KPCE_MOUSE
ID KPCE_MOUSE Reviewed; 737 AA.
AC P16054;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Protein kinase C epsilon type;
DE EC=2.7.11.13;
DE AltName: Full=nPKC-epsilon;
GN Name=Prkce; Synonyms=Pkce, Pkcea;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2917656; DOI=10.1016/0014-5793(89)80160-7;
RA Schaap D., Parker P.J., Bristol A., Kriz R., Knopf J.;
RT "Unique substrate specificity and regulatory properties of PKC-epsilon: a
RT rationale for diversity.";
RL FEBS Lett. 243:351-357(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9467942; DOI=10.1038/sj.onc.1201507;
RA Wang Q.J., Acs P., Goodnight J., Blumberg P.M., Mischak H., Mushinski J.F.;
RT "The catalytic domain of PKC-epsilon, in reciprocal PKC-delta and - epsilon
RT chimeras, is responsible for conferring tumorgenicity to NIH3T3 cells,
RT whereas both regulatory and catalytic domains of PKC-epsilon contribute to
RT in vitro transformation.";
RL Oncogene 16:53-60(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Wheeler D.L.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, INTERACTION WITH ACTIN, AND ACTIN-BINDING MOTIF.
RX PubMed=11746497; DOI=10.1002/jcb.1246;
RA Hernandez R.M., Wescott G.G., Mayhew M.W., McJilton M.A., Terrian D.M.;
RT "Biochemical and morphogenic effects of the interaction between protein
RT kinase C-epsilon and actin in vitro and in cultured NIH3T3 cells.";
RL J. Cell. Biochem. 83:532-546(2001).
RN [5]
RP FUNCTION IN PHOSPHORYLATION OF PRKD1.
RX PubMed=12407104; DOI=10.1074/jbc.m208075200;
RA Waldron R.T., Rozengurt E.;
RT "Protein kinase C phosphorylates protein kinase D activation loop Ser744
RT and Ser748 and releases autoinhibition by the pleckstrin homology domain.";
RL J. Biol. Chem. 278:154-163(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-710, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP FUNCTION.
RX PubMed=15949469; DOI=10.1016/j.cardiores.2005.03.002;
RA Stawowy P., Margeta C., Blaschke F., Lindschau C., Spencer-Haensch C.,
RA Leitges M., Biagini G., Fleck E., Graf K.;
RT "Protein kinase C epsilon mediates angiotensin II-induced activation of
RT beta1-integrins in cardiac fibroblasts.";
RL Cardiovasc. Res. 67:50-59(2005).
RN [8]
RP FUNCTION IN PHOSPHORYLATION OF VIM.
RX PubMed=16270034; DOI=10.1038/sj.emboj.7600847;
RA Ivaska J., Vuoriluoto K., Huovinen T., Izawa I., Inagaki M., Parker P.J.;
RT "PKCepsilon-mediated phosphorylation of vimentin controls integrin
RT recycling and motility.";
RL EMBO J. 24:3834-3845(2005).
RN [9]
RP FUNCTION IN PHOSPHORYLATION OF TNNI3.
RX PubMed=16445938; DOI=10.1016/j.yjmcc.2005.12.009;
RA Scruggs S.B., Walker L.A., Lyu T., Geenen D.L., Solaro R.J., Buttrick P.M.,
RA Goldspink P.H.;
RT "Partial replacement of cardiac troponin I with a non-phosphorylatable
RT mutant at serines 43/45 attenuates the contractile dysfunction associated
RT with PKCepsilon phosphorylation.";
RL J. Mol. Cell. Cardiol. 40:465-473(2006).
RN [10]
RP FUNCTION IN PHOSPHORYLATION OF TICAM2/TRAM.
RX PubMed=16757566; DOI=10.1073/pnas.0600462103;
RA McGettrick A.F., Brint E.K., Palsson-McDermott E.M., Rowe D.C.,
RA Golenbock D.T., Gay N.J., Fitzgerald K.A., O'Neill L.A.J.;
RT "Trif-related adapter molecule is phosphorylated by PKCepsilon during Toll-
RT like receptor 4 signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9196-9201(2006).
RN [11]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-729, AND MUTAGENESIS OF
RP SER-729.
RX PubMed=17611075; DOI=10.1016/j.cellsig.2007.05.009;
RA Xu T.R., He G., Dobson K., England K., Rumsby M.;
RT "Phosphorylation at Ser729 specifies a Golgi localisation for protein
RT kinase C epsilon (PKCepsilon) in 3T3 fibroblasts.";
RL Cell. Signal. 19:1986-1995(2007).
RN [12]
RP PHOSPHORYLATION AT SER-234; SER-316 AND SER-368.
