EKS-MUM-00175

Eukaryotic Protein Kinase & Protein Phosphatase Database

Tag

Content

EKPD ID

EKS-MUM-00175

Classification

Group/Family	Score	E-Value	Start	End	Domain Length
AGC/PKC	472.0	1.3E-141	408	668	261

Status

Reviewed

Ensembl Protein

ENSMUSP00000094873

UniProt Accession

P16054;

Protein Name

Protein kinase C epsilon type

Protein Synonyms/Alias

nPKC-epsilon;

Gene Name

Prkce

Gene Synonyms/Alias

Prkce; Pkce, Pkcea;

Ensembl Information

Ensembl Gene ID	Ensembl Protein ID	Ensembl Transcript ID
ENSMUSG00000045038	ENSMUSP00000094873	ENSMUST00000097274
ENSMUSG00000045038	ENSMUSP00000094874	ENSMUST00000097275

Organism

Mus musculus

Functional Description

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.

Protein Length

737

Protein Sequence
(FASTA)

MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR IGQTATKQKT 60

NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI QFEELLQNGS RHFEDWIDLE 120

PEGKVYVIID LSGSSGEAPK DNEERVFRER MRPRKRQGAV RRRVHQVNGH KFMATYLRQP 180

TYCSHCRDFI WGVIGKQGYQ CQVCTCVVHK RCHELIITKC AGLKKQETPD EVGSQRFSVN 240

MPHKFGIHNY KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA 300

KVLADLGVTP DKITNSGQRR KKLAAGAESP QPASGNSPSE DDRSKSAPTS PCDQELKELE 360

NNIRKALSFD NRGEEHRASS ATDGQLASPG ENGEVRPGQA KRLGLDEFNF IKVLGKGSFG 420

KVMLAELKGK DEVYAVKVLK KDVILQDDDV DCTMTEKRIL ALARKHPYLT QLYCCFQTKD 480

RLFFVMEYVN GGDLMFQIQR SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL 540

DAEGHCKLAD FGMCKEGIMN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM 600

MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL GCVAAQNGED 660

AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ DFTREEPILT LVDEAIIKQI 720

NQEEFKGFSY FGEDLMP 737

Nucleotide Sequence
(FASTA)

