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Serine/threonine-protein kinase D1 (EC 2.7.11.13) (Protein kinase C mu type) (Protein kinase D) (nPKC-D1) (nPKC-mu)

 KPCD1_HUMAN             Reviewed;         912 AA.
Q15139; A6NL64; B2RAF6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
14-OCT-2008, sequence version 2.
30-AUG-2017, entry version 179.
RecName: Full=Serine/threonine-protein kinase D1;
EC=2.7.11.13;
AltName: Full=Protein kinase C mu type;
AltName: Full=Protein kinase D;
AltName: Full=nPKC-D1;
AltName: Full=nPKC-mu;
Name=PRKD1; Synonyms=PKD, PKD1, PRKCM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8119958;
Johannes F.-J., Prestle J., Eis S., Oberhagemann P., Pfizenmaier K.;
"PKCmu is a novel, atypical member of the protein kinase C family.";
J. Biol. Chem. 269:6140-6148(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION IN EGFR PHOSPHORYLATION.
PubMed=10523301; DOI=10.1093/emboj/18.20.5567;
Bagowski C.P., Stein-Gerlach M., Choidas A., Ullrich A.;
"Cell-type specific phosphorylation of threonines T654 and T669 by PKD
defines the signal capacity of the EGF receptor.";
EMBO J. 18:5567-5576(1999).
[6]
FUNCTION IN APOPTOSIS.
PubMed=10764790; DOI=10.1074/jbc.M002266200;
Endo K., Oki E., Biedermann V., Kojima H., Yoshida K., Johannes F.J.,
Kufe D., Datta R.;
"Proteolytic cleavage and activation of protein kinase C [micro] by
caspase-3 in the apoptotic response of cells to 1-beta -D-
arabinofuranosylcytosine and other genotoxic agents.";
J. Biol. Chem. 275:18476-18481(2000).
[7]
INTERACTION WITH ADAP1.
PubMed=12893243; DOI=10.1016/S0006-291X(03)01187-2;
Zemlickova E., Dubois T., Kerai P., Clokie S., Cronshaw A.D.,
Wakefield R.I.D., Johannes F.-J., Aitken A.;
"Centaurin-alpha(1) associates with and is phosphorylated by isoforms
of protein kinase C.";
Biochem. Biophys. Res. Commun. 307:459-465(2003).
[8]
FUNCTION IN CELL SURVIVAL.
PubMed=12505989; DOI=10.1093/emboj/cdg009;
Storz P., Toker A.;
"Protein kinase D mediates a stress-induced NF-kappaB activation and
survival pathway.";
EMBO J. 22:109-120(2003).
[9]
FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT TYR-432; TYR-463 AND
TYR-502, AND MUTAGENESIS OF TYR-432; TYR-463; TYR-502 AND LYS-612.
PubMed=12637538; DOI=10.1074/jbc.M213224200;
Storz P., Doppler H., Johannes F.J., Toker A.;
"Tyrosine phosphorylation of protein kinase D in the pleckstrin
homology domain leads to activation.";
J. Biol. Chem. 278:17969-17976(2003).
[10]
FUNCTION IN PHOSPHORYLATION OF TRPV1.
PubMed=15471852; DOI=10.1074/jbc.M410331200;
Wang Y., Kedei N., Wang M., Wang Q.J., Huppler A.R., Toth A., Tran R.,
Blumberg P.M.;
"Interaction between protein kinase Cmu and the vanilloid receptor
type 1.";
J. Biol. Chem. 279:53674-53682(2004).
[11]
PHOSPHORYLATION AT TYR-463; SER-738 AND SER-742.
PubMed=15024053; DOI=10.1128/MCB.24.7.2614-2626.2004;
Storz P., Doppler H., Toker A.;
"Protein kinase Cdelta selectively regulates protein kinase D-
dependent activation of NF-kappaB in oxidative stress signaling.";
Mol. Cell. Biol. 24:2614-2626(2004).
