KPCD1_RAT
ID KPCD1_RAT Reviewed; 918 AA.
AC Q9WTQ1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Serine/threonine-protein kinase D1;
DE EC=2.7.11.13;
DE AltName: Full=Protein kinase C mu type;
DE AltName: Full=Protein kinase D;
DE AltName: Full=nPKC-D1;
DE AltName: Full=nPKC-mu;
GN Name=Prkd1; Synonyms=Pkcm, Pkd, Prkcm;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 718-864.
RC STRAIN=Wistar; TISSUE=Brain;
RA Minami H., Owada Y., Kondo H.;
RT "Rat PKC mu mRNA partial cds.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION IN GOLGI REGULATION.
RX PubMed=10412981; DOI=10.1016/s0092-8674(00)80606-6;
RA Jamora C., Yamanouye N., Van Lint J., Laudenslager J., Vandenheede J.R.,
RA Faulkner D.J., Malhotra V.;
RT "Gbetagamma-mediated regulation of Golgi organization is through the direct
RT activation of protein kinase D.";
RL Cell 98:59-68(1999).
RN [4]
RP FUNCTION IN CARDIOMYOCYTE.
RX PubMed=15514163; DOI=10.1161/01.res.0000149299.34793.3c;
RA Haworth R.S., Cuello F., Herron T.J., Franzen G., Kentish J.C., Gautel M.,
RA Avkiran M.;
RT "Protein kinase D is a novel mediator of cardiac troponin I phosphorylation
RT and regulates myofilament function.";
RL Circ. Res. 95:1091-1099(2004).
RN [5]
RP PHOSPHORYLATION AT SER-744; SER-748 AND SER-916.
RX PubMed=15145937; DOI=10.1074/jbc.m404170200;
RA Wang Y., Schattenberg J.M., Rigoli R.M., Storz P., Czaja M.J.;
RT "Hepatocyte resistance to oxidative stress is dependent on protein kinase
RT C-mediated down-regulation of c-Jun/AP-1.";
RL J. Biol. Chem. 279:31089-31097(2004).
RN [6]
RP FUNCTION IN CARDIAC HYPERTROPHY.
RX PubMed=15367659; DOI=10.1128/mcb.24.19.8374-8385.2004;
RA Vega R.B., Harrison B.C., Meadows E., Roberts C.R., Papst P.J., Olson E.N.,
RA McKinsey T.A.;
RT "Protein kinases C and D mediate agonist-dependent cardiac hypertrophy
RT through nuclear export of histone deacetylase 5.";
RL Mol. Cell. Biol. 24:8374-8385(2004).
RN [7]
RP FUNCTION IN NEURONAL POLARITY.
RX PubMed=18784310; DOI=10.1523/jneurosci.1879-08.2008;
RA Bisbal M., Conde C., Donoso M., Bollati F., Sesma J., Quiroga S.,
RA Diaz Anel A., Malhotra V., Marzolo M.P., Caceres A.;
RT "Protein kinase d regulates trafficking of dendritic membrane proteins in
RT developing neurons.";
RL J. Neurosci. 28:9297-9308(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-206, 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).
CC -!- FUNCTION: Serine/threonine-protein kinase that converts transient
CC diacylglycerol (DAG) signals into prolonged physiological effects
CC downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and
CC Ras signaling, Golgi membrane integrity and trafficking, cell survival
CC through NF-kappa-B activation, cell migration, cell differentiation by
CC mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2)
CC signaling, and plays a role in cardiac hypertrophy, VEGFA-induced
CC angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated
CC inflammatory response. Phosphorylates the epidermal growth factor
CC receptor (EGFR) on dual threonine residues, which leads to the
CC suppression of epidermal growth factor (EGF)-induced MAPK8/JNK1
CC activation and subsequent JUN phosphorylation. Phosphorylates RIN1,
CC inducing RIN1 binding to 14-3-3 proteins YWHAB, YWHAE and YWHAZ and
CC increased competition with RAF1 for binding to GTP-bound form of Ras
CC proteins (NRAS, HRAS and KRAS). Acts downstream of the heterotrimeric
CC G-protein beta/gamma-subunit complex to maintain the structural
CC integrity of the Golgi membranes, and is required for protein transport
CC along the secretory pathway. In the trans-Golgi network (TGN),
CC regulates the fission of transport vesicles that are on their way to
CC the plasma membrane. May act by activating the lipid kinase
CC phosphatidylinositol 4-kinase beta (PI4KB) at the TGN for the local
CC synthesis of phosphorylated inositol lipids, which induces a sequential
CC production of DAG, phosphatidic acid (PA) and lyso-PA (LPA) that are
CC necessary for membrane fission and generation of specific transport
CC carriers to the cell surface. Under oxidative stress, is phosphorylated
CC at Tyr-469 via SRC-ABL1 and contributes to cell survival by activating
CC IKK complex and subsequent nuclear translocation and activation of
CC NFKB1. Involved in cell migration by regulating integrin alpha-5/beta-3
CC recycling and promoting its recruitment in newly forming focal
CC adhesion. In osteoblast differentiation, mediates the bone
CC morphogenetic protein 2 (BMP2)-induced nuclear export of HDAC7, which
CC results in the inhibition of HDAC7 transcriptional repression of RUNX2.
