGTAGAT  1560
1561  TGGTGGGCGT  ACGGTGTGCT  GCTGTACGAG  ATGCTAGCCG  GGCAGCCTCC  GTTTGATGGT  1620
1621  GAAGATGAAG  ATGAACTGTT  TCAGTCTATA  ATGGAGCACA  ACGTGTCCTA  CCCCAAATCC  1680
1681  TTGTCCAAGG  AAGCCGTCTC  TATCTGCAAA  GGACTTATGA  CCAAACACCC  TGCCAAGCGG  1740
1741  CTGGGCTGCG  GGCCCGAGGG  AGAGAGGGAT  GTCAGAGAGC  ATGCCTTCTT  CAGGAGAATC  1800
1801  GACTGGGAGA  AACTGGAGAA  CAGGGAGATC  CAACCACCAT  TCAAGCCCAA  AGTGTGTGGC  1860
1861  AAAGGAGCAG  AAAACTTTGA  CAAGTTCTTC  ACGCGAGGAC  AGCCTGTCTT  AACACCACCA  1920
1921  GATCAGCTGG  TCATTGCTAA  CATAGACCAA  TCTGATTTTG  AAGGGTTCTC  GTATGTCAAC  1980
1981  CCCCAGTTTG  TGCACCCAAT  CTTGCAAAGT  GCAGTATGA  2019

▼ KEYWORD

ID
Family
Acetylation
Angiogenesis
Apoptosis
ATP-binding
Calcium
Cell adhesion
Cell membrane
Complete proteome
Cytoplasm
Kinase
Membrane
Metal-binding
Mitochondrion
Nucleotide-binding
Nucleus
Phosphoprotein
Polymorphism
Reference proteome
Repeat
Serine/threonine-protein kinase
Transferase
Zinc
Zinc-finger

▼ GENE ONTOLOGY

ID
Classification
Description
Cellular Component
Alphav-beta3 integrin-PKCalpha complex
Cellular Component
Apical part of cell
Cellular Component
Axon
Cellular Component
Calyx of Held
Cellular Component
Cytoplasm
Cellular Component
Cytosol
Cellular Component
Dendrite
Cellular Component
Endoplasmic reticulum
Cellular Component
Intercalated disc
Cellular Component
Membrane
Cellular Component
Membrane raft
Cellular Component
Mitochondrial membrane
Cellular Component
Mitochondrion
Cellular Component
Neuron projection
Cellular Component
Neuronal cell body
Cellular Component
Nucleus
Cellular Component
Perinuclear region of cytoplasm
Cellular Component
Photoreceptor outer segment
Cellular Component
Plasma membrane
Cellular Component
Presynaptic cytosol
Cellular Component
Protein-containing complex
Molecular Function
ATP binding
Molecular Function
Calcium-dependent protein kinase C activity
Molecular Function
Enzyme binding
Molecular Function
Histone kinase activity (H3-T6 specific)
Molecular Function
Integrin binding
Molecular Function
Protein kinase activity
Molecular Function
Protein kinase C activity
Molecular Function
Protein serine/threonine kinase activity
Molecular Function
Zinc ion binding
Biological Process
Angiogenesis
Biological Process
Cell adhesion
Biological Process
Cellular calcium ion homeostasis
Biological Process
Cellular response to carbohydrate stimulus
Biological Process
Central nervous system neuron axonogenesis
Biological Process
Chondrocyte differentiation
Biological Process
Desmosome assembly
Biological Process
Histone H3-T6 phosphorylation
Biological Process
Inactivation of MAPK activity
Biological Process
Induction of positive chemotaxis
Biological Process
Intracellular signal transduction
Biological Process
Intrinsic apoptotic signaling pathway
Biological Process
Learning or memory
Biological Process
Negative regulation of anion channel activity
Biological Process
Negative regulation of cell population proliferation
Biological Process
Negative regulation of glial cell apoptotic process
Biological Process
Negative regulation of glucose import
Biological Process
Negative regulation of heart contraction
Biological Process
Negative regulation of insulin receptor signaling pathway
Biological Process
Negative regulation of protein kinase activity
Biological Process
Negative regulation of protein phosphorylation
Biological Process
Negative regulation of translation
Biological Process
Neutrophil chemotaxis
Biological Process
Peptidyl-serine autophosphorylation
Biological Process
Peptidyl-serine phosphorylation
Biological Process
Peptidyl-threonine phosphorylation
Biological Process
Positive regulation of angiogenesis
Biological Process
Positive regulation of blood vessel endothelial cell migration
Biological Process
Positive regulation of bone resorption
Biological Process
Positive regulation of cardiac muscle hypertrophy
Biological Process
Positive regulation of cell adhesion
Biological Process
Positive regulation of cell migration
Biological Process
Positive regulation of dense core granule biogenesis
Biological Process
Positive regulation of endothelial cell migration
Biological Process
Positive regulation of endothelial cell proliferation
Biological Process
Positive regulation of ERK1 and ERK2 cascade
Biological Process
Positive regulation of exocytosis
Biological Process
Positive regulation of inflammatory response
Biological Process
Positive regulation of lipopolysaccharide-mediated signaling pathway
Biological Process
Positive regulation of macrophage differentiation
Biological Process
Positive regulation of mitotic cell cycle
Biological Process
Positive regulation of protein phosphorylation
Biological Process
Positive regulation of smooth muscle cell proliferation
Biological Process
Positive regulation of synapse assembly
Biological Process
Presynaptic modulation of chemical synaptic transmission
Biological Process
Protein autophosphorylation
Biological Process
Protein phosphorylation
Biological Process
Regulation of muscle contraction
Biological Process
Regulation of peptidyl-tyrosine phosphorylation
Biological Process
Regulation of platelet aggregation
Biological Process
Regulation of receptor-mediated endocytosis
Biological Process
Regulation of response to osmotic stress
Biological Process
Regulation of synaptic vesicle exocytosis
Biological Process
Regulation of the force of heart contraction
Biological Process
Response to estradiol
Biological Process
Response to ethanol
Biological Process
Response to interleukin-1
Biological Process
Response to reactive oxygen species