RX PubMed=18237277; DOI=10.1042/bj20071348;
RA Durgan J., Cameron A.J., Saurin A.T., Hanrahan S., Totty N., Messing R.O.,
RA Parker P.J.;
RT "The identification and characterization of novel PKCepsilon
RT phosphorylation sites provide evidence for functional cross-talk within the
RT PKC superfamily.";
RL Biochem. J. 411:319-331(2008).
RN [13]
RP FUNCTION, INTERACTION WITH YWHAB, PHOSPHORYLATION AT SER-346; SER-350 AND
RP SER-368, AND MUTAGENESIS OF SER-346 AND SER-368.
RX PubMed=18604201; DOI=10.1038/ncb1749;
RA Saurin A.T., Durgan J., Cameron A.J., Faisal A., Marber M.S., Parker P.J.;
RT "The regulated assembly of a PKCepsilon complex controls the completion of
RT cytokinesis.";
RL Nat. Cell Biol. 10:891-901(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-329; SER-337;
RP SER-346; THR-349 AND SER-388, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-
CC dependent serine/threonine-protein kinase that plays essential roles in
CC the regulation of multiple cellular processes linked to cytoskeletal
CC proteins, such as cell adhesion, motility, migration and cell cycle,
CC functions in neuron growth and ion channel regulation, and is involved
CC in immune response, cancer cell invasion and regulation of apoptosis.
CC Mediates cell adhesion to the extracellular matrix via integrin-
CC dependent signaling, by mediating angiotensin-2-induced activation of
CC integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS,
CC which phosphorylates and activates PTK2/FAK, leading to the spread of
CC cardiomyocytes. Involved in the control of the directional transport of
CC ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an
CC intermediate filament (IF) protein. In epithelial cells, associates
CC with and phosphorylates keratin-8 (KRT8), which induces targeting of
CC desmoplakin at desmosomes and regulates cell-cell contact.
CC Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-
CC cell detachment prior to migration. During cytokinesis, forms a complex
CC with YWHAB, which is crucial for daughter cell separation, and
CC facilitates abscission by a mechanism which may implicate the
CC regulation of RHOA. In cardiac myocytes, regulates myofilament function
CC and excitation coupling at the Z-lines, where it is indirectly
CC associated with F-actin via interaction with COPB1. During endothelin-
CC induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK,
CC which is critical for cardiomyocyte survival and regulation of
CC sarcomere length. Plays a role in the pathogenesis of dilated
CC cardiomyopathy via persistent phosphorylation of troponin I (TNNI3).
CC Involved in nerve growth factor (NFG)-induced neurite outgrowth and
CC neuron morphological change independently of its kinase activity, by
CC inhibition of RHOA pathway, activation of CDC42 and cytoskeletal
CC rearrangement. May be involved in presynaptic facilitation by mediating
CC phorbol ester-induced synaptic potentiation. Phosphorylates gamma-
CC aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the
CC response of GABA receptors to ethanol and benzodiazepines and may
CC mediate acute tolerance to the intoxicating effects of ethanol. Upon
CC PMA treatment, phosphorylates the capsaicin- and heat-activated cation
CC channel TRPV1, which is required for bradykinin-induced sensitization
CC of the heat response in nociceptive neurons. Is able to form a complex
CC with PDLIM5 and N-type calcium channel, and may enhance channel
CC activities and potentiates fast synaptic transmission by
CC phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2).
CC Downstream of TLR4, plays an important role in the lipopolysaccharide
CC (LPS)-induced immune response by phosphorylating and activating
CC TICAM2/TRAM, which in turn activates the transcription factor IRF3 and
CC subsequent cytokines production. In differentiating erythroid
CC progenitors, is regulated by EPO and controls the protection against
CC the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the
CC regulation of the insulin-induced phosphorylation and activation of
CC AKT1. Phosphorylates NLRP5/MATER and may thereby modulate AKT pathway
CC activation in cumulus cells (By similarity).
CC {ECO:0000250|UniProtKB:Q02156, ECO:0000269|PubMed:11746497,
CC ECO:0000269|PubMed:12407104, ECO:0000269|PubMed:15949469,
CC ECO:0000269|PubMed:16270034, ECO:0000269|PubMed:16445938,
CC ECO:0000269|PubMed:16757566, ECO:0000269|PubMed:18604201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13;
CC -!- ACTIVITY REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are
CC calcium-insensitive, but activated by diacylglycerol (DAG) and
CC phosphatidylserine. Three specific sites; Thr-566 (activation loop of
CC the kinase domain), Thr-710 (turn motif) and Ser-729 (hydrophobic
CC region), need to be phosphorylated for its full activation.