[12]
PHOSPHORYLATION BY DAPK1, INTERACTION WITH DAPK1, PHOSPHORYLATION AT
SER-910, AND ENZYME REGULATION.
PubMed=17703233; DOI=10.1038/sj.cdd.4402212;
Eisenberg-Lerner A., Kimchi A.;
"DAP kinase regulates JNK signaling by binding and activating protein
kinase D under oxidative stress.";
Cell Death Differ. 14:1908-1915(2007).
[13]
PHOSPHORYLATION AT TYR-95.
PubMed=17804414; DOI=10.1074/jbc.M703584200;
Doppler H., Storz P.;
"A novel tyrosine phosphorylation site in protein kinase D contributes
to oxidative stress-mediated activation.";
J. Biol. Chem. 282:31873-31881(2007).
[14]
FUNCTION IN INNATE IMMUNITY.
PubMed=17442957; DOI=10.4049/jimmunol.178.9.5735;
Ivison S.M., Graham N.R., Bernales C.Q., Kifayet A., Ng N.,
Shobab L.A., Steiner T.S.;
"Protein kinase D interaction with TLR5 is required for inflammatory
signaling in response to bacterial flagellin.";
J. Immunol. 178:5735-5743(2007).
[15]
ENZYME REGULATION, PHORBOL-ESTER BINDING, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF PRO-157 AND PRO-281.
PubMed=18076381; DOI=10.1042/BJ20071334;
Chen J., Deng F., Li J., Wang Q.J.;
"Selective binding of phorbol esters and diacylglycerol by individual
C1 domains of the PKD family.";
Biochem. J. 411:333-342(2008).
[16]
FUNCTION IN PHOSPHORYLATION OF HDAC5, AND FUNCTION IN ANGIOGENESIS.
PubMed=18332134; DOI=10.1074/jbc.M800264200;
Ha C.H., Wang W., Jhun B.S., Wong C., Hausser A., Pfizenmaier K.,
McKinsey T.A., Olson E.N., Jin Z.G.;
"Protein kinase D-dependent phosphorylation and nuclear export of
histone deacetylase 5 mediates vascular endothelial growth factor-
induced gene expression and angiogenesis.";
J. Biol. Chem. 283:14590-14599(2008).
[17]
FUNCTION IN PHOSPHORYLATION OF HDAC7.
PubMed=18509061; DOI=10.1073/pnas.0802857105;
Wang S., Li X., Parra M., Verdin E., Bassel-Duby R., Olson E.N.;
"Control of endothelial cell proliferation and migration by VEGF
signaling to histone deacetylase 7.";
Proc. Natl. Acad. Sci. U.S.A. 105:7738-7743(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
PHOSPHORYLATION AT SER-397 AND SER-401, INTERACTION WITH MAPK13, AND
FUNCTION.
PubMed=19135240; DOI=10.1016/j.cell.2008.11.018;
Sumara G., Formentini I., Collins S., Sumara I., Windak R.,
Bodenmiller B., Ramracheya R., Caille D., Jiang H., Platt K.A.,
Meda P., Aebersold R., Rorsman P., Ricci R.;
"Regulation of PKD by the MAPK p38delta in insulin secretion and
glucose homeostasis.";
Cell 136:235-248(2009).
[20]
FUNCTION IN ANGIOGENESIS.
PubMed=19211839; DOI=10.1091/mbc.E08-09-0957;
Czoendoer K., Ellwanger K., Fuchs Y.F., Lutz S., Gulyas M.,
Mansuy I.M., Hausser A., Pfizenmaier K., Schlett K.;
"Protein kinase D controls the integrity of Golgi apparatus and the
maintenance of dendritic arborization in hippocampal neurons.";
Mol. Biol. Cell 20:2108-2120(2009).
[21]
REVIEW ON FUNCTION IN TRAFFICKING.
