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Protein kinase C delta type (EC 2.7.11.13) (nPKC-delta)

 F1P3G1_CHICK            Unreviewed;       699 AA.
F1P3G1;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
03-MAY-2011, sequence version 1.
28-MAR-2018, entry version 59.
RecName: Full=Protein kinase C delta type {ECO:0000256|PIRNR:PIRNR000551};
EC=2.7.11.13 {ECO:0000256|PIRNR:PIRNR000551};
AltName: Full=nPKC-delta {ECO:0000256|PIRNR:PIRNR000551};
Name=PRKCD {ECO:0000313|Ensembl:ENSGALP00000003132};
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00000003132, ECO:0000313|Proteomes:UP000000539};
[1] {ECO:0000313|Ensembl:ENSGALP00000003132, ECO:0000313|Proteomes:UP000000539}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000003132,
ECO:0000313|Proteomes:UP000000539};
PubMed=15592404; DOI=10.1038/nature03154;
International Chicken Genome Sequencing Consortium;
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
Mardis E.R., Wilson R.K.;
"Sequence and comparative analysis of the chicken genome provide
unique perspectives on vertebrate evolution.";
Nature 432:695-716(2004).
[2] {ECO:0000313|Ensembl:ENSGALP00000003132}
IDENTIFICATION.
STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000003132};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- 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.
{ECO:0000256|PIRNR:PIRNR000551}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00935732}.
-!- ENZYME REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are
calcium-insensitive, but activated by diacylglycerol (DAG) and
phosphatidylserine. {ECO:0000256|PIRNR:PIRNR000551}.
-!- SUBUNIT: Interacts with PDPK1 (via N-terminal region), RAD9A,
CDCP1, MUC1 and VASP. {ECO:0000256|PIRNR:PIRNR000551}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000551}.
Cytoplasm, perinuclear region {ECO:0000256|PIRNR:PIRNR000551}.
Nucleus {ECO:0000256|PIRNR:PIRNR000551}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily.
{ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00929254}.
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EMBL; AADN04000453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
ProteinModelPortal; F1P3G1; -.
STRING; 9031.ENSGALP00000003132; -.
PaxDb; F1P3G1; -.
Ensembl; ENSGALT00000003137; ENSGALP00000003132; ENSGALG00000002016.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00820000126964; -.
InParanoid; F1P3G1; -.
OMA; FIFHKVL; -.
OrthoDB; EOG091G0QRS; -.
PhylomeDB; F1P3G1; -.
TreeFam; TF102004; -.
Reactome; R-GGA-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-GGA-111933; Calmodulin induced events.
Reactome; R-GGA-114508; Effects of PIP2 hydrolysis.
Reactome; R-GGA-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-GGA-1489509; DAG and IP3 signaling.
Reactome; R-GGA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-GGA-450520; HuR (ELAVL1) binds and stabilizes mRNA.
Reactome; R-GGA-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-GGA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-GGA-6798695; Neutrophil degranulation.
Reactome; R-GGA-877300; Interferon gamma signaling.
Proteomes; UP000000539; Chromosome 12.
Bgee; ENSGALG00000002016; -.
ExpressionAtlas; F1P3G1; baseline and differential.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008047; F:enzyme activator activity; IEA:Ensembl.
GO; GO:0043560; F:insulin receptor substrate binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071447; P:cellular response to hydroperoxide; IEA:Ensembl.
GO; GO:0090398; P:cellular senescence; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
GO; GO:0016572; P:histone phosphorylation; IEA:Ensembl.
GO; GO:0016064; P:immunoglobulin mediated immune response; IEA:Ensembl.
GO; GO:0032613; P:interleukin-10 production; IEA:Ensembl.
GO; GO:0032615; P:interleukin-12 production; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:Ensembl.
GO; GO:0051490; P:negative regulation of filopodium assembly; IEA:Ensembl.
GO; GO:0034351; P:negative regulation of glial cell apoptotic process; IEA:Ensembl.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0090331; P:negative regulation of platelet aggregation; IEA:Ensembl.
GO; GO:0042119; P:neutrophil activation; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; IEA:Ensembl.
GO; GO:0032079; P:positive regulation of endodeoxyribonuclease activity; IEA:Ensembl.
GO; GO:2000753; P:positive regulation of glucosylceramide catabolic process; IEA:Ensembl.