CC -!- SUBUNIT: Forms a ternary complex with TRIM63 and RACK1/GN2BL1 (By
CC similarity). Can form a complex with PDLIM5 and N-type calcium channel
CC (By similarity). Interacts with COPB1 (By similarity). Interacts with
CC DGKQ (By similarity). Interacts with STAT3 (By similarity). Interacts
CC with YWHAB (PubMed:18604201). Interacts with HSP90AB1; promotes
CC functional activation in a heat shock-dependent manner (By similarity).
CC Interacts (via phorbol-ester/DAG-type 2 domain) with PRPH and VIM (By
CC similarity). Interacts with NLRP5/MATER (By similarity).
CC {ECO:0000250|UniProtKB:P09216, ECO:0000250|UniProtKB:Q02156,
CC ECO:0000269|PubMed:18604201}.
CC -!- INTERACTION:
CC P16054; P23242: Gja1; NbExp=3; IntAct=EBI-298451, EBI-298630;
CC P16054; Q9CQV8: Ywhab; NbExp=5; IntAct=EBI-298451, EBI-771608;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q02156}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02156}. Cell membrane
CC {ECO:0000250|UniProtKB:Q02156}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:17611075}. Nucleus {ECO:0000269|PubMed:17611075}.
CC Note=Translocated to plasma membrane in epithelial cells stimulated by
CC HGF (By similarity). Associated with the Golgi at the perinuclear site
CC in pre-passage fibroblasts (PubMed:17611075). In passaging cells,
CC translocated to the cell periphery (PubMed:17611075). Translocated to
CC the nucleus in PMA-treated cells (PubMed:17611075).
CC {ECO:0000250|UniProtKB:Q02156, ECO:0000269|PubMed:17611075}.
CC -!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type region 1
CC (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a
CC non-calcium binding domain.
CC -!- PTM: Phosphorylation on Thr-566 by PDPK1 triggers autophosphorylation
CC on Ser-729 (By similarity). Phosphorylation in the hinge domain at Ser-
CC 350 by MAPK11 or MAPK14, Ser-346 by GSK3B and Ser-368 by
CC autophosphorylation is required for interaction with YWHAB.
CC {ECO:0000250, ECO:0000269|PubMed:17611075, ECO:0000269|PubMed:18237277,
CC ECO:0000269|PubMed:18604201}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; AF028009; AAB84189.1; -; mRNA.
DR EMBL; AF325507; AAG53692.1; -; mRNA.
DR CCDS; CCDS29008.1; -.
DR PIR; S02270; KIMSCE.
DR RefSeq; NP_035234.1; NM_011104.3.
DR AlphaFoldDB; P16054; -.
DR SMR; P16054; -.
DR BioGRID; 202198; 27.
DR CORUM; P16054; -.
DR DIP; DIP-31066N; -.
DR IntAct; P16054; 97.
DR MINT; P16054; -.
DR STRING; 10090.ENSMUSP00000094874; -.
DR BindingDB; P16054; -.
DR ChEMBL; CHEMBL4366; -.
DR GuidetoPHARMACOLOGY; 1486; -.
DR iPTMnet; P16054; -.
DR PhosphoSitePlus; P16054; -.
DR SwissPalm; P16054; -.
DR EPD; P16054; -.
DR jPOST; P16054; -.
DR MaxQB; P16054; -.
DR PaxDb; P16054; -.
DR PeptideAtlas; P16054; -.
DR PRIDE; P16054; -.
DR ProteomicsDB; 265020; -.
DR Antibodypedia; 4528; 712 antibodies from 43 providers.
DR DNASU; 18754; -.
DR Ensembl; ENSMUST00000097274; ENSMUSP00000094873; ENSMUSG00000045038.
DR Ensembl; ENSMUST00000097275; ENSMUSP00000094874; ENSMUSG00000045038.
DR GeneID; 18754; -.
DR KEGG; mmu:18754; -.
DR UCSC; uc008dug.2; mouse.
DR CTD; 5581; -.
DR MGI; MGI:97599; Prkce.
DR VEuPathDB; HostDB:ENSMUSG00000045038; -.
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000154711; -.
DR HOGENOM; CLU_000288_54_4_1; -.
DR InParanoid; P16054; -.
DR OMA; LEEMEYG; -.
DR OrthoDB; 222529at2759; -.
DR PhylomeDB; P16054; -.
DR TreeFam; TF351133; -.
DR BRENDA; 2.7.11.13; 3474.
DR Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-MMU-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-MMU-1489509; DAG and IP3 signaling.
DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR BioGRID-ORCS; 18754; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Prkce; mouse.
DR PRO; PR:P16054; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P16054; protein.
