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Protein kinase C delta type (EC 2.7.11.13) (Tyrosine-protein kinase PRKCD) (EC 2.7.10.2) (nPKC-delta) [Cleaved into: Protein kinase C delta type regulatory subunit; Protein kinase C delta type catalytic subunit (Sphingosine-dependent protein kinase-1) (SDK1)]

 KPCD_CANLF              Reviewed;         674 AA.
Q5PU49;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 1.
22-NOV-2017, entry version 109.
RecName: Full=Protein kinase C delta type;
EC=2.7.11.13;
AltName: Full=Tyrosine-protein kinase PRKCD;
EC=2.7.10.2;
AltName: Full=nPKC-delta;
Contains:
RecName: Full=Protein kinase C delta type regulatory subunit;
Contains:
RecName: Full=Protein kinase C delta type catalytic subunit;
AltName: Full=Sphingosine-dependent protein kinase-1;
Short=SDK1;
Name=PRKCD;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Hsieh Y.-T., Chen H.-C.;
"Canine protein kinase C delta.";
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Calcium-independent, phospholipid- and diacylglycerol
(DAG)-dependent serine/threonine-protein kinase that plays
contrasting roles in cell death and cell survival by functioning
as a pro-apoptotic protein during DNA damage-induced apoptosis,
but acting as an anti-apoptotic protein during cytokine receptor-
initiated cell death, is involved in tumor suppression, is
required for oxygen radical production by NADPH oxidase and acts
as positive or negative regulator in platelet functional
responses. Upon DNA damage, activates the promoter of the death-
promoting transcription factor BCLAF1/Btf to trigger BCLAF1-
mediated p53/TP53 gene transcription and apoptosis. In response to
oxidative stress, interact with and activate CHUK/IKKA in the
nucleus, causing the phosphorylation of p53/TP53. In the case of
ER stress or DNA damage-induced apoptosis, can form a complex with
the tyrosine-protein kinase ABL1 which trigger apoptosis
independently of p53/TP53. In cytosol can trigger apoptosis by
activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the
level of X-linked inhibitor of apoptosis protein (XIAP), whereas
in nucleus induces apoptosis via the activation of MAPK8 or MAPK9.
Upon ionizing radiation treatment, is required for the activation
of the apoptosis regulators BAX and BAK, which trigger the
mitochondrial cell death pathway. Can phosphorylate MCL1 and
target it for degradation which is sufficient to trigger for BAX
activation and apoptosis. Is required for the control of cell
cycle progression both at G1/S and G2/M phases. Mediates phorbol
12-myristate 13-acetate (PMA)-induced inhibition of cell cycle
progression at G1/S phase by up-regulating the CDK inhibitor
CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In
response to UV irradiation can phosphorylate CDK1, which is
important for the G2/M DNA damage checkpoint activation. Can
protect glioma cells from the apoptosis induced by TNFSF10/TRAIL,
probably by inducing increased phosphorylation and subsequent
activation of AKT1. Can also act as tumor suppressor upon
mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-
leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1
(p47-phox) phosphorylation and activation of NADPH oxidase
activity, and regulates TNF-elicited superoxide anion production
in neutrophils, by direct phosphorylation and activation of NCF1
or indirectly through MAPK1/3 (ERK1/2) signaling pathways. May
also play a role in the regulation of NADPH oxidase activity in
eosinophil after stimulation with IL5, leukotriene B4 or PMA. In
collagen-induced platelet aggregation, acts a negative regulator
of filopodia formation and actin polymerization by interacting
with and negatively regulating VASP phosphorylation. Downstream of
PAR1, PAR4 and CD36/GP4 receptors, regulates differentially
platelet dense granule secretion; acts as a positive regulator in
PAR-mediated granule secretion, whereas it negatively regulates
CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-
terminal and regulates the interaction between MUC1 and beta-
catenin (By similarity). The catalytic subunit phosphorylates 14-
3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent
fashion. Phosphorylates ELAVL1 in response to angiotensin-2
treatment (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10027}.
-!- ENZYME REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are
calcium-insensitive, but activated by diacylglycerol (DAG) and
phosphatidylserine. Three specific sites; Thr-505 (activation loop
of the kinase domain), Ser-643 (turn motif) and Ser-662
(hydrophobic region), need to be phosphorylated for its full
activation. Activated by caspase-3 (CASP3) cleavage during
apoptosis. After cleavage, the pseudosubstrate motif in the
regulatory subunit is released from the substrate recognition site
of the catalytic subunit, which enables PRKCD to become
constitutively activated. The catalytic subunit which displays
properties of a sphingosine-dependent protein kinase is activated
by D-erythro-sphingosine (Sph) or N,N-dimethyl-D-
erythrosphingosine (DMS) or N,N,N-trimethyl-D-erythrosphingosine
(TMS), but not by ceramide or Sph-1-P and is strongly inhibited by
phosphatidylserine (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with PDPK1 (via N-terminal region). Interacts
with RAD9A (By similarity). Interacts with CDCP1. Interacts with
MUC1. Interacts with VASP. Interacts with CAVIN3. Interacts with
PRKD2 (via N-terminus and zing-finger domain 1 and 2) in response
to oxidative stress; the interaction is independent of PRKD2
tyrosine phosphorylation. {ECO:0000250|UniProtKB:P28867,
ECO:0000250|UniProtKB:Q05655}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm,
perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}.
Endoplasmic reticulum {ECO:0000250}. Mitochondrion {ECO:0000250}.
Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
-!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type
region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor.