GO; GO:1900163; P:positive regulation of phospholipid scramblase activity; IEA:Ensembl.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IEA:Ensembl.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IEA:Ensembl.
GO; GO:2000755; P:positive regulation of sphingomyelin catabolic process; IEA:Ensembl.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
GO; GO:0023021; P:termination of signal transduction; IEA:Ensembl.
CDD; cd00029; C1; 2.
CDD; cd05620; STKc_nPKC_delta; 1.
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; IPR034667; nPKC_delta.
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.
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; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 2.
3: Inferred from homology;
Apoptosis {ECO:0000256|PIRNR:PIRNR000551};
ATP-binding {ECO:0000256|PIRNR:PIRNR000551,
ECO:0000256|PIRSR:PIRSR000551-51, ECO:0000256|SAAS:SAAS00593399};
Cell cycle {ECO:0000256|PIRNR:PIRNR000551};
Complete proteome {ECO:0000313|Proteomes:UP000000539};
Cytoplasm {ECO:0000256|PIRNR:PIRNR000551};
Kinase {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00593706};
Metal-binding {ECO:0000256|SAAS:SAAS00732991};
Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000551,
ECO:0000256|PIRSR:PIRSR000551-51, ECO:0000256|SAAS:SAAS00593399};
Nucleus {ECO:0000256|PIRNR:PIRNR000551};
Reference proteome {ECO:0000313|Proteomes:UP000000539};
Repeat {ECO:0000256|SAAS:SAAS01019132};
Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000551,
ECO:0000256|SAAS:SAAS00593706};
Transferase {ECO:0000256|PIRNR:PIRNR000551,
ECO:0000256|SAAS:SAAS00593706}; Zinc {ECO:0000256|SAAS:SAAS00732991};
Zinc-finger {ECO:0000256|SAAS:SAAS00732991}.
DOMAIN 156 206 Phorbol-ester/DAG-type.
{ECO:0000259|PROSITE:PS50081}.
DOMAIN 228 278 Phorbol-ester/DAG-type.
{ECO:0000259|PROSITE:PS50081}.
DOMAIN 357 626 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
DOMAIN 627 698 AGC-kinase C-terminal.
{ECO:0000259|PROSITE:PS51285}.
NP_BIND 363 371 ATP. {ECO:0000256|PIRSR:PIRSR000551-51}.
ACT_SITE 496 496 Proton acceptor.
{ECO:0000256|PIRSR:PIRSR000551-50}.
BINDING 386 386 ATP. {ECO:0000256|PIRSR:PIRSR000551-51}.
SEQUENCE 699 AA; 80178 MW; DB74EE203675878C CRC64;
MAPFLRISFN SFELGPVQNQ GEQLQPFCAI KMKEALTTER GKTLIQRKPT MYPEWKSTFD
AHIYEGRVIQ IVLMKAAEEP LSEVTVGVSV LAERCKKGSG KAEFWLDLQP QGKVLMAVQY
FLEDADCRQS MREEEGTVTI NRRGAIKQAK IHYIKNHEFI ATFFGQPTFC SVCKDFVWGL
NKQGYKCRQC NAAIHKKCID KIIGRCTGTA ANSRDTMFQK ERFNIDMPHR FKVYNYMSPT
FCDHCGSLLW GLVRQGLKCE ECAMNVHHKC QKKVANLCGI NQKLLAEALT QVSQKSTRRS
DSGSVENVGI YQDFDKKPRG PGGDTGDNSQ YDKLWEGSTA KAAPRIASRR KFNIDSFVFH
KVLGKGSFGK VLLAELKGKN EFFAIKALKK DVVLIDDDVE CTMVEKRVLA LAWENPFLTH
LYCTFQTKDH LFFVMEFLNG GDLMFHIQDK GRFDLYRATF YGAEILCGLQ FLHSKGIIYR
KFTSITSEPN WSSFRDLKLD NVMLDKEGHI KIADFGMCKE NVVGENKAST FCGTPDYIAP
EILQGLKYTF SVDWWSFGVL LYEMLIGQSP FHGDDEDELF ESIRVDTPHY PRWITKESKD
LLEKLFERDP TRRLGVTGNI RDHPFFKTIN WTTLEKREID PPFKPKVKSA SDYNNFDREF
LNEKPKLSYS DKNLIDSMDQ SAFAGFSFTN PKFEQILEK


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