CC In neurons, plays an important role in neuronal polarity by regulating
CC the biogenesis of TGN-derived dendritic vesicles, and is involved in
CC the maintenance of dendritic arborization and Golgi structure in
CC hippocampal cells. May potentiate mitogenesis induced by the
CC neuropeptide bombesin or vasopressin by mediating an increase in the
CC duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of
CC immediate-early gene products including FOS that stimulate cell cycle
CC progression. Plays an important role in the proliferative response
CC induced by low calcium in keratinocytes, through sustained activation
CC of MAPK1/3 (ERK1/2) pathway. Downstream of novel PKC signaling, plays a
CC role in cardiac hypertrophy by phosphorylating HDAC5, which in turn
CC triggers XPO1/CRM1-dependent nuclear export of HDAC5, MEF2A
CC transcriptional activation and induction of downstream target genes
CC that promote myocyte hypertrophy and pathological cardiac remodeling.
CC Mediates cardiac troponin I (TNNI3) phosphorylation at the PKA sites,
CC which results in reduced myofilament calcium sensitivity, and
CC accelerated crossbridge cycling kinetics. The PRKD1-HDAC5 pathway is
CC also involved in angiogenesis by mediating VEGFA-induced specific
CC subset of gene expression, cell migration, and tube formation. In
CC response to VEGFA, is necessary and required for HDAC7 phosphorylation
CC which induces HDAC7 nuclear export and endothelial cell proliferation
CC and migration. During apoptosis induced by cytarabine and other
CC genotoxic agents, PRKD1 is cleaved by caspase-3 at Asp-378, resulting
CC in activation of its kinase function and increased sensitivity of cells
CC to the cytotoxic effects of genotoxic agents. In epithelial cells, is
CC required for transducing flagellin-stimulated inflammatory responses by
CC binding and phosphorylating TLR5, which contributes to MAPK14/p38
CC activation and production of inflammatory cytokines. May play a role in
CC inflammatory response by mediating activation of NF-kappa-B. May be
CC involved in pain transmission by directly modulating TRPV1 receptor.
CC Plays a role in activated KRAS-mediated stabilization of ZNF304 in
CC colorectal cancer (CRC) cells (By similarity). Regulates nuclear
CC translocation of transcription factor TFEB in macrophages upon live
CC S.enterica infection (By similarity). {ECO:0000250|UniProtKB:Q15139,
CC ECO:0000250|UniProtKB:Q62101, ECO:0000269|PubMed:10412981,
CC ECO:0000269|PubMed:15367659, ECO:0000269|PubMed:15514163,
CC ECO:0000269|PubMed:18784310}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by DAG and phorbol esters. Phorbol-
CC ester/DAG-type domain 1 binds DAG with high affinity and appears to
CC play the dominant role in mediating translocation to the cell membrane
CC and trans-Golgi network. Phorbol-ester/DAG-type domain 2 binds phorbol
CC ester with higher affinity. Autophosphorylation of Ser-748 and
CC phosphorylation of Ser-744 by PKC relieves auto-inhibition by the PH
CC domain. Phosphorylation on Tyr-469 by the SRC-ABL1 pathway in response
CC to oxidative stress, is also required for activation. Activated by
CC DAPK1 under oxidative stress (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via N-terminus) with ADAP1/CENTA1. Interacts with
CC MAPK13. Interacts with DAPK1 in an oxidative stress-regulated manner.
CC Interacts with USP28; the interaction induces phosphorylation of USP28
CC and activated KRAS-mediated stabilization of ZNF304 (By similarity).
CC Interacts with AKAP13 (via C-terminal domain) (By similarity).
CC {ECO:0000250|UniProtKB:Q15139, ECO:0000250|UniProtKB:Q62101}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15139}. Cell
CC membrane {ECO:0000250|UniProtKB:Q15139}. Golgi apparatus, trans-Golgi
CC network {ECO:0000250|UniProtKB:Q62101}. Note=Translocation to the cell
CC membrane is required for kinase activation. {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-403 and Ser-407 by MAPK13 during regulation
CC of insulin secretion in pancreatic beta cells. Phosphorylated by DAPK1.
CC Phosphorylated at Tyr-93 and by ABL at Tyr-469, which primes the kinase
CC in response to oxidative stress, and promotes a second step activating
CC phosphorylation at Ser-744/Ser-748 by PKRD. Phosphorylated on Ser-916
CC upon S.enterica infection in macrophages.
CC {ECO:0000250|UniProtKB:Q15139, ECO:0000250|UniProtKB:Q62101}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PKD subfamily. {ECO:0000305}.
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DR EMBL; AABR03048549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03048623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03048825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03049215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03049278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03050321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03052344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB020616; BAA78373.1; -; mRNA.
DR RefSeq; NP_001263644.1; NM_001276715.1.
DR AlphaFoldDB; Q9WTQ1; -.
DR SMR; Q9WTQ1; -.
DR BioGRID; 250093; 4.