PubMed=11978539; DOI=10.1016/S0962-8924(02)02262-6;
Van Lint J., Rykx A., Maeda Y., Vantus T., Sturany S., Malhotra V.,
Vandenheede J.R., Seufferlein T.;
"Protein kinase D: an intracellular traffic regulator on the move.";
Trends Cell Biol. 12:193-200(2002).
[22]
REVIEW ON FUNCTION.
PubMed=15701647; DOI=10.1074/jbc.R500002200;
Rozengurt E., Rey O., Waldron R.T.;
"Protein kinase D signaling.";
J. Biol. Chem. 280:13205-13208(2005).
[23]
REVIEW ON FUNCTION.
PubMed=18239146; DOI=10.1161/CIRCRESAHA.107.168211;
Avkiran M., Rowland A.J., Cuello F., Haworth R.S.;
"Protein kinase d in the cardiovascular system: emerging roles in
health and disease.";
Circ. Res. 102:157-163(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-345; SER-448
AND SER-473, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[25]
REVIEW ON FUNCTION IN ANGIOGENESIS.
PubMed=19655095; DOI=10.1007/s10059-009-0109-9;
Ha C.H., Jin Z.G.;
"Protein kinase D1, a new molecular player in VEGF signaling and
angiogenesis.";
Mol. Cells 28:1-5(2009).
[26]
REVIEW ON FUNCTION.
PubMed=21357900; DOI=10.1152/physiol.00037.2010;
Rozengurt E.;
"Protein kinase D signaling: multiple biological functions in health
and disease.";
Physiology (Bethesda) 26:23-33(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205 AND SER-208, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
FUNCTION, INTERACTION WITH USP28, AND INDUCTION.
PubMed=24623306; DOI=10.7554/eLife.02313;
Serra R.W., Fang M., Park S.M., Hutchinson L., Green M.R.;
"A KRAS-directed transcriptional silencing pathway that mediates the
CpG island methylator phenotype.";
Elife 3:E02313-E02313(2014).
[29]
VARIANTS [LARGE SCALE ANALYSIS] TYR-152 AND LYS-857.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[30]
VARIANTS [LARGE SCALE ANALYSIS] PRO-225; GLN-478; SER-585; MET-677;
LEU-679 AND ARG-891.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[31]
INVOLVEMENT IN CHDED, AND VARIANTS CHDED TRP-299 AND ARG-592.
PubMed=27479907; DOI=10.1038/ng.3627;
INTERVAL Study;
UK10K Consortium;
Deciphering Developmental Disorders Study;
Sifrim A., Hitz M.P., Wilsdon A., Breckpot J., Turki S.H.,
Thienpont B., McRae J., Fitzgerald T.W., Singh T., Swaminathan G.J.,
Prigmore E., Rajan D., Abdul-Khaliq H., Banka S., Bauer U.M.,
Bentham J., Berger F., Bhattacharya S., Bu'Lock F., Canham N.,
Colgiu I.G., Cosgrove C., Cox H., Daehnert I., Daly A., Danesh J.,
Fryer A., Gewillig M., Hobson E., Hoff K., Homfray T., Kahlert A.K.,
Ketley A., Kramer H.H., Lachlan K., Lampe A.K., Louw J.J.,
Manickara A.K., Manase D., McCarthy K.P., Metcalfe K., Moore C.,
Newbury-Ecob R., Omer S.O., Ouwehand W.H., Park S.M., Parker M.J.,
Pickardt T., Pollard M.O., Robert L., Roberts D.J., Sambrook J.,
Setchfield K., Stiller B., Thornborough C., Toka O., Watkins H.,
Williams D., Wright M., Mital S., Daubeney P.E., Keavney B.,
Goodship J., Abu-Sulaiman R.M., Klaassen S., Wright C.F., Firth H.V.,
Barrett J.C., Devriendt K., FitzPatrick D.R., Brook J.D., Hurles M.E.;
"Distinct genetic architectures for syndromic and nonsyndromic
congenital heart defects identified by exome sequencing.";
Nat. Genet. 48:1060-1065(2016).