DR Bgee; ENSMUSG00000045038; Expressed in anterior amygdaloid area and 254 other tissues.
DR ExpressionAtlas; P16054; baseline and differential.
DR Genevisible; P16054; MM.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0071889; F:14-3-3 protein binding; IPI:UniProtKB.
DR GO; GO:0003785; F:actin monomer binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0004699; F:calcium-independent protein kinase C activity; IDA:MGI.
DR GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0035276; F:ethanol binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004697; F:protein kinase C activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0030546; F:signaling receptor activator activity; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:MGI.
DR GO; GO:0071361; P:cellular response to ethanol; IGI:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:MGI.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:MGI.
DR GO; GO:0007635; P:chemosensory behavior; TAS:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0035641; P:locomotory exploration behavior; IGI:MGI.
DR GO; GO:0002281; P:macrophage activation involved in immune response; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; IDA:MGI.
DR GO; GO:0070254; P:mucus secretion; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051562; P:negative regulation of mitochondrial calcium ion concentration; ISO:MGI.
DR GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:ParkinsonsUK-UCL.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:MGI.
DR GO; GO:2001031; P:positive regulation of cellular glucuronidation; ISO:MGI.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0070257; P:positive regulation of mucus secretion; IMP:MGI.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IMP:MGI.
DR GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:MGI.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IDA:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0043278; P:response to morphine; IMP:MGI.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IMP:MGI.
DR GO; GO:0035669; P:TRAM-dependent toll-like receptor 4 signaling pathway; IMP:UniProtKB.
DR CDD; cd00029; C1; 2.
DR CDD; cd05591; STKc_nPKC_epsilon; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR034669; nPKC_epsilon.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR027274; PKC_epsilon.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR014376; Prot_kin_PKC_delta.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000551; PKC_delta; 1.
DR PIRSF; PIRSF501106; Protein_kin_C_epsilon; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell adhesion; Cell cycle; Cell division; Cell membrane;
KW Cytoplasm; Cytoskeleton; Immunity; Kinase; Membrane; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..737
FT /note="Protein kinase C epsilon type"
FT /id="PRO_0000055698"
FT DOMAIN 1..117
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 408..668
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 669..737
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 169..220
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 242..292
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 310..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 223..228
FT /note="Interaction with actin"
FT COMPBIAS 330..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 532
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 414..422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q02156"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18237277"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q02156"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18237277"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine; by GSK3-beta"
FT /evidence="ECO:0000269|PubMed:18604201,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 349
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 350
FT /note="Phosphoserine; by MAPK11 and MAPK14"
FT /evidence="ECO:0000269|PubMed:18604201"
FT MOD_RES 368
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18237277,
FT ECO:0000269|PubMed:18604201"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 566
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:Q02156"
FT MOD_RES 703
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255"
FT MOD_RES 710
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 729
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:17611075"
FT MUTAGEN 346
FT /note="S->A: Loss of interaction with YWHAB and defects in
FT the completion of cytokinesis."
FT /evidence="ECO:0000269|PubMed:18604201"
FT MUTAGEN 368
FT /note="S->A: Loss of interaction with YWHAB and defects in
FT the completion of cytokinesis."
FT /evidence="ECO:0000269|PubMed:18604201"
FT MUTAGEN 729
FT /note="S->A,E,T: Loss of localization to the perinuclear
FT region. Loss of translocation to the nucleus upon PMA
FT stimulation."
FT /evidence="ECO:0000269|PubMed:17611075"
SQ SEQUENCE 737 AA; 83561 MW; 7AEBB8CC10C99F57 CRC64;
MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR IGQTATKQKT
NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI QFEELLQNGS RHFEDWIDLE
PEGKVYVIID LSGSSGEAPK DNEERVFRER MRPRKRQGAV RRRVHQVNGH KFMATYLRQP
TYCSHCRDFI WGVIGKQGYQ CQVCTCVVHK RCHELIITKC AGLKKQETPD EVGSQRFSVN
MPHKFGIHNY KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA
KVLADLGVTP DKITNSGQRR KKLAAGAESP QPASGNSPSE DDRSKSAPTS PCDQELKELE
NNIRKALSFD NRGEEHRASS ATDGQLASPG ENGEVRPGQA KRLGLDEFNF IKVLGKGSFG
KVMLAELKGK DEVYAVKVLK KDVILQDDDV DCTMTEKRIL ALARKHPYLT QLYCCFQTKD
RLFFVMEYVN GGDLMFQIQR SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL
DAEGHCKLAD FGMCKEGIMN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM
MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL GCVAAQNGED
AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ DFTREEPILT LVDEAIIKQI
NQEEFKGFSY FGEDLMP
