LLPS-Ran-0818
Prkce

▼ OVERVIEW

Status: Unreviewed
Protein Name: Protein kinase C epsilon type; nPKC-epsilon
Gene Name: Prkce, Pkce
Ensembl Gene: ENSRNOG00000015603.7
Ensembl Protein: ENSRNOP00000020959.7
Organism: Rattus norvegicus
Taxa ID: 10116
LLPS Type: Others
PDB: 1GMI (A) More


▼ PROPERTY


——— Disorder propensity (calculated by IUPred2A)

▼ Classification

Condensates:
CondensateEvidenceOrthologs
Centrosome/Spindle pole body, Postsynaptic densityPredicted from orthologs(View)

▼ FUNCTION

Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-cell detachment prior to migration. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1.

▼ CROSS REFERENCE

▼ SEQUENCE

Protein Sequence (FASTA)
1     FRGVIGKQGY  QCQVCTCVVH  KRCHELIITK  CAGLKKQETP  DEVGSQRFSV  NMPHKFGIHN  60
61    YKVPTFCDHC  GSLLWGLLRQ  GLQCKVCKMN  VHRRCETNVA  PNCGVDARGI  AKVLADLGVT  120
121   PDKITNSGQR  RKKLAAGAES  PQPASGNSPS  EDDRSKSAPT  SPCDQELKEL  ENNIRKALSF  180
181   DNRGEEHRAS  SSTDGQLASP  GENGEVRQGQ  AKRLGLDEFN  FIKVLGKGSF  GKVMLAELKG  240
241   KDEVYAVKVL  KKDVILQDDD  VDCTMTEKRI  LALARKHPYL  TQLYCCFQTK  DRLFFVMEYV  300
301   NGGDLMFQIQ  RSRKFDEPRS  RFYAAEVTSA  LMFLHQHGVI  YRDLKLDNIL  LDAEGHCKLA  360
361   DFGMCKEGIL  NGVTTTTFCG  TPDYIAPEIL  QELEYGPSVD  WWALGVLMYE  MMAGQPPFEA  420
421   DNEDDLFESI  LHDDVLYPVW  LSKEAVSILK  AFMTKNPHKR  LGCVAAQNGE  DAIKQHPFFK  480
481   EIDWVLLEQK  KIKPPFKPRI  KTKRDVNNFD  QDFTREEPIL  TLVDEAIVKQ  INQEEFKGFS  540
541   YFGEDLMP  548
Nucleotide CDS Sequence (FASTA)
1     TTCAGGGGTG  TCATAGGAAA  ACAGGGATAT  CAATGTCAAG  TTTGTACCTG  CGTCGTCCAC  60
61    AAACGATGCC  ATGAGCTCAT  TATTACGAAG  TGCGCTGGGC  TAAAGAAACA  GGAAACCCCT  120
121   GACGAGGTGG  GCTCCCAACG  CTTCAGCGTC  AACATGCCCC  ACAAGTTCGG  GATCCACAAC  180
181   TACAAGGTCC  CCACGTTCTG  TGACCACTGT  GGCTCCCTGC  TCTGGGGCCT  CTTGCGGCAG  240
241   GGCCTGCAGT  GTAAAGTCTG  CAAAATGAAT  GTTCACCGTC  GATGCGAGAC  CAACGTGGCT  300
301   CCCAATTGTG  GGGTGGACGC  CAGAGGAATT  GCCAAGGTGC  TGGCCGATCT  TGGCGTTACT  360
361   CCAGACAAAA  TCACCAACAG  TGGCCAGAGA  AGGAAAAAGC  TCGCTGCTGG  TGCTGAGTCC  420
421   CCACAGCCGG  CTTCTGGAAA  CTCCCCATCA  GAAGACGACC  GATCCAAGTC  AGCGCCCACC  480
481   TCCCCTTGTG  ACCAGGAACT  AAAAGAACTT  GAAAACAACA  TCCGGAAGGC  CTTGTCATTT  540
541   GACAACCGAG  GAGAGGAGCA  CCGAGCCTCG  TCGTCTACTG  ATGGCCAGCT  GGCAAGCCCT  600
601   GGCGAGAACG  GTGAAGTCCG  GCAAGGCCAG  GCCAAGCGCT  TGGGCCTGGA  TGAGTTCAAC  660
661   TTCATCAAGG  TGTTAGGCAA  AGGCAGCTTT  GGCAAGGTCA  TGCTGGCCGA  GCTCAAGGGT  720
721   AAGGATGAAG  TCTATGCTGT  GAAGGTCTTA  AAGAAGGACG  TCATCCTGCA  GGATGACGAC  780
781   GTGGACTGCA  CGATGACAGA  GAAGAGGATT  TTGGCTCTGG  CGCGGAAACA  CCCTTATCTA  840
841   ACCCAACTCT  ATTGCTGCTT  CCAGACCAAG  GACCGCCTCT  TCTTCGTCAT  GGAATATGTA  900
901   AACGGTGGAG  ACCTCATGTT  CCAGATTCAG  CGGTCCCGAA  AATTCGATGA  GCCTCGTTCC  960
961   CGGTTCTATG  CTGCCGAGGT  CACATCTGCT  CTCATGTTTC  TCCACCAACA  TGGAGTGATC  1020
1021  TACAGGGATT  TGAAACTGGA  CAACATCCTT  CTAGATGCAG  AAGGTCACTG  CAAGCTGGCT  1080
1081  GACTTTGGGA  TGTGCAAGGA  AGGGATTCTG  AATGGCGTGA  CAACTACCAC  CTTCTGTGGG  1140
1141  ACTCCTGACT  ACATAGCTCC  AGAGATCCTG  CAGGAGTTGG  AGTACGGCCC  CTCAGTGGAC  1200
1201  TGGTGGGCCC  TGGGCGTGCT  GATGTACGAG  ATGATGGCCG  GGCAGCCCCC  CTTTGAAGCT  1260
1261  GACAACGAGG  ACGACTTGTT  TGAATCCATC  CTTCACGATG  ACGTTCTCTA  CCCTGTCTGG  1320
1321  CTTAGCAAGG  AGGCTGTCAG  CATCCTGAAA  GCTTTCATGA  CCAAGAACCC  GCACAAGCGC  1380
1381  CTGGGCTGCG  TGGCAGCACA  GAACGGGGAA  GATGCCATCA  AGCAACATCC  ATTCTTCAAG  1440
1441  GAGATTGACT  GGGTACTGCT  GGAGCAGAAG  AAAATCAAGC  CCCCCTTCAA  GCCGAGAATT  1500
1501  AAAACCAAGA  GAGATGTCAA  TAACTTTGAC  CAAGACTTTA  CCCGGGAAGA  GCCAATACTT  1560
1561  ACACTTGTGG  ATGAAGCAAT  CGTGAAGCAG  ATCAACCAGG  AAGAATTCAA  AGGCTTCTCC  1620
1621  TACTTTGGTG  AAGACCTGAT  GCCCTGA  1647