-!- FUNCTION: Serine/threonine-protein kinase that converts transient
diacylglycerol (DAG) signals into prolonged physiological effects
downstream of PKC, and is involved in the regulation of MAPK8/JNK1
and Ras signaling, Golgi membrane integrity and trafficking, cell
survival through NF-kappa-B activation, cell migration, cell
differentiation by mediating HDAC7 nuclear export, cell
proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in
cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced
apoptosis and flagellin-stimulated inflammatory response.
Phosphorylates the epidermal growth factor receptor (EGFR) on dual
threonine residues, which leads to the suppression of epidermal
growth factor (EGF)-induced MAPK8/JNK1 activation and subsequent
JUN phosphorylation. Phosphorylates RIN1, inducing RIN1 binding to
14-3-3 proteins YWHAB, YWHAE and YWHAZ and increased competition
with RAF1 for binding to GTP-bound form of Ras proteins (NRAS,
HRAS and KRAS). Acts downstream of the heterotrimeric G-protein
beta/gamma-subunit complex to maintain the structural integrity of
the Golgi membranes, and is required for protein transport along
the secretory pathway. In the trans-Golgi network (TGN), regulates
the fission of transport vesicles that are on their way to the
plasma membrane. May act by activating the lipid kinase
phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the
local synthesis of phosphorylated inositol lipids, which induces a
sequential production of DAG, phosphatidic acid (PA) and lyso-PA
(LPA) that are necessary for membrane fission and generation of
specific transport carriers to the cell surface. Under oxidative
stress, is phosphorylated at Tyr-463 via SRC-ABL1 and contributes
to cell survival by activating IKK complex and subsequent nuclear
translocation and activation of NFKB1. Involved in cell migration
by regulating integrin alpha-5/beta-3 recycling and promoting its
recruitment in newly forming focal adhesion. In osteoblast
differentiation, mediates the bone morphogenetic protein 2 (BMP2)-
induced nuclear export of HDAC7, which results in the inhibition
of HDAC7 transcriptional repression of RUNX2. In neurons, plays an
important role in neuronal polarity by regulating the biogenesis
of TGN-derived dendritic vesicles, and is involved in the
maintenance of dendritic arborization and Golgi structure in
hippocampal cells. May potentiate mitogenesis induced by the
neuropeptide bombesin or vasopressin by mediating an increase in
the duration of MAPK1/3 (ERK1/2) signaling, which leads to
accumulation of immediate-early gene products including FOS that
stimulate cell cycle progression. Plays an important role in the
proliferative response induced by low calcium in keratinocytes,
through sustained activation of MAPK1/3 (ERK1/2) pathway.
Downstream of novel PKC signaling, plays a role in cardiac
hypertrophy by phosphorylating HDAC5, which in turn triggers
XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A transcriptional
activation and induction of downstream target genes that promote
myocyte hypertrophy and pathological cardiac remodeling. Mediates
cardiac troponin I (TNNI3) phosphorylation at the PKA sites, which
results in reduced myofilament calcium sensitivity, and
accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway
is also involved in angiogenesis by mediating VEGFA-induced
specific subset of gene expression, cell migration, and tube
formation. In response to VEGFA, is necessary and required for
HDAC7 phosphorylation which induces HDAC7 nuclear export and
endothelial cell proliferation and migration. During apoptosis
induced by cytarabine and other genotoxic agents, PRKD1 is cleaved
by caspase-3 at Asp-378, resulting in activation of its kinase
function and increased sensitivity of cells to the cytotoxic
