ID Q6DUV1_RAT Unreviewed; 737 AA. AC Q6DUV1; F1LMV8; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 27-MAR-2024, entry version 145. DE RecName: Full=Protein kinase C epsilon type {ECO:0000256|PIRNR:PIRNR000551}; DE EC=2.7.11.13 {ECO:0000256|PIRNR:PIRNR000551}; DE AltName: Full=nPKC-epsilon {ECO:0000256|PIRNR:PIRNR000551}; GN Name=Prkce {ECO:0000313|Ensembl:ENSRNOP00000020959.8, GN ECO:0000313|RGD:61925}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:AAT65503.1}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000020959.8, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000020959.8, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|EMBL:AAT65503.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Wistar {ECO:0000313|EMBL:AAT65503.1}; RC TISSUE=Liver {ECO:0000313|EMBL:AAT65503.1}; RA Burchfield J.G., Schmitz-Peiffer C., Biden T.J.; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0007829|PubMed:22673903} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [4] {ECO:0000313|Ensembl:ENSRNOP00000020959.8} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000020959.8}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. 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. {ECO:0000256|PIRNR:PIRNR000551}. 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 Evidence={ECO:0000256|ARBA:ARBA00000946}; 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; Evidence={ECO:0000256|ARBA:ARBA00000569, CC ECO:0000256|PIRNR:PIRNR000551}; CC -!- ACTIVITY REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are CC calcium-insensitive, but activated by diacylglycerol (DAG) and CC phosphatidylserine. {ECO:0000256|PIRNR:PIRNR000551}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000551}. CC Cytoplasm, cytoskeleton {ECO:0000256|PIRNR:PIRNR000551}. Cell membrane CC {ECO:0000256|PIRNR:PIRNR000551}. Cytoplasm, perinuclear region CC {ECO:0000256|PIRNR:PIRNR000551}. Nucleus CC {ECO:0000256|PIRNR:PIRNR000551}. Note=Translocated to plasma membrane CC in epithelial cells stimulated by HGF. Associated with the Golgi at the CC perinuclear site in pre-passage fibroblasts. In passaging cells, CC translocated to the cell periphery. Translocated to the nucleus in PMA- CC treated cells. {ECO:0000256|PIRNR:PIRNR000551}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490, CC ECO:0000256|PIRNR:PIRNR000551}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY642593; AAT65503.1; -; mRNA. DR RefSeq; NP_058867.1; NM_017171.1. DR Ensembl; ENSRNOT00000020959.8; ENSRNOP00000020959.8; ENSRNOG00000015603.8. DR GeneID; 29340; -. DR KEGG; rno:29340; -. DR CTD; 5581; -. DR RGD; 61925; Prkce. DR VEuPathDB; HostDB:ENSRNOG00000015603; -. DR GeneTree; ENSGT00940000154711; -. DR HOGENOM; CLU_000288_54_4_1; -. DR OMA; VARICTC; -. DR OrthoDB; 841660at2759; -. DR TreeFam; TF351133; -. DR Proteomes; UP000002494; Chromosome 6. DR Bgee; ENSRNOG00000015603; Expressed in frontal cortex and 19 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; IEA:GOC. DR GO; GO:0071889; F:14-3-3 protein binding; IEA:Ensembl. DR GO; GO:0003785; F:actin monomer binding; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004699; F:diacylglycerol-dependent, calcium-independent serine/threonine kinase activity; IEA:Ensembl. DR GO; GO:0008047; F:enzyme activator activity; IEA:Ensembl. DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl. DR GO; GO:0035276; F:ethanol binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030546; F:signaling receptor activator activity; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl. DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl. DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl. DR GO; GO:0002281; P:macrophage activation involved in immune response; IEA:Ensembl. DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl. DR GO; GO:0070254; P:mucus secretion; IEA:Ensembl. DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl. DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl. DR GO; GO:2001031; P:positive regulation of cellular glucuronidation; IEA:Ensembl. DR GO; GO:0032467; P:positive regulation of cytokinesis; IEA:Ensembl. DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl. DR GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl. DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl. DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IEA:Ensembl. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl. DR GO; GO:0070257; P:positive regulation of mucus secretion; IEA:Ensembl. DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IEA:Ensembl. DR GO; GO:0090303; P:positive regulation of wound healing; IEA:Ensembl. DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl. DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl. DR GO; GO:0043278; P:response to morphine; IEA:Ensembl. DR GO; GO:0051932; P:synaptic transmission, GABAergic; IEA:Ensembl. DR GO; GO:0035669; P:TRAM-dependent toll-like receptor 4 signaling pathway; IEA:Ensembl. DR CDD; cd20835; C1_nPKC_epsilon-like_rpt1; 1. DR CDD; cd20838; C1_nPKC_epsilon-like_rpt2; 1. DR CDD; cd04014; C2_PKC_epsilon; 1. DR CDD; cd05591; STKc_nPKC_epsilon; 1. DR Gene3D; 3.30.60.20; -; 2. DR Gene3D; 2.60.40.150; C2 domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR24351:SF182; PROTEIN KINASE C EPSILON TYPE; 1. DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1. 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; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. 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; 1. DR PROSITE; PS50081; ZF_DAG_PE_2; 2. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000551}; KW Cell adhesion {ECO:0000256|PIRNR:PIRNR000551}; KW Cell cycle {ECO:0000256|PIRNR:PIRNR000551}; KW Cell division {ECO:0000256|PIRNR:PIRNR000551}; KW Cell membrane {ECO:0000256|PIRNR:PIRNR000551}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000551}; KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR000551}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000551}; KW Membrane {ECO:0000256|PIRNR:PIRNR000551}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR000551}; Nucleus {ECO:0000256|PIRNR:PIRNR000551}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q6DUV1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|PIRNR:PIRNR000551}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000551}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 1..117 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT DOMAIN 169..220 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT DOMAIN 242..292 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000259|PROSITE:PS50081" FT DOMAIN 408..668 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT DOMAIN 669..737 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000259|PROSITE:PS51285" FT REGION 310..356 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 369..398 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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:0000256|PIRSR:PIRSR000551-50" FT BINDING 414..422 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51" FT BINDING 437 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51, FT ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 737 AA; 83576 MW; CF77776819A26333 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 STDGQLASPG ENGEVRQGQA KRLGLDEFNF IKVLGKGSFG KVMLAELKGK DEVYAVKVLK KDVILQDDDV DCTMTEKRIL ALARKHPYLT QLYCCFQTKD RLFFVMEYVN GGDLMFQIQR SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL DAEGHCKLAD FGMCKEGILN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL GCVAAQNGED AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ DFTREEPILT LVDEAIVKQI NQEEFKGFSY FGEDLMP //