-!- DOMAIN: The C2 domain is a non-calcium binding domain. It binds
proteins containing phosphotyrosine in a sequence-specific manner
(By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylated and/or phosphorylated at Thr-505, within
the activation loop; phosphorylation at Thr-505 is not a
prerequisite for enzymatic activity. Autophosphorylated at Ser-299
and Ser-302. Upon TNFSF10/TRAIL treatment, phosphorylated at Tyr-
155; phosphorylation is required for its translocation to the
endoplasmic reticulum and cleavage by caspase-3. Phosphorylated at
Tyr-310, Tyr-332 and Tyr-565; phosphorylation of Tyr-310 and Tyr-
565 following thrombin stimulation potentiates its kinase
activity. Phosphorylated by protein kinase PDPK1; phosphorylation
is inhibited by the apoptotic C-terminal cleavage product of PKN2
(By similarity). {ECO:0000250}.
-!- PTM: Proteolytically cleaved into a catalytic subunit and a
regulatory subunit by caspase-3 during apoptosis which results in
kinase activation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY825360; AAV80465.1; -; mRNA.
RefSeq; NP_001008716.1; NM_001008716.1.
UniGene; Cfa.16226; -.
ProteinModelPortal; Q5PU49; -.
STRING; 9615.ENSCAFP00000012799; -.
PaxDb; Q5PU49; -.
GeneID; 494005; -.
KEGG; cfa:494005; -.
CTD; 5580; -.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; Q5PU49; -.
KO; K06068; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
GO; GO:0004697; F:protein kinase C activity; ISS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:1904385; P:cellular response to angiotensin; ISS:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0030837; P:negative regulation of actin filament polymerization; ISS:UniProtKB.
GO; GO:0051490; P:negative regulation of filopodium assembly; ISS:UniProtKB.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; ISS:UniProtKB.
GO; GO:0090331; P:negative regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:UniProtKB.
CDD; cd00029; C1; 2.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR027436; PKC_delta.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR014376; Prot_kin_PKC_delta.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 2.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000551; PKC_delta; 1.
PIRSF; PIRSF501104; Protein_kin_C_delta; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 2.
PROSITE; PS50081; ZF_DAG_PE_2; 2.
2: Evidence at transcript level;
Apoptosis; ATP-binding; Cell cycle; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Kinase; Membrane; Metal-binding; Mitochondrion;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Repeat; Serine/threonine-protein kinase; Transferase;
Tumor suppressor; Zinc; Zinc-finger.
CHAIN 1 674 Protein kinase C delta type.
/FTId=PRO_0000055693.
CHAIN 1 328 Protein kinase C delta type regulatory
subunit. {ECO:0000250}.
/FTId=PRO_0000421665.
CHAIN 329 674 Protein kinase C delta type catalytic
subunit. {ECO:0000250}.
/FTId=PRO_0000421666.
DOMAIN 1 90 C2.
DOMAIN 347 601 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 602 673 AGC-kinase C-terminal.
ZN_FING 158 208 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 230 280 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 353 361 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 471 471 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 376 376 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 48 48 Interaction with phosphotyrosine-
containing peptide. {ECO:0000250}.
SITE 62 62 Interaction with phosphotyrosine-
containing peptide. {ECO:0000250}.
SITE 67 67 Interaction with phosphotyrosine-
containing peptide. {ECO:0000250}.
SITE 123 123 Interaction with phosphotyrosine-
containing peptide. {ECO:0000250}.
SITE 328 329 Cleavage; by caspase-3. {ECO:0000250}.
MOD_RES 43 43 Phosphothreonine.
{ECO:0000250|UniProtKB:P28867}.
MOD_RES 50 50 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 64 64 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09215}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 141 141 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 155 155 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 218 218 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 299 299 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 302 302 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 310 310 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P28867}.
MOD_RES 332 332 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P09215}.
MOD_RES 449 449 Phosphothreonine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 504 504 Phosphoserine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 505 505 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 565 565 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 643 643 Phosphoserine.
{ECO:0000250|UniProtKB:Q05655,
ECO:0000305}.
MOD_RES 652 652 Phosphoserine.
{ECO:0000250|UniProtKB:Q05655}.
MOD_RES 662 662 Phosphoserine.
{ECO:0000250|UniProtKB:Q05655}.
SEQUENCE 674 AA; 77338 MW; 5A25DADDB7A364BA CRC64;
MAPFLRIAFT SYELGSLQAA DEASQPFCAV KMKEALSTER GKTLVQKKPT MYPEWKSTFD
AHIYEGRVIQ IVLMRAAEEP MSEVTVGVSV LAERCKKNNX KAEFWLDLQP QAKVLMSVQY
FLEDIDCRQS MHGEDEAKLP TMNRRGAIKQ AKIHYIKNHE FIATFFGQPT FCSVCKDFVW
GLNKQGYKCR QCNAAIHKKC IDKIIGRCTG TAANSRDTIF QKERFNIDMP HRFKVYNYMS
PTFCDHCGSL LWGLVKQGLK CEDCGMNVHH KCQKKVANLC GINQKLLAEA LNQVTQRSSR
KSETESVGIY QNFERKPGVS GDIAPGEDNG TYGKIWEGST RCNIDNFIFH KVLGKGSFGK
VLLVELKGKK EFFAIKALKK DVVLIDDDVE CTMVEKRVLA LAWENPFLTH LFCTFQTKDH
LFFVMEFLNG GDLMYHIQDK GRFELYRATF YAAEIVCGLQ FLHNKGIIYR DLKLDNVMLD
QDGHIKIADF GMCKENIFGE KQASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML
IGQSPFHGDD EDELFESIRV DTPHYPRWIT KESKDILEKL LERDTTKRLG VTGNIKIHPF
FKTINWTLLE KRAVEPPFKP KVKSPGDYSN FDQEFLNEKA RLSYTDKNLI DSMDQTAFAG
FSFVNPKFER FLEK


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