KPCD3_MOUSE
ID KPCD3_MOUSE Reviewed; 889 AA.
AC Q8K1Y2;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein kinase D3;
DE EC=2.7.11.13;
DE AltName: Full=Protein kinase C nu type;
DE AltName: Full=nPKC-nu;
GN Name=Prkd3; Synonyms=Prkcn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND SER-216, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41; SER-44; THR-535
RP AND SER-539, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Converts transient diacylglycerol (DAG) signals into
CC prolonged physiological effects, downstream of PKC. Involved in
CC resistance to oxidative stress (By similarity). {ECO:0000250}.
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 domains 1 and 2 bind both DAG and phorbol ester with
CC high affinity and mediate translocation to the cell membrane.
CC Autophosphorylation of Ser-734 and phosphorylation of Ser-730 by PKC
CC relieves auto-inhibition by the PH domain.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC Note=Translocation to the cell membrane is required for kinase
CC activation. {ECO:0000250}.
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; BC037012; AAH37012.1; -; mRNA.
DR CCDS; CCDS37699.1; -.
DR RefSeq; NP_083515.2; NM_029239.3.
DR AlphaFoldDB; Q8K1Y2; -.
DR SMR; Q8K1Y2; -.
DR BioGRID; 217368; 1.
DR STRING; 10090.ENSMUSP00000113395; -.
DR iPTMnet; Q8K1Y2; -.
DR PhosphoSitePlus; Q8K1Y2; -.
DR EPD; Q8K1Y2; -.
DR jPOST; Q8K1Y2; -.
DR MaxQB; Q8K1Y2; -.
DR PaxDb; Q8K1Y2; -.
DR PRIDE; Q8K1Y2; -.
DR ProteomicsDB; 263645; -.
DR Antibodypedia; 14569; 428 antibodies from 37 providers.
DR DNASU; 75292; -.
DR Ensembl; ENSMUST00000003191; ENSMUSP00000003191; ENSMUSG00000024070.
DR Ensembl; ENSMUST00000168887; ENSMUSP00000132004; ENSMUSG00000024070.
DR GeneID; 75292; -.
DR KEGG; mmu:75292; -.
DR UCSC; uc008dpr.2; mouse.
DR CTD; 23683; -.
DR MGI; MGI:1922542; Prkd3.
DR VEuPathDB; HostDB:ENSMUSG00000024070; -.
DR eggNOG; KOG4236; Eukaryota.
DR GeneTree; ENSGT00950000183024; -.
DR InParanoid; Q8K1Y2; -.
DR OMA; VCSVVYQ; -.
DR PhylomeDB; Q8K1Y2; -.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR BioGRID-ORCS; 75292; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Prkd3; mouse.
DR PRO; PR:Q8K1Y2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8K1Y2; protein.
DR Bgee; ENSMUSG00000024070; Expressed in rostral migratory stream and 258 other tissues.
DR ExpressionAtlas; Q8K1Y2; baseline and differential.
DR Genevisible; Q8K1Y2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:0016301; F:kinase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0089700; P:protein kinase D signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 ATP-binding; Cytoplasm; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..889
FT /note="Serine/threonine-protein kinase D3"
FT /id="PRO_0000055718"
FT DOMAIN 416..532
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 575..831
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 154..204
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 271..321
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 336..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 698
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 581..589
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94806"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 426
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 457
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL6"
FT MOD_RES 535
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 730
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 734
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q15139"
FT MOD_RES 741
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZL6"
SQ SEQUENCE 889 AA; 100078 MW; 7D03938ED4ECC2E4 CRC64;
MSANNSPPSA QKSVFPATVS AVLPAPSPCS SPKTGLSARL SNGSFSAPSL TNSRGSVHTV
SFLLQIGLTR ESVTIEAQEL SLSAVKDLVC SIVYQKFPEC GFFGMYDKIL LFRHDMNSEN
ILQLITSADE IHEGDLVEVV LSALATVEDF QIRPHALYVH SYKAPTFCDY CGEMLWGLVR
QGLKCEGCGL NYHKRCAFKI PNNCSGVRKR RLSNVSLPGP GLSVPRPLQP ECVPLLSEES
HTHQEPSKRI PSWSGRPIWM EKMVMCRVKV PHTFAVHSYG RPTICQYCKR LLKGLFRQGM
QCKDCKFNCH KRCASKVPRD CLGEVTFNGE PCSVGTDADM PMDIDSSDVN SDGSRGLDDS
EEPSPPEDKM FFLDPTDLDV ERDEETVKTI SPSTSNNIPL MRVVQSIKHT KRRSSTVVKE
GWMVHYTSRD NLRKRHYWRL DSKCLTLFQN ESGSKYYKEI PLSEILRVSS PQDFTSISQG
SNPHCFEIIT DTVVYFVGEN NGSSSHNPVL AATGVGLDVA QSWEKAIRQA LMPVTPQASV
CTSPGQGKDH NLATSISVSN CQVQENVDIS SVYQIFADEV LGSGQFGIVY GGKHRKTGRD
VAIKVIDKMR FPTKQESQLR NEVAILQNLH HPGIVNLECM FETPERVFVV MEKLHGDMLE
MILSSEKSRL PERITKFMVT QILVALRNLH FKNIVHCDLK PENVLLASAE PFPQVKLCDF
GFARIIGEKS FRRSVVGTPA YLAPEVLRSK GYNRSLDMWS VGVIVYVSLS GTFPFNEDED
INDQIQNAAF MYPPNPWREI SSEAIDLINN LLQVKMRKRY SVDKSLSHPW LQDYQTWLDL
REFETRIGER YITHESDDAR WEIHAYTHNL EYPKHFIMAP NPDDMEEDP
