KPCD_RAT
ID KPCD_RAT Reviewed; 673 AA.
AC P09215; Q6DG48; Q9JK29; Q9JL03;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Protein kinase C delta type {ECO:0000305};
DE EC=2.7.11.13 {ECO:0000250|UniProtKB:Q05655};
DE AltName: Full=nPKC-delta;
DE Contains:
DE RecName: Full=Protein kinase C delta type regulatory subunit;
DE Contains:
DE RecName: Full=Protein kinase C delta type catalytic subunit;
DE AltName: Full=Sphingosine-dependent protein kinase-1;
DE Short=SDK1;
GN Name=Prkcd {ECO:0000312|RGD:67383}; Synonyms=Pkcd;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=2834397; DOI=10.1016/s0021-9258(18)68732-0;
RA Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.;
RT "The structure, expression, and properties of additional members of the
RT protein kinase C family.";
RL J. Biol. Chem. 263:6927-6932(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar Kyoto;
RX PubMed=10721703; DOI=10.1016/s0378-1119(99)00539-9;
RA Kurkinen K.M.A., Keinanen R.A., Karhu R., Koistinaho J.;
RT "Genomic structure and chromosomal localization of the rat PKCdelta-gene.";
RL Gene 242:115-123(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10708593; DOI=10.1006/bbrc.2000.2331;
RA Ueyama T., Ren Y., Ohmori S., Sakai K., Tamaki N., Saito N.;
RT "cDNA cloning of an alternative splicing variant of protein kinase C delta
RT (PKC deltaIII), a new truncated form of PKCdelta, in rats.";
RL Biochem. Biophys. Res. Commun. 269:557-563(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 123-286.
RX PubMed=3691811; DOI=10.1016/0014-5793(87)80564-1;
RA Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.;
RT "Identification of three additional members of rat protein kinase C family:
RT delta-, epsilon- and zeta-subspecies.";
RL FEBS Lett. 226:125-128(1987).
RN [6]
RP PROTEIN SEQUENCE OF 142-153.
RX PubMed=1915352; DOI=10.1111/j.1432-1033.1991.tb16248.x;
RA Olivier A.R., Parker P.J.;
RT "Expression and characterization of protein kinase C-delta.";
RL Eur. J. Biochem. 200:805-810(1991).
RN [7]
RP MUTAGENESIS OF THR-505, AND PHOSPHORYLATION AT THR-505.
RX PubMed=9677322; DOI=10.1042/bj3330631;
RA Garcia-Paramio P., Cabrerizo Y., Bornancin F., Parker P.J.;
RT "The broad specificity of dominant inhibitory protein kinase C mutants
RT infers a common step in phosphorylation.";
RL Biochem. J. 333:631-636(1998).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, CLEAVAGE BY CASPASE-3, AND ACTIVITY
RP REGULATION.
RX PubMed=12855683; DOI=10.1074/jbc.m305294200;
RA Hamaguchi A., Suzuki E., Murayama K., Fujimura T., Hikita T., Iwabuchi K.,
RA Handa K., Withers D.A., Masters S.C., Fu H., Hakomori S.;
RT "Sphingosine-dependent protein kinase-1, directed to 14-3-3, is identified
RT as the kinase domain of protein kinase C delta.";
RL J. Biol. Chem. 278:41557-41565(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [10]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-64 AND TYR-155.
RX PubMed=17562707; DOI=10.1074/jbc.m703661200;
RA DeVries-Seimon T.A., Ohm A.M., Humphries M.J., Reyland M.E.;
RT "Induction of apoptosis is driven by nuclear retention of protein kinase C
RT delta.";
RL J. Biol. Chem. 282:22307-22314(2007).
RN [11]
RP PHOSPHORYLATION AT THR-505.
RX PubMed=17569658; DOI=10.1074/jbc.m701676200;
RA Rybin V.O., Guo J., Gertsberg Z., Elouardighi H., Steinberg S.F.;
RT "Protein kinase Cepsilon (PKCepsilon) and Src control PKCdelta activation
RT loop phosphorylation in cardiomyocytes.";
RL J. Biol. Chem. 282:23631-23638(2007).
RN [12]
RP PHOSPHORYLATION AT TYR-311; TYR-332 AND THR-505.