▼ KEYWORD

ID
Family
3D-structure
ATP-binding
Cell adhesion
Cell cycle
Cell division
Cell membrane
Complete proteome
Cytoplasm
Cytoskeleton
Immunity
Kinase
Membrane
Metal-binding
Nucleotide-binding
Nucleus
Phosphoprotein
Reference proteome
Repeat
Serine/threonine-protein kinase
Transferase
Zinc
Zinc-finger

▼ GENE ONTOLOGY

ID
Classification
Description
Cellular Component
Cell periphery
Cellular Component
Cytoskeleton
Cellular Component
Cytosol
Cellular Component
Glutamatergic synapse
Cellular Component
Golgi membrane
Cellular Component
Mitochondrion
Cellular Component
Neuromuscular junction
Cellular Component
Nucleus
Cellular Component
Perinuclear region of cytoplasm
Cellular Component
Plasma membrane
Cellular Component
Presynaptic cytosol
Cellular Component
T-tubule
Molecular Function
Actin monomer binding
Molecular Function
ATP binding
Molecular Function
Calcium-independent protein kinase C activity
Molecular Function
Metal ion binding
Molecular Function
Protein kinase binding
Molecular Function
Protein kinase C activity
Molecular Function
Protein serine/threonine kinase activity
Molecular Function
SH3 domain binding
Molecular Function
Signaling receptor binding
Biological Process
Cell adhesion
Biological Process
Cell cycle
Biological Process
Cell division
Biological Process
Cellular response to platelet-derived growth factor stimulus
Biological Process
Intracellular signal transduction
Biological Process
Lipopolysaccharide-mediated signaling pathway
Biological Process
Negative regulation of apoptotic process
Biological Process
Negative regulation of mitochondrial calcium ion concentration
Biological Process
Negative regulation of mitochondrial membrane potential
Biological Process
Negative regulation of release of sequestered calcium ion into cytosol
Biological Process
Peptidyl-serine phosphorylation
Biological Process
Positive regulation of actin filament polymerization
Biological Process
Positive regulation of cytokinesis
Biological Process
Positive regulation of epithelial cell migration
Biological Process
Positive regulation of fibroblast migration
Biological Process
Positive regulation of wound healing
Biological Process
Regulation of synaptic vesicle exocytosis
Biological Process
TRAM-dependent toll-like receptor 4 signaling pathway