ATGGTAGTGT TCAATGGCCT TCTTAAGATC AAAATCTGCG AGGCGGTGAG CTTGAAGCCC 60

ACAGCCTGGT CGCTGCGCCA TGCGGTGGGA CCCCGGCCAC AGACGTTCCT TTTGGACCCC 120

TACATTGCCC TTAACGTGGA CGACTCGCGC ATCGGCCAAA CAGCCACCAA GCAAAAGACC 180

AACAGCCCGG CCTGGCACGA TGAGTTCGTC ACCGATGTGT GCAATGGGCG CAAGATCGAG 240

CTGGCTGTCT TTCACGACGC TCCTATCGGC TACGACGACT TCGTGGCCAA CTGCACCATC 300

CAGTTCGAGG AGCTGCTGCA GAATGGGAGC CGTCACTTCG AGGACTGGAT TGACCTGGAG 360

CCAGAAGGAA AAGTGTACGT GATCATCGAT CTCTCGGGAT CATCGGGTGA AGCCCCTAAA 420

GACAATGAAG AACGAGTGTT CAGGGAGCGT ATGCGGCCAA GGAAGCGGCA AGGGGCTGTC 480

AGGCGCAGGG TCCACCAGGT CAATGGCCAC AAGTTCATGG CCACCTACTT GCGGCAACCC 540

ACCTACTGCT CCCACTGCAG AGATTTCATC TGGGGTGTCA TAGGAAAACA GGGATATCAA 600

TGTCAAGTTT GCACTTGCGT TGTCCACAAG CGATGTCATG AGCTCATTAT TACAAAGTGC 660

GCTGGGCTGA AGAAACAGGA AACCCCTGAC GAGGTGGGCT CCCAACGGTT CAGCGTCAAC 720

ATGCCCCACA AGTTCGGGAT CCACAACTAC AAGGTCCCCA CGTTCTGTGA CCACTGTGGG 780

TCCCTGCTCT GGGGCCTCTT GCGGCAGGGC TTGCAGTGTA AAGTCTGCAA AATGAATGTT 840

CACCGGCGAT GTGAGACCAA TGTGGCTCCC AACTGTGGGG TAGACGCCAG AGGAATTGCC 900

AAAGTGCTGG CTGACCTTGG TGTTACTCCA GACAAAATCA CCAACAGTGG CCAAAGGAGG 960

AAAAAGCTCG CTGCTGGTGC TGAGTCCCCA CAGCCGGCTT CTGGAAACTC CCCATCTGAA 1020

GACGACCGAT CCAAGTCAGC GCCCACCTCC CCTTGTGACC AGGAACTAAA AGAACTTGAA 1080

AACAACATTC GGAAGGCCTT GTCATTTGAC AACCGAGGAG AGGAGCACCG AGCGTCGTCG 1140

GCCACCGATG GCCAGCTGGC AAGCCCCGGA GAGAACGGGG AAGTCCGGCC AGGCCAGGCC 1200

AAGCGCTTGG GGCTGGATGA GTTCAACTTC ATCAAGGTGT TGGGCAAAGG CAGCTTTGGC 1260

AAGGTCATGT TGGCGGAACT CAAAGGCAAA GATGAAGTCT ACGCTGTGAA GGTCTTGAAG 1320

AAGGACGTTA TCCTACAAGA CGATGATGTG GACTGCACAA TGACAGAGAA GAGGATTTTG 1380

GCTCTGGCTC GGAAACACCC TTATCTAACC CAACTCTATT GCTGCTTCCA GACCAAGGAC 1440

CGCCTCTTCT TCGTCATGGA ATATGTAAAT GGTGGAGACC TCATGTTCCA GATTCAGCGG 1500

TCCCGAAAAT TTGATGAGCC TCGTTCTCGG TTCTATGCCG CAGAGGTCAC ATCAGCCCTC 1560

ATGTTTCTCC ACCAGCACGG AGTGATCTAC AGGGATTTGA AACTGGACAA CATCCTTCTA 1620

GATGCAGAAG GCCACTGCAA GCTGGCTGAC TTTGGGATGT GCAAGGAAGG GATTATGAAT 1680

GGTGTGACAA CTACCACCTT CTGTGGGACT CCTGACTACA TAGCTCCAGA GATCCTACAG 1740

GAGTTGGAGT ACGGCCCCTC AGTGGACTGG TGGGCCCTGG GGGTGCTGAT GTACGAGATG 1800

ATGGCTGGGC AGCCCCCCTT TGAAGCTGAC AACGAGGACG ACTTGTTCGA ATCCATCCTT 1860

CATGATGATG TTCTCTATCC TGTCTGGCTT AGCAAGGAAG CTGTCAGCAT CCTGAAAGCT 1920

TTCATGACCA AGAACCCGCA CAAGCGCCTG GGCTGTGTGG CAGCGCAGAA CGGGGAGGAC 1980

GCCATCAAGC AACATCCATT CTTCAAGGAG ATTGACTGGG TACTGCTGGA GCAGAAGAAA 2040

ATCAAGCCCC CCTTCAAGCC GAGAATTAAA ACCAAAAGAG ATGTCAATAA CTTTGACCAA 2100

GACTTTACGC GGGAAGAGCC AATACTTACA CTTGTGGATG AAGCAATCAT TAAGCAGATC 2160

AACCAGGAAG AATTCAAAGG CTTCTCCTAC TTTGGTGAAG ACCTGATGCC CTGA 2214

Domain Profile

S: 1     fellkvlGkGsfgkvllaelkktdelyaikvlkkdvvlqdddveltlvekrvlalaskkp  60

         f+++kvlGkGsfgkv+laelk++de+ya+kvlkkdv+lqdddv++t++ekr+lala+k+p

Q: 408   FNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHP  467

         99**********************************************************

S: 61    flvqlfscfqtedrlffvleyvnGGdlmfhiqkarklkeerarfyaaeiilalkflhekg  120

         +l+ql++cfqt+drlffv+eyvnGGdlmf+iq++rk++e+r+rfyaae+++al+flh++g

Q: 468   YLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSRFYAAEVTSALMFLHQHG  527

         ************************************************************

S: 121   iiyrdlkldnvlldaeGhikladfGlckeeilegkttstfcGtPdyiaPeilkeeeygks  180

         +iyrdlkldn+lldaeGh+kladfG+cke+i++g tt+tfcGtPdyiaPeil+e eyg s

Q: 528   VIYRDLKLDNILLDAEGHCKLADFGMCKEGIMNGVTTTTFCGTPDYIAPEILQELEYGPS  587

         ************************************************************

S: 181   vdwwalGvllyemlagqsPfegededelfesilekevlyPkslskeaveilkglltkdpe  240

         vdwwalGvl+yem+agq+Pfe+++ed+lfesil+++vlyP++lskeav+ilk+++tk+p+

Q: 588   VDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPH  647

         ************************************************************

S: 241   krlGv..keegeedikehaff  259

         krlG+  +++ge++ik+h+ff

Q: 648   KRLGCvaAQNGEDAIKQHPFF  668

         *****6449***********9

Domain Sequence
(FASTA)

FNFIKVLGKG SFGKVMLAEL KGKDEVYAVK VLKKDVILQD DDVDCTMTEK RILALARKHP 60

YLTQLYCCFQ TKDRLFFVME YVNGGDLMFQ IQRSRKFDEP RSRFYAAEVT SALMFLHQHG 120

VIYRDLKLDN ILLDAEGHCK LADFGMCKEG IMNGVTTTTF CGTPDYIAPE ILQELEYGPS 180

VDWWALGVLM YEMMAGQPPF EADNEDDLFE SILHDDVLYP VWLSKEAVSI LKAFMTKNPH 240

KRLGCVAAQN GEDAIKQHPF F 261

Keyword

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.