effects of genotoxic agents. In epithelial cells, is required for
transducing flagellin-stimulated inflammatory responses by binding
and phosphorylating TLR5, which contributes to MAPK14/p38
activation and production of inflammatory cytokines. May play a
role in inflammatory response by mediating activation of NF-kappa-
B. May be involved in pain transmission by directly modulating
TRPV1 receptor. Plays a role in activated KRAS-mediated
stabilization of ZNF304 in colorectal cancer (CRC) cells
(PubMed:24623306). Regulates nuclear translocation of
transcription factor TFEB in macrophages upon live S.enterica
infection (By similarity). {ECO:0000250|UniProtKB:Q62101,
ECO:0000269|PubMed:10523301, ECO:0000269|PubMed:10764790,
ECO:0000269|PubMed:12505989, ECO:0000269|PubMed:12637538,
ECO:0000269|PubMed:15471852, ECO:0000269|PubMed:17442957,
ECO:0000269|PubMed:18332134, ECO:0000269|PubMed:18509061,
ECO:0000269|PubMed:19135240, ECO:0000269|PubMed:19211839,
ECO:0000269|PubMed:24623306}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Activated by DAG and phorbol esters. Phorbol-
ester/DAG-type domain 1 binds DAG with high affinity and appears
to play the dominant role in mediating translocation to the cell
membrane and trans-Golgi network. Phorbol-ester/DAG-type domain 2
binds phorbol ester with higher affinity. Autophosphorylation of
Ser-742 and phosphorylation of Ser-738 by PKC relieves auto-
inhibition by the PH domain. Phosphorylation on Tyr-463 by the
SRC-ABL1 pathway in response to oxidative stress, is also required
for activation. Activated by DAPK1 under oxidative stress.
{ECO:0000269|PubMed:12637538, ECO:0000269|PubMed:17703233,
ECO:0000269|PubMed:18076381}.
-!- SUBUNIT: Interacts (via N-terminus) with ADAP1/CENTA1
(PubMed:12893243). Interacts with MAPK13 (PubMed:19135240).
Interacts with DAPK1 in an oxidative stress-regulated manner
(PubMed:17703233). Interacts with USP28; the interaction induces
phosphorylation of USP28 and activated KRAS-mediated stabilization
of ZNF304 (PubMed:24623306). Interacts with AKAP13 (via C-terminal
domain) (By similarity). {ECO:0000250|UniProtKB:Q62101,
ECO:0000269|PubMed:12893243, ECO:0000269|PubMed:17703233,
ECO:0000269|PubMed:19135240, ECO:0000269|PubMed:24623306}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1181072, EBI-1181072;
Q07021:C1QBP; NbExp=9; IntAct=EBI-1181072, EBI-347528;
P12830:CDH1; NbExp=7; IntAct=EBI-1181072, EBI-727477;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-1181072, EBI-352572;
O15264:MAPK13; NbExp=6; IntAct=EBI-1181072, EBI-2116951;
P02795:MT2A; NbExp=7; IntAct=EBI-1181072, EBI-996616;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18076381}.
Cell membrane {ECO:0000269|PubMed:18076381}. Golgi apparatus,
trans-Golgi network {ECO:0000250|UniProtKB:Q62101}.
Note=Translocation to the cell membrane is required for kinase
activation.
-!- INDUCTION: Up-regulated by the intestine-specific transcription
factor CDX1 in a activated KRAS-dependent manner in colorectal
cancer (CRC) cells (PubMed:24623306).
{ECO:0000269|PubMed:24623306}.
-!- PTM: Phosphorylated at Ser-397 and Ser-401 by MAPK13 during
regulation of insulin secretion in pancreatic beta cells
(PubMed:19135240). Phosphorylated by DAPK1 (PubMed:17703233).
Phosphorylated at Tyr-95 and by ABL at Tyr-463, which primes the
kinase in response to oxidative stress, and promotes a second step
activating phosphorylation at Ser-738/Ser-742 by PKRD
(PubMed:12637538, PubMed:15024053, PubMed:17804414).
Phosphorylated on Ser-910 upon S.enterica infection in macrophages
(By similarity). {ECO:0000250|UniProtKB:Q62101,
ECO:0000269|PubMed:12637538, ECO:0000269|PubMed:15024053,
ECO:0000269|PubMed:17703233, ECO:0000269|PubMed:17804414,
ECO:0000269|PubMed:19135240}.