▼ KEGG


▼ ORTHOLOGY

DrLLPS IDOrganismIdentityE-valueScore
LLPS-Mea-4325Mesocricetus auratus99.850.01404
LLPS-Nol-2740Nomascus leucogenys99.840.01281
LLPS-Maf-2821Macaca fascicularis99.70.01402
LLPS-Cea-0184Cercocebus atys99.70.01402
LLPS-Paa-0504Papio anubis99.70.01402
LLPS-Man-1154Macaca nemestrina99.70.01402
LLPS-Pap-1516Pan paniscus99.680.01304
LLPS-Mal-4117Mandrillus leucophaeus99.670.01279
LLPS-Ict-0681Ictidomys tridecemlineatus99.670.01256
LLPS-Gog-3736Gorilla gorilla99.550.01400
LLPS-Caj-1500Callithrix jacchus99.550.01400
LLPS-Aon-3174Aotus nancymaae99.550.01400
LLPS-Aim-3306Ailuropoda melanoleuca99.550.01389
LLPS-Mam-2317Macaca mulatta99.480.01197
LLPS-Ran-2688Rattus norvegicus99.40.01395
LLPS-Dio-1398Dipodomys ordii99.40.01399
LLPS-Pat-0278Pan troglodytes99.40.01398
LLPS-Hos-2011Homo sapiens99.40.01400
LLPS-Cas-0127Carlito syrichta99.350.01278
LLPS-Chs-0762Chlorocebus sabaeus99.340.01259
LLPS-Fud-0807Fukomys damarensis99.260.01399
LLPS-Caf-2146Canis familiaris99.190.01279
LLPS-Bot-1825Bos taurus99.170.01254
LLPS-Loa-2349Loxodonta africana98.810.01389
LLPS-Cap-0350Cavia porcellus98.640.01200
LLPS-Ova-4366Ovis aries98.220.01266
LLPS-Urm-1315Ursus maritimus98.190.01233
LLPS-Otg-2055Otolemur garnettii98.090.01392
LLPS-Sah-3826Sarcophilus harrisii97.920.01181
LLPS-Mod-3533Monodelphis domestica97.920.01381
LLPS-Fec-1747Felis catus97.650.01387
LLPS-Mup-2132Mustela putorius furo96.80.01383
LLPS-Eqc-2370Equus caballus96.670.01389
LLPS-Rhb-1748Rhinopithecus bieti96.350.01206
LLPS-Ora-1217Ornithorhynchus anatinus95.920.01168
LLPS-Anp-1901Anas platyrhynchos95.450.01237
LLPS-Poa-2858Pongo abelii95.390.01326
LLPS-Meg-1983Meleagris gallopavo94.970.01232
LLPS-Tag-1182Taeniopygia guttata94.810.01231
LLPS-Pes-0156Pelodiscus sinensis94.240.01243
LLPS-Myl-1438Myotis lucifugus93.280.01163
LLPS-Gaga-2847Gallus gallus92.670.01326
LLPS-Fia-3557Ficedula albicollis92.110.01319
LLPS-Lac-2409Latimeria chalumnae90.660.01095
LLPS-Anc-2017Anolis carolinensis88.910.01162
LLPS-Scf-0490Scleropages formosus87.70.01247
LLPS-Leo-1218Lepisosteus oculatus87.630.01079
LLPS-Icp-0366Ictalurus punctatus86.650.01233
LLPS-Orl-0110Oryzias latipes86.520.01233
LLPS-Gaa-2173Gasterosteus aculeatus86.40.01215
LLPS-Pof-1240Poecilia formosa85.080.01211
LLPS-Xim-1867Xiphophorus maculatus84.930.01212
LLPS-Scm-1142Scophthalmus maximus84.820.01215
LLPS-Dar-2697Danio rerio84.60.01209
LLPS-Tar-2209Takifugu rubripes84.570.01193
LLPS-Asm-2463Astyanax mexicanus79.730.01124
LLPS-Orn-2672Oreochromis niloticus78.110.01095
LLPS-Cae-0682Caenorhabditis elegans69.250.0 966
LLPS-Drm-1985Drosophila melanogaster68.910.0 958
LLPS-Xet-1635Xenopus tropicalis58.172e-129 401
LLPS-Cis-0057Ciona savignyi56.871e-134 420
LLPS-Ten-1276Tetraodon nigroviridis56.743e-124 391
LLPS-Sus-3108Sus scrofa47.240.0 590
LLPS-Orc-1985Oryctolagus cuniculus47.090.0 588