▼ KEGG


▼ ORTHOLOGY

DrLLPS IDOrganismIdentityE-valueScore
LLPS-Mum-4767Mus musculus99.270.01096
LLPS-Eqc-0925Equus caballus98.90.01093
LLPS-Cap-4218Cavia porcellus98.90.01088
LLPS-Fud-1539Fukomys damarensis98.720.01085
LLPS-Dio-1632Dipodomys ordii98.720.01095
LLPS-Ict-4391Ictidomys tridecemlineatus98.720.01092
LLPS-Aon-0482Aotus nancymaae98.530.01089
LLPS-Bot-2172Bos taurus98.530.01089
LLPS-Myl-2698Myotis lucifugus98.530.01088
LLPS-Orc-1985Oryctolagus cuniculus98.530.01085
LLPS-Sus-3108Sus scrofa98.350.01088
LLPS-Loa-2918Loxodonta africana98.350.01090
LLPS-Otg-3518Otolemur garnettii98.350.01087
LLPS-Gog-0292Gorilla gorilla98.170.01087
LLPS-Ova-2128Ovis aries98.170.01085
LLPS-Pat-1278Pan troglodytes98.170.01087
LLPS-Pap-0143Pan paniscus98.170.01087
LLPS-Hos-1016Homo sapiens98.170.01087
LLPS-Poa-4349Pongo abelii98.170.01087
LLPS-Nol-3969Nomascus leucogenys98.170.01087
LLPS-Cea-2282Cercocebus atys97.990.01081
LLPS-Chs-1534Chlorocebus sabaeus97.990.01082
LLPS-Maf-3829Macaca fascicularis97.990.01081
LLPS-Caj-2538Callithrix jacchus97.990.01083
LLPS-Mal-1203Mandrillus leucophaeus97.990.01081
LLPS-Paa-2579Papio anubis97.990.01081
LLPS-Man-4180Macaca nemestrina97.990.01081
LLPS-Fec-0861Felis catus97.990.01084
LLPS-Rhb-0433Rhinopithecus bieti97.990.01082
LLPS-Mam-3073Macaca mulatta97.990.01081
LLPS-Caf-4354Canis familiaris97.990.01083
LLPS-Aim-1354Ailuropoda melanoleuca97.80.01076
LLPS-Mup-2087Mustela putorius furo97.440.01075
LLPS-Anp-1658Anas platyrhynchos95.53e-64 227
LLPS-Pes-0119Pelodiscus sinensis94.020.01040
LLPS-Anc-3824Anolis carolinensis93.450.01033
LLPS-Meg-0794Meleagris gallopavo93.30.01038
LLPS-Fia-3794Ficedula albicollis93.30.01033
LLPS-Gaga-3441Gallus gallus93.30.01037
LLPS-Tag-2860Taeniopygia guttata93.120.01033
LLPS-Xet-1773Xenopus tropicalis91.420.01012
LLPS-Mea-0699Mesocricetus auratus89.190.0 959
LLPS-Scf-0035Scleropages formosus86.470.0 926
LLPS-Icp-1540Ictalurus punctatus85.920.0 939
LLPS-Dar-2821Danio rerio84.830.0 925
LLPS-Ten-3282Tetraodon nigroviridis83.00.0 901
LLPS-Orn-3608Oreochromis niloticus81.870.0 921
LLPS-Scm-3209Scophthalmus maximus81.740.0 908
LLPS-Orl-3374Oryzias latipes80.590.0 900
LLPS-Xim-4136Xiphophorus maculatus80.420.0 897
LLPS-Gaa-3848Gasterosteus aculeatus79.750.0 866
LLPS-Pof-3508Poecilia formosa79.340.0 858
LLPS-Tar-1122Takifugu rubripes76.640.0 809
LLPS-Asm-1752Astyanax mexicanus73.280.0 756
LLPS-Cae-0673Caenorhabditis elegans62.680.0 674
LLPS-Cas-2230Carlito syrichta61.060.0 668
LLPS-Drm-2395Drosophila melanogaster60.660.0 662
LLPS-Cis-0057Ciona savignyi57.270.0 603
LLPS-Mod-3533Monodelphis domestica48.04e-0860.5
LLPS-Sah-0631Sarcophilus harrisii47.581e-166 496
LLPS-Lac-3024Latimeria chalumnae47.426e-166 495
LLPS-Leo-1624Lepisosteus oculatus47.329e-168 500
LLPS-Urm-2936Ursus maritimus46.743e-161 484