-!- DISEASE: Congenital heart defects and ectodermal dysplasia (CHDED)
[MIM:617364]: An autosomal dominant syndrome characterized by
atrial and/or ventricular septal congenital heart defects and
variable features of ectodermal dysplasia, including sparse hair,
dry skin, thin skin, fragile nails, premature loss of primary
teeth, and small widely spaced teeth. Patients manifest
developmental disabilities ranging from motor delay and delayed
speech to global developmental retardation.
{ECO:0000269|PubMed:27479907}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. PKD subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PRKCMID41860ch14q11.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X75756; CAA53384.1; -; mRNA.
EMBL; AK314170; BAG36853.1; -; mRNA.
EMBL; AL135858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471078; EAW65971.1; -; Genomic_DNA.
CCDS; CCDS9637.1; -.
PIR; A53215; A53215.
RefSeq; NP_002733.2; NM_002742.2.
UniGene; Hs.508999; -.
ProteinModelPortal; Q15139; -.
SMR; Q15139; -.
BioGrid; 111573; 34.
DIP; DIP-38481N; -.
IntAct; Q15139; 8.
MINT; MINT-88491; -.
STRING; 9606.ENSP00000333568; -.
BindingDB; Q15139; -.
ChEMBL; CHEMBL3863; -.
GuidetoPHARMACOLOGY; 1489; -.
iPTMnet; Q15139; -.
PhosphoSitePlus; Q15139; -.
BioMuta; PRKD1; -.
DMDM; 209572639; -.
EPD; Q15139; -.
MaxQB; Q15139; -.
PaxDb; Q15139; -.
PeptideAtlas; Q15139; -.
PRIDE; Q15139; -.
DNASU; 5587; -.
Ensembl; ENST00000331968; ENSP00000333568; ENSG00000184304.
Ensembl; ENST00000616995; ENSP00000482645; ENSG00000184304.
GeneID; 5587; -.
KEGG; hsa:5587; -.
UCSC; uc001wqh.4; human.
CTD; 5587; -.
DisGeNET; 5587; -.
GeneCards; PRKD1; -.
H-InvDB; HIX0037727; -.
HGNC; HGNC:9407; PRKD1.
HPA; CAB018367; -.
HPA; HPA029834; -.
MalaCards; PRKD1; -.
MIM; 605435; gene.
MIM; 617364; phenotype.
neXtProt; NX_Q15139; -.
OpenTargets; ENSG00000184304; -.
PharmGKB; PA33771; -.
eggNOG; KOG4236; Eukaryota.
eggNOG; ENOG410XQZ3; LUCA.
GeneTree; ENSGT00840000129794; -.
HOVERGEN; HBG003564; -.
InParanoid; Q15139; -.
KO; K06070; -.
PhylomeDB; Q15139; -.
TreeFam; TF314320; -.
BRENDA; 2.7.11.13; 2681.
Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
SignaLink; Q15139; -.
SIGNOR; Q15139; -.
ChiTaRS; PRKD1; human.
GeneWiki; Protein_kinase_D1; -.
GenomeRNAi; 5587; -.
PRO; PR:Q15139; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000184304; -.
CleanEx; HS_PKD1; -.
CleanEx; HS_PRKD1; -.
ExpressionAtlas; Q15139; baseline and differential.
Genevisible; Q15139; HS.
GO; GO:0000421; C:autophagosome membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:CACAO.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004697; F:protein kinase C activity; IDA:CACAO.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0034198; P:cellular response to amino acid starvation; IMP:ParkinsonsUK-UCL.
GO; GO:0071447; P:cellular response to hydroperoxide; IMP:ParkinsonsUK-UCL.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:UniProtKB.
GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO; GO:0048193; P:Golgi vesicle transport; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; IMP:BHF-UCL.
GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
GO; GO:0045806; P:negative regulation of endocytosis; TAS:BHF-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IMP:BHF-UCL.
GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IGI:BHF-UCL.
GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IMP:BHF-UCL.
GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IGI:BHF-UCL.