RX PubMed=18550549; DOI=10.1074/jbc.m802396200;
RA Sumandea M.P., Rybin V.O., Hinken A.C., Wang C., Kobayashi T., Harleton E.,
RA Sievert G., Balke C.W., Feinmark S.J., Solaro R.J., Steinberg S.F.;
RT "Tyrosine phosphorylation modifies protein kinase C delta-dependent
RT phosphorylation of cardiac troponin I.";
RL J. Biol. Chem. 283:22680-22689(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311; SER-643 AND SER-662, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-123.
RX PubMed=9687370; DOI=10.1016/s0969-2126(98)00090-2;
RA Pappa H., Murray-Rust J., Dekker L.V., Parker P.J., McDonald N.Q.;
RT "Crystal structure of the C2 domain from protein kinase C-delta.";
RL Structure 6:885-894(1998).
CC -!- FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-
CC dependent serine/threonine-protein kinase that plays contrasting roles
CC in cell death and cell survival by functioning as a pro-apoptotic
CC protein during DNA damage-induced apoptosis, but acting as an anti-
CC apoptotic protein during cytokine receptor-initiated cell death, is
CC involved in tumor suppression, is required for oxygen radical
CC production by NADPH oxidase and acts as positive or negative regulator
CC in platelet functional responses. Upon DNA damage, activates the
CC promoter of the death-promoting transcription factor BCLAF1/Btf to
CC trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In
CC response to oxidative stress, interact with and activate CHUK/IKKA in
CC the nucleus, causing the phosphorylation of p53/TP53. In the case of ER
CC stress or DNA damage-induced apoptosis, can form a complex with the
CC tyrosine-protein kinase ABL1 which trigger apoptosis independently of
CC p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or
CC MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor
CC of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via
CC the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is
CC required for the activation of the apoptosis regulators BAX and BAK,
CC which trigger the mitochondrial cell death pathway. Can phosphorylate
CC MCL1 and target it for degradation which is sufficient to trigger for
CC BAX activation and apoptosis. Is required for the control of cell cycle
CC progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate
CC 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S
CC phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the
CC cyclin CCNA2 promoter activity. In response to UV irradiation can
CC phosphorylate CDK1, which is important for the G2/M DNA damage
CC checkpoint activation. Can protect glioma cells from the apoptosis
CC induced by TNFSF10/TRAIL, probably by inducing increased
CC phosphorylation and subsequent activation of AKT1. Can also act as
CC tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-
CC formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required
CC for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase
CC activity, and regulates TNF-elicited superoxide anion production in
CC neutrophils, by direct phosphorylation and activation of NCF1 or
CC indirectly through MAPK1/3 (ERK1/2) signaling pathways. Involved in
CC antifungal immunity by mediating phosphorylation and activation of
CC CARD9 downstream of C-type lectin receptors activation, promoting
CC interaction between CARD9 and BCL10, followed by activation of NF-
CC kappa-B and MAP kinase p38 pathways (By similarity). May also play a
CC role in the regulation of NADPH oxidase activity in eosinophil after
CC stimulation with IL5, leukotriene B4 or PMA. In collagen-induced
CC platelet aggregation, acts a negative regulator of filopodia formation
CC and actin polymerization by interacting with and negatively regulating
CC VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors,
CC regulates differentially platelet dense granule secretion; acts as a
CC positive regulator in PAR-mediated granule secretion, whereas it
CC negatively regulates CD36/GP4-mediated granule release. Phosphorylates
CC MUC1 in the C-terminal and regulates the interaction between MUC1 and
CC beta-catenin (By similarity). The catalytic subunit phosphorylates 14-
CC 3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent
CC fashion. Phosphorylates ELAVL1 in response to angiotensin-2 treatment
CC (By similarity). Phosphorylates mitochondrial phospholipid scramblase 3
CC (PLSCR3), resulting in increased cardiolipin expression on the
CC mitochondrial outer membrane which facilitates apoptosis (By
CC similarity). Phosphorylates SMPD1 which induces SMPD1 secretion (By
CC similarity). {ECO:0000250|UniProtKB:P28867,
CC ECO:0000250|UniProtKB:Q05655}.
CC -!- FUNCTION: Truncated isoform 2 is inactive.