DR IntAct; Q9WTQ1; 1.
DR STRING; 10116.ENSRNOP00000063159; -.
DR iPTMnet; Q9WTQ1; -.
DR PhosphoSitePlus; Q9WTQ1; -.
DR PaxDb; Q9WTQ1; -.
DR PRIDE; Q9WTQ1; -.
DR Ensembl; ENSRNOT00000068077; ENSRNOP00000063159; ENSRNOG00000004165.
DR GeneID; 85421; -.
DR KEGG; rno:85421; -.
DR UCSC; RGD:620964; rat.
DR CTD; 5587; -.
DR RGD; 620964; Prkd1.
DR eggNOG; KOG4236; Eukaryota.
DR GeneTree; ENSGT00950000183024; -.
DR InParanoid; Q9WTQ1; -.
DR OMA; SIMAPKQ; -.
DR OrthoDB; 367841at2759; -.
DR PhylomeDB; Q9WTQ1; -.
DR Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:Q9WTQ1; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004165; Expressed in pancreas and 18 other tissues.
DR ExpressionAtlas; Q9WTQ1; baseline and differential.
DR GO; GO:0000421; C:autophagosome membrane; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
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:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004697; F:protein kinase C activity; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:RGD.
DR GO; GO:0071447; P:cellular response to hydroperoxide; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0048193; P:Golgi vesicle transport; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISO:RGD.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISO:RGD.
DR GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:1901727; P:positive regulation of histone deacetylase activity; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0089700; P:protein kinase D signaling; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0010837; P:regulation of keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; ISO:RGD.
DR CDD; cd00029; C1; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015727; Protein_Kinase_C_mu-related.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22968; PTHR22968; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000552; PKC_mu_nu_D2; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50003; PH_DOMAIN; 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 Angiogenesis; Apoptosis; ATP-binding; Cell membrane; Cytoplasm;
KW Differentiation; Golgi apparatus; Immunity; Inflammatory response;
KW Innate immunity; Kinase; Magnesium; Membrane; Metal-binding; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..918
FT /note="Serine/threonine-protein kinase D1"
FT /id="PRO_0000333881"
FT DOMAIN 428..547
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 589..845
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 144..194
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 276..326
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 338..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 712
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 595..603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 93
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZ03"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL6"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 403
FT /note="Phosphoserine; by MAPK13"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 407
FT /note="Phosphoserine; by MAPK13"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 438
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 469
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL6"
FT MOD_RES 508
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1Y2"
FT MOD_RES 744
FT /note="Phosphoserine; by PKC/PRKCD"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 748
FT /note="Phosphoserine; by autocatalysis and PKC/PRKCD"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 755
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL6"
FT MOD_RES 916
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15145937"
FT CONFLICT 718
FT /note="V -> G (in Ref. 2; BAA78373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 918 AA; 102043 MW; 93E46AF6C0242B86 CRC64;
MSAPPLLRPP SPLLPAAAAV AAAAAALVPG SGPAPFPAPG AAPAGGISFH LQIGLSREPV
LLLQDSSGDY SLAHVREMAC SIVDQKFPEC GFYGLYDKIL LFRHDPASEN ILQLVKIASD
IQEGDLIEVV LSASATFEDF QIRPHALFVH SYRAPAFCDH CGEMLWGLVR QGLKCEGCGL
NYHKRCAFKI PNNCSGVRRR RLSNVSLTGL GTVRTASAEF STSAPDEPLL SPVSPGFEQK
SPSESFIGRE KRSNSQSYVG RPIQLDKLLM SKVKVPHTFV IHSYTRPTVC QFCKKLLKGL
FRQGLQCKDC RFNCHKRCAP KVPNNCLGEV TINGELLSPG AESDVVMEEG SDDNDSERNS
GLMDDMDEAM VQDTEMALAE GQSDGAEMQD PDADQEDSNR TISPSTSNNI PLMRVVQSVK
HTKRRSSTVM KEGWMVHYTS KDTLRKRHYW RLDSKSITLF QNDTGSRYYK EIPLSEILCL
EPAKPSALIP TGANPHCFEI TTANVVYYVG ENVVNPSSPP PNNSVPPSGI GTDVARMWEV
AIQHALMPVI PKGSSVGSGT NSHKDISVSI SVSNSQIQEN VDISTVYQIF PDEVLGSGQF
GIVYGGKHRK TGRDVAIKII DKLRFPTKQE SQLRNEVAIL QNLHHPGVVN LECMFETPER
VFVVMEKLHG DMLEMILSSE KGRLPEHITK FLITQILVAL RHLHFKNIVH CDLKPENVLL
ASADPFPQVK LCDFGFARII GEKSFRRSVV GTPAYLAPEV LRNKGYNRSL DMWSVGVIIY
VSLSGTFPFN EDEDIHDQIQ NAAFMYPPNP WKEISHEAID LINNLLQVKM RKRYSVDKTL
SHPWLQDYQT WLDLRELECR IGERYITHES DDSRWEQYAG EQGLQYPAHL INLSASHGDS
PEAEEREMKA LSERVSIL