GO; GO:1901727; P:positive regulation of histone deacetylase activity; IGI:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IGI:BHF-UCL.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IC:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0089700; P:protein kinase D signaling; IGI:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0007265; P:Ras protein signal transduction; IMP:UniProtKB.
GO; GO:2001044; P:regulation of integrin-mediated signaling pathway; TAS:BHF-UCL.
GO; GO:0010837; P:regulation of keratinocyte proliferation; ISS:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
CDD; cd00029; C1; 2.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR015727; Protein_Kinase_C_mu-related.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR22968; PTHR22968; 1.
Pfam; PF00130; C1_1; 2.
Pfam; PF00169; PH; 1.
Pfam; PF00069; Pkinase; 1.
PIRSF; PIRSF000552; PKC_mu_nu_D2; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00233; PH; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50003; PH_DOMAIN; 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.
1: Evidence at protein level;
Angiogenesis; Apoptosis; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; Differentiation; Disease mutation;
Ectodermal dysplasia; Golgi apparatus; Immunity;
Inflammatory response; Innate immunity; Kinase; Magnesium; Membrane;
Metal-binding; Neurogenesis; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
CHAIN 1 912 Serine/threonine-protein kinase D1.
/FTId=PRO_0000055714.
DOMAIN 422 541 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 583 839 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 146 196 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 270 320 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 589 597 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 17 26 Poly-Ala.
COMPBIAS 200 203 Poly-Arg.
ACT_SITE 706 706 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 612 612 ATP.
MOD_RES 95 95 Phosphotyrosine.
{ECO:0000269|PubMed:17804414}.
MOD_RES 205 205 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:21406692}.
MOD_RES 208 208 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 397 397 Phosphoserine; by MAPK13.
{ECO:0000269|PubMed:19135240}.
MOD_RES 401 401 Phosphoserine; by MAPK13.
{ECO:0000269|PubMed:19135240}.
MOD_RES 432 432 Phosphotyrosine.
{ECO:0000269|PubMed:12637538}.
MOD_RES 448 448 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 463 463 Phosphotyrosine; by ABL.
{ECO:0000269|PubMed:12637538,
ECO:0000269|PubMed:15024053}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 502 502 Phosphotyrosine.
{ECO:0000269|PubMed:12637538}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K1Y2}.
MOD_RES 738 738 Phosphoserine; by PKC/PRKCD.
{ECO:0000269|PubMed:15024053}.
MOD_RES 742 742 Phosphoserine; by autocatalysis and
PKC/PRKCD. {ECO:0000269|PubMed:15024053}.
MOD_RES 910 910 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:17703233}.
VARIANT 152 152 H -> Y (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035468.
VARIANT 225 225 S -> P. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_042324.
VARIANT 299 299 L -> W (in CHDED).
{ECO:0000269|PubMed:27479907}.
/FTId=VAR_078602.
VARIANT 478 478 K -> Q (in dbSNP:rs55852813).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042325.
VARIANT 585 585 P -> S (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042326.
VARIANT 592 592 G -> R (in CHDED).
{ECO:0000269|PubMed:27479907}.
/FTId=VAR_078603.
VARIANT 677 677 R -> M (in a lung bronchoalveolar
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042327.
VARIANT 679 679 P -> L (in dbSNP:rs34588699).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042328.
VARIANT 825 825 R -> K (in dbSNP:rs11161065).
/FTId=VAR_046988.
VARIANT 857 857 E -> K (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035469.
VARIANT 891 891 H -> R (in dbSNP:rs45582934).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042329.
MUTAGEN 157 157 P->G: Increase in ability to bind phorbol
ester, loss of ability to bind DAG.
{ECO:0000269|PubMed:18076381}.
MUTAGEN 281 281 P->G: No effect on ability to bind
phorbol ester, slight increase in ability
to bind DAG.
{ECO:0000269|PubMed:18076381}.
MUTAGEN 432 432 Y->E: Decreased phosphorylation level
when coexpressed with SRC in HeLa cells.