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; Evidence={ECO:0000250|UniProtKB:Q05655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10027};
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-505 (activation loop of
CC the kinase domain), Ser-643 (turn motif) and Ser-662 (hydrophobic
CC region), need to be phosphorylated for its full activation. Activated
CC by caspase-3 (CASP3) cleavage during apoptosis. After cleavage, the
CC pseudosubstrate motif in the regulatory subunit is released from the
CC substrate recognition site of the catalytic subunit, which enables
CC PRKCD to become constitutively activated. The catalytic subunit which
CC displays properties of a sphingosine-dependent protein kinase is
CC activated by D-erythro-sphingosine (Sph) or N,N-dimethyl-D-
CC erythrosphingosine (DMS) or N,N,N-trimethyl-D-erythrosphingosine (TMS),
CC but not by ceramide or Sph-1-P and is strongly inhibited by
CC phosphatidylserine. {ECO:0000269|PubMed:12855683}.
CC -!- SUBUNIT: Interacts with PDPK1 (via N-terminal region). Interacts with
CC RAD9A (By similarity). Interacts with CDCP1. Interacts with MUC1.
CC Interacts with VASP. Interacts with CAVIN3. Interacts with PRKD2 (via
CC N-terminus and zing-finger domain 1 and 2) in response to oxidative
CC stress; the interaction is independent of PRKD2 tyrosine
CC phosphorylation (By similarity). Interacts with PLSC3; interaction is
CC enhanced by UV irradiation (By similarity).
CC {ECO:0000250|UniProtKB:P28867, ECO:0000250|UniProtKB:Q05655}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17562707}. Nucleus
CC {ECO:0000269|PubMed:17562707}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:17562707}. Cell membrane
CC {ECO:0000250|UniProtKB:Q05655}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q05655}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q05655}. Endomembrane system
CC {ECO:0000250|UniProtKB:Q05655}. Note=Translocates to the mitochondria
CC upon apoptotic stimulation. Upon activation, translocates to the plasma
CC membrane followed by partial location to the endolysosomes.
CC {ECO:0000250|UniProtKB:Q05655}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PKC-delta-I;
CC IsoId=P09215-1; Sequence=Displayed;
CC Name=2; Synonyms=PKC-delta-III;
CC IsoId=P09215-2; Sequence=VSP_004742;
CC -!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type region 1
CC (C1A) and 2 (C1B), is the diacylglycerol sensor.
CC -!- DOMAIN: The C2 domain is a non-calcium binding domain. It binds
CC proteins containing phosphotyrosine in a sequence-specific manner (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated and/or phosphorylated at Thr-505, within the
CC activation loop; phosphorylation at Thr-505 is not a prerequisite for
CC enzymatic activity (PubMed:9677322, PubMed:17569658).
CC Autophosphorylated at Ser-299 (By similarity). Upon TNFSF10/TRAIL
CC treatment, phosphorylated at Tyr-155; phosphorylation is required for
CC its translocation to the endoplasmic reticulum and cleavage by caspase-
CC 3 (PubMed:17562707). Phosphorylated at Tyr-311, Tyr-332 and Tyr-565;
CC phosphorylation of Tyr-311 and Tyr-565 following thrombin or zymosan
CC stimulation potentiates its kinase activity (PubMed:18550549).
CC Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by
CC the apoptotic C-terminal cleavage product of PKN2 (By similarity).
CC Phosphorylated at Tyr-311 and Tyr-332 by SRC; phosphorylation leads to
CC enhanced autophosphorylation at Thr-505 (PubMed:18550549).
CC Phosphorylated at Tyr-311 through a SYK and SRC mechanism downstream of
CC C-type lectin receptors activation, promoting its activation (By
CC similarity). {ECO:0000250|UniProtKB:P28867,
CC ECO:0000250|UniProtKB:Q05655, ECO:0000269|PubMed:17562707,
CC ECO:0000269|PubMed:17569658, ECO:0000269|PubMed:18550549,
CC ECO:0000269|PubMed:9677322}.
CC -!- PTM: Proteolytically cleaved into a catalytic subunit and a regulatory
CC subunit by caspase-3 during apoptosis which results in kinase
CC activation. {ECO:0000269|PubMed:12855683}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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; M18330; AAA41871.1; -; mRNA.
DR EMBL; AJ230617; CAB75578.1; -; Genomic_DNA.
DR EMBL; AJ230618; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230619; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230620; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230621; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230622; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230623; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230624; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230625; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230626; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230627; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230628; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230629; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230630; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230631; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230632; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AJ230633; CAB75578.1; JOINED; Genomic_DNA.