Sequence Source

Ensembl

Orthology

Ortholog group

Ailuropoda melanoleuca"; ?>Anolis carolinensis"; ?>Bos taurus"; ?>Caenorhabditis elegans"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Danio rerio"; ?>Drosophila melanogaster"; ?>Felis catus"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Homo sapiens"; ?>Ictidomys tridecemlineatus"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Meleagris gallopavo"; ?>Microcebus murinus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Rattus norvegicus"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tarsius syrichta"; ?>Tetraodon nigroviridis"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>Saccharomyces cerevisiae"; ?>

Gene Ontology

GO:0071944	; C:cell periphery
GO:0005856	; C:cytoskeleton
GO:0005829	; C:cytosol
GO:0005783	; C:endoplasmic reticulum
GO:0000139	; C:Golgi membrane
GO:0016020	; C:membrane
GO:0005739	; C:mitochondrion
GO:0005634	; C:nucleus
GO:0048471	; C:perinuclear region of cytoplasm
GO:0005886	; C:plasma membrane
GO:0003785	; F:actin monomer binding
GO:0005524	; F:ATP binding
GO:0004699	; F:calcium-independent protein kinase C activity
GO:0008047	; F:enzyme activator activity
GO:0035276	; F:ethanol binding
GO:0046872	; F:metal ion binding
GO:0030546	; F:receptor activator activity
GO:0007155	; P:cell adhesion
GO:0007049	; P:cell cycle
GO:0051301	; P:cell division
GO:0071361	; P:cellular response to ethanol
GO:0071456	; P:cellular response to hypoxia
GO:0007635	; P:chemosensory behavior
GO:0035556	; P:intracellular signal transduction
GO:0031663	; P:lipopolysaccharide-mediated signaling pathway
GO:0035641	; P:locomotory exploration behavior
GO:0002281	; P:macrophage activation involved in immune response
GO:0030838	; P:positive regulation of actin filament polymerization
GO:0071777	; P:positive regulation of cell cycle cytokinesis
GO:0010811	; P:positive regulation of cell-substrate adhesion
GO:2001031	; P:positive regulation of cellular glucuronidation
GO:0010634	; P:positive regulation of epithelial cell migration
GO:0010763	; P:positive regulation of fibroblast migration
GO:0043123	; P:positive regulation of I-kappaB kinase/NF-kappaB cascade
GO:0032024	; P:positive regulation of insulin secretion
GO:0050996	; P:positive regulation of lipid catabolic process
GO:0043410	; P:positive regulation of MAPK cascade
GO:0070257	; P:positive regulation of mucus secretion
GO:0032230	; P:positive regulation of synaptic transmission, GABAergic
GO:0090303	; P:positive regulation of wound healing
GO:0061178	; P:regulation of insulin secretion involved in cellular response to glucose stimulus
GO:0050730	; P:regulation of peptidyl-tyrosine phosphorylation
GO:0051209	; P:release of sequestered calcium ion into cytosol
GO:0043278	; P:response to morphine
GO:0035669	; P:TRAM-dependent toll-like receptor 4 signaling pathway

KEGG

mmu:18754

;

InterPros

IPR000961	; AGC-kinase_C.
IPR000008	; C2_Ca-dep.
IPR008973	; C2_Ca/lipid-bd_dom_CaLB.
IPR018029	; C2_membr_targeting.
IPR020454	; DAG/PE-bd.
IPR011009	; Kinase-like_dom.
IPR017892	; Pkinase_C.
IPR014376	; Prot_kin_PKC_delta.
IPR002219	; Prot_Kinase_C-like_PE/DAG-bd.
IPR000719	; Prot_kinase_cat_dom.
IPR017441	; Protein_kinase_ATP_BS.
IPR002290	; Ser/Thr_dual-sp_kinase_dom.
IPR008271	; Ser/Thr_kinase_AS.

Pfam

PF00130	; C1_1; 2.
PF00168	; C2; 1.
PF00069	; Pkinase; 1.
PF00433	; Pkinase_C; 1.

SMARTs

SM00109	; C1; 2.
SM00239	; C2; 1.
SM00133	; S_TK_X; 1.
SM00220	; S_TKc; 1.

Prosites

PS51285	; AGC_KINASE_CTER; 1.
PS50004	; C2; 1.
PS00107	; PROTEIN_KINASE_ATP; 1.
PS50011	; PROTEIN_KINASE_DOM; 1.
PS00108	; PROTEIN_KINASE_ST; 1.
PS00479	; ZF_DAG_PE_1; 2.
PS50081	; ZF_DAG_PE_2; 2.

Prints

PR00008

; DAGPEDOMAIN.

Created Date

20-Feb-2013