Unchanged phosphorylation level when
coexpressed with ABL.
{ECO:0000269|PubMed:12637538}.
MUTAGEN 432 432 Y->F: Decreased phosphorylation level
when coexpressed with SRC in HeLa cells.
Unchanged phosphorylation level when
coexpressed with ABL. Unaltered kinase
activity. Decreased kinase activity; when
associated with F-463 and F-502.
{ECO:0000269|PubMed:12637538}.
MUTAGEN 463 463 Y->E: Constitutive activation and
constitutive phosphorylation of S-738 and
S-742. {ECO:0000269|PubMed:12637538}.
MUTAGEN 463 463 Y->F: Decreased phosphorylation level
when coexpressed with either SRC or ABL
in HeLa cells. Decreased kinase activity.
{ECO:0000269|PubMed:12637538}.
MUTAGEN 502 502 Y->E: Loss of activation.
{ECO:0000269|PubMed:12637538}.
MUTAGEN 502 502 Y->F: Decreased phosphorylation level
when coexpressed with SRC in HeLa cells.
Unchanged phosphorylation level when
coexpressed with ABL. Unaltered kinase
activity. Decreased kinase activity; when
associated with F-432 and F-502.
{ECO:0000269|PubMed:12637538}.
MUTAGEN 612 612 K->W: Loss of kinase activity.
{ECO:0000269|PubMed:12637538}.
CONFLICT 135 135 A -> R (in Ref. 1; CAA53384).
{ECO:0000305}.
CONFLICT 877 877 G -> R (in Ref. 1; CAA53384).
{ECO:0000305}.
SEQUENCE 912 AA; 101704 MW; 0BC9414C335D2DBB CRC64;
MSAPPVLRPP SPLLPVAAAA AAAAAALVPG SGPGPAPFLA PVAAPVGGIS FHLQIGLSRE
PVLLLQDSSG DYSLAHVREM ACSIVDQKFP ECGFYGMYDK ILLFRHDPTS ENILQLVKAA
SDIQEGDLIE VVLSASATFE DFQIRPHALF VHSYRAPAFC DHCGEMLWGL VRQGLKCEGC
GLNYHKRCAF KIPNNCSGVR RRRLSNVSLT GVSTIRTSSA ELSTSAPDEP LLQKSPSESF
IGREKRSNSQ SYIGRPIHLD KILMSKVKVP HTFVIHSYTR PTVCQYCKKL LKGLFRQGLQ
CKDCRFNCHK RCAPKVPNNC LGEVTINGDL LSPGAESDVV MEEGSDDNDS ERNSGLMDDM
EEAMVQDAEM AMAECQNDSG EMQDPDPDHE DANRTISPST SNNIPLMRVV QSVKHTKRKS
STVMKEGWMV HYTSKDTLRK RHYWRLDSKC ITLFQNDTGS RYYKEIPLSE ILSLEPVKTS
ALIPNGANPH CFEITTANVV YYVGENVVNP SSPSPNNSVL TSGVGADVAR MWEIAIQHAL
MPVIPKGSSV GTGTNLHRDI SVSISVSNCQ IQENVDISTV YQIFPDEVLG SGQFGIVYGG
KHRKTGRDVA IKIIDKLRFP TKQESQLRNE VAILQNLHHP GVVNLECMFE TPERVFVVME
KLHGDMLEMI LSSEKGRLPE HITKFLITQI LVALRHLHFK NIVHCDLKPE NVLLASADPF
PQVKLCDFGF ARIIGEKSFR RSVVGTPAYL APEVLRNKGY NRSLDMWSVG VIIYVSLSGT
FPFNEDEDIH DQIQNAAFMY PPNPWKEISH EAIDLINNLL QVKMRKRYSV DKTLSHPWLQ
DYQTWLDLRE LECKIGERYI THESDDLRWE KYAGEQGLQY PTHLINPSAS HSDTPETEET
EMKALGERVS IL


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