DR EMBL; AF219629; AAF32345.1; -; mRNA.
DR EMBL; BC076505; AAH76505.1; -; mRNA.
DR PIR; A28163; KIRTCD.
DR RefSeq; NP_579841.1; NM_133307.1. [P09215-1]
DR PDB; 1BDY; X-ray; 2.20 A; A/B=1-123.
DR PDBsum; 1BDY; -.
DR AlphaFoldDB; P09215; -.
DR SMR; P09215; -.
DR BioGRID; 250924; 10.
DR IntAct; P09215; 6.
DR STRING; 10116.ENSRNOP00000025858; -.
DR BindingDB; P09215; -.
DR ChEMBL; CHEMBL3633; -.
DR DrugCentral; P09215; -.
DR iPTMnet; P09215; -.
DR PhosphoSitePlus; P09215; -.
DR jPOST; P09215; -.
DR PaxDb; P09215; -.
DR PRIDE; P09215; -.
DR GeneID; 170538; -.
DR KEGG; rno:170538; -.
DR UCSC; RGD:67383; rat. [P09215-1]
DR CTD; 5580; -.
DR RGD; 67383; Prkcd.
DR eggNOG; KOG0694; Eukaryota.
DR InParanoid; P09215; -.
DR OrthoDB; 222529at2759; -.
DR PhylomeDB; P09215; -.
DR BRENDA; 2.7.11.13; 5301.
DR Reactome; R-RNO-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-RNO-111933; Calmodulin induced events.
DR Reactome; R-RNO-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-RNO-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-RNO-1489509; DAG and IP3 signaling.
DR Reactome; R-RNO-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-RNO-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-RNO-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-RNO-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-877300; Interferon gamma signaling.
DR EvolutionaryTrace; P09215; -.
DR PRO; PR:P09215; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0036019; C:endolysosome; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
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:RGD.
DR GO; GO:0008047; F:enzyme activator activity; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0043560; F:insulin receptor substrate binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0004697; F:protein kinase C activity; EXP:Reactome.
DR GO; GO:0106310; F:protein serine kinase activity; ISS:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0070976; F:TIR domain binding; IPI:BHF-UCL.
DR GO; GO:0032147; P:activation of protein kinase activity; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006915; P:apoptotic process; IMP:CACAO.
DR GO; GO:0042100; P:B cell proliferation; ISO:RGD.
DR GO; GO:0060326; P:cell chemotaxis; ISO:RGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1904385; P:cellular response to angiotensin; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; IEP:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:RGD.
DR GO; GO:0071447; P:cellular response to hydroperoxide; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:CACAO.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; ISO:RGD.
DR GO; GO:0032963; P:collagen metabolic process; IMP:RGD.
DR GO; GO:0070779; P:D-aspartate import across plasma membrane; IMP:RGD.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0016572; P:histone phosphorylation; ISO:RGD.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0051490; P:negative regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:RGD.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
DR GO; GO:0042119; P:neutrophil activation; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; ISO:RGD.
DR GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; ISO:RGD.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:RGD.
DR GO; GO:2000753; P:positive regulation of glucosylceramide catabolic process; ISO:RGD.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:RGD.
DR GO; GO:1900163; P:positive regulation of phospholipid scramblase activity; ISO:RGD.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:RGD.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:RGD.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISO:RGD.
DR GO; GO:2000755; P:positive regulation of sphingomyelin catabolic process; ISO:RGD.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:RGD.
DR GO; GO:2000303; P:regulation of ceramide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0042325; P:regulation of phosphorylation; IDA:CACAO.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0023021; P:termination of signal transduction; ISO:RGD.
DR CDD; cd00029; C1; 2.
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; IPR002219; PE/DAG-bd.
DR InterPro; IPR027436; PKC_delta.
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; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000551; PKC_delta; 1.
DR PIRSF; PIRSF501104; Protein_kin_C_delta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
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 3D-structure; Alternative splicing; Apoptosis; ATP-binding; Cell cycle;
KW Cell membrane; Cytoplasm; Direct protein sequencing; Kinase; Membrane;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase;
KW Tumor suppressor; Zinc; Zinc-finger.
FT CHAIN 1..673
FT /note="Protein kinase C delta type"
FT /id="PRO_0000055696"
FT CHAIN 1..327
FT /note="Protein kinase C delta type regulatory subunit"
FT /id="PRO_0000421671"
FT CHAIN 328..673
FT /note="Protein kinase C delta type catalytic subunit"
FT /id="PRO_0000421672"
FT DOMAIN 1..106
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 347..601
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 602..673
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 158..208
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 230..280
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ACT_SITE 471
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 353..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 48
FT /note="Interaction with phosphotyrosine-containing peptide"
FT /evidence="ECO:0000250"
FT SITE 62
FT /note="Interaction with phosphotyrosine-containing peptide"
FT /evidence="ECO:0000250"
FT SITE 67
FT /note="Interaction with phosphotyrosine-containing peptide"
FT /evidence="ECO:0000250"
FT SITE 123
FT /note="Interaction with phosphotyrosine-containing peptide"
FT /evidence="ECO:0000250"
FT SITE 327..328
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000305"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28867"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05655"
FT MOD_RES 64
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17562707"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05655"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05655"
FT MOD_RES 155
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:17562707"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05655"
FT MOD_RES 299
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q05655"
FT MOD_RES 311
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:18550549,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 332
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:18550549"
FT MOD_RES 372
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q05655"
FT MOD_RES 449
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05655"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05655"
FT MOD_RES 505
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:17569658,
FT ECO:0000269|PubMed:18550549, ECO:0000269|PubMed:9677322"
FT MOD_RES 565
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q05655"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05655"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16396499,
FT ECO:0007744|PubMed:22673903"
FT VAR_SEQ 327..673
FT /note="DNNGTYGKIWEGSNRCRLENFTFQKVLGKGSFGKVLLAELKGKERYFAIKYL
FT KKDVVLIDDDVECTMVEKRVLALAWENPFLTHLICTFQTKDHLFFVMEFLNGGDLMFHI
FT QDKGRFELYRATFYAAEIICGLQFLHGKGIIYRDLKLDNVMLDKDGHIKIADFGMCKEN
FT IFGENRASTFCGTPDYIAPEILQGLKYSFSVDWWSFGVLLYEMLIGQSPFHGDDEDELF
FT ESIRVDTPHYPRWITKESKDIMEKLFERDPAKRLGVTGNIRLHPFFKTINWNLLEKRKV
FT EPPFKPKVKSPSDYSNFDPEFLNEKPQLSFSDKNLIDSMDQTAFKGFSFVNPKYEQFLE
FT -> GESGSHIPLKLPFPDRAREKNSSETWDKTTTGPMARSGRGATGAALRTSPSRKYLA
FT KAALARYCLQN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10708593"
FT /id="VSP_004742"
FT MUTAGEN 505
FT /note="T->A: Decrease in the phosphorylation level."
FT /evidence="ECO:0000269|PubMed:9677322"
FT CONFLICT 147
FT /note="A -> S (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="T -> S (in Ref. 2; CAB75578 and 4; AAH76505)"
FT /evidence="ECO:0000305"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:1BDY"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:1BDY"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1BDY"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1BDY"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1BDY"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:1BDY"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:1BDY"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:1BDY"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:1BDY"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1BDY"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1BDY"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:1BDY"
SQ SEQUENCE 673 AA; 77520 MW; D2C767E55863A23C CRC64;
MAPFLRISFN SYELGSLQAE DDASQPFCAV KMKEALTTDR GKTLVQKKPT MYPEWKSTFD
AHIYEGRVIQ IVLMRAAEDP MSEVTVGVSV LAERCKKNNG KAEFWLDLQP QAKVLMCVQY
FLEDGDCKQS MRSEEEAMFP TMNRRGAIKQ AKIHYIKNHE FIATFFGQPT FCSVCKEFVW
GLNKQGYKCR QCNAAIHKKC IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS
PTFCDHCGTL LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQKASR
KPETPETVGI YQGFEKKTAV SGNDIPDNNG TYGKIWEGSN RCRLENFTFQ KVLGKGSFGK
VLLAELKGKE RYFAIKYLKK DVVLIDDDVE CTMVEKRVLA LAWENPFLTH LICTFQTKDH
LFFVMEFLNG GDLMFHIQDK GRFELYRATF YAAEIICGLQ FLHGKGIIYR DLKLDNVMLD
KDGHIKIADF GMCKENIFGE NRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML
IGQSPFHGDD EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPAKRLG VTGNIRLHPF
FKTINWNLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI DSMDQTAFKG
FSFVNPKYEQ FLE
