LOCUS       NP_001164475             890 aa            linear   ROD 28-APR-2025
DEFINITION  serine/threonine-protein kinase D3 isoform 1 [Mus musculus].
ACCESSION   NP_001164475
VERSION     NP_001164475.1
DBSOURCE    REFSEQ: accession NM_001171004.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 890)
  AUTHORS   Waheed-Ullah,Q., Wilsdon,A., Abbad,A., Rochette,S., Bu'Lock,F.,
            Hitz,M.P., Dombrowsky,G., Cuello,F., Brook,J.D. and Loughna,S.
  TITLE     Effect of deletion of the protein kinase PRKD1 on development of
            the mouse embryonic heart
  JOURNAL   J Anat 245 (1), 70-83 (2024)
   PUBMED   38419169
REFERENCE   2  (residues 1 to 890)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 890)
  AUTHORS   Burciaga,S.D., Saavedra,F., Fischer,L., Johnstone,K. and
            Jensen,E.D.
  TITLE     Protein kinase D3 conditional knockout impairs osteoclast formation
            and increases trabecular bone volume in male mice
  JOURNAL   Bone 172, 116759 (2023)
   PUBMED   37044359
  REMARK    GeneRIF: Protein kinase D3 conditional knockout impairs osteoclast
            formation and increases trabecular bone volume in male mice.
REFERENCE   4  (residues 1 to 890)
  AUTHORS   Veazey,J.M., Wong,G.S., Eliseeva,S.I., Smyth,T.R., Chapman,T.J.,
            Lim,K., Kim,M. and Georas,S.N.
  TITLE     Protein kinase D3 promotes neutrophil migration during viral
            infection
  JOURNAL   Immunol Cell Biol 101 (2), 130-141 (2023)
   PUBMED   36318273
  REMARK    GeneRIF: Protein kinase D3 promotes neutrophil migration during
            viral infection.
REFERENCE   5  (residues 1 to 890)
  AUTHORS   Koutnik,J., Leitges,M. and Siegmund,K.
  TITLE     T cell-intrinsic protein kinase D3 is dispensable for the cells'
            activation
  JOURNAL   Front Immunol 13, 1049033 (2022)
   PUBMED   36466811
  REMARK    GeneRIF: T cell-intrinsic protein kinase D3 is dispensable for the
            cells' activation.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 890)
  AUTHORS   Ellwanger,K., Pfizenmaier,K., Lutz,S. and Hausser,A.
  TITLE     Expression patterns of protein kinase D 3 during mouse development
  JOURNAL   BMC Dev Biol 8, 47 (2008)
   PUBMED   18439271
  REMARK    GeneRIF: PKD3 is increasingly expressed in neuronal as well as in
            the supporting connective tissue and in skeletal muscles
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 890)
  AUTHORS   Oster,H., Abraham,D. and Leitges,M.
  TITLE     Expression of the protein kinase D (PKD) family during mouse
            embryogenesis
  JOURNAL   Gene Expr Patterns 6 (4), 400-408 (2006)
   PUBMED   16377259
REFERENCE   8  (residues 1 to 890)
  AUTHORS   Rey,O., Papazyan,R., Waldron,R.T., Young,S.H.,
            Lippincott-Schwartz,J., Jacamo,R. and Rozengurt,E.
  TITLE     The nuclear import of protein kinase D3 requires its catalytic
            activity
  JOURNAL   J Biol Chem 281 (8), 5149-5157 (2006)
   PUBMED   16380377
  REMARK    GeneRIF: the catalytic activity of PKD3 may regulate its nuclear
            import through autophosphorylation and/or interaction with another
            protein
REFERENCE   9  (residues 1 to 890)
  AUTHORS   Matthews,S.A., Dayalu,R., Thompson,L.J. and Scharenberg,A.M.
  TITLE     Regulation of protein kinase Cnu by the B-cell antigen receptor
  JOURNAL   J Biol Chem 278 (11), 9086-9091 (2003)
   PUBMED   12506120
  REMARK    GeneRIF: PKCnu is an important component of signaling pathways
            downstream from novel PKC enzymes after B-cell receptor engagement
REFERENCE   10 (residues 1 to 890)
  AUTHORS   Morrow,T.A., Muljo,S.A., Zhang,J., Hardwick,J.M. and Schlissel,M.S.
  TITLE     Pro-B-cell-specific transcription and proapoptotic function of
            protein kinase Ceta
  JOURNAL   Mol Cell Biol 19 (8), 5608-5618 (1999)
   PUBMED   10409750
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC151293.2, BC089164.1 and AC154274.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (1).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089164.1, SRR9219381.351152.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..890
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="17"
                     /map="17 49.69 cM"
     Protein         1..890
                     /product="serine/threonine-protein kinase D3 isoform 1"
                     /EC_number="2.7.11.13"
                     /note="protein kinase C, nu; serine/threonine-protein
                     kinase D3; nPKC-nu; protein kinase C nu type"
                     /calculated_mol_wt=100077
     Site            27
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O94806; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            44
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Region          145..219
                     /region_name="C1_PKD3_rpt1"
                     /note="first protein kinase C conserved region 1 (C1
                     domain) found in protein kinase D3 (PKD3) and similar
                     proteins; cd20841"
                     /db_xref="CDD:410391"
     Site            order(160..166,174..178,181)
                     /site_type="other"
                     /note="putative DAG/PE binding site [chemical binding]"
                     /db_xref="CDD:410391"
     Site            213
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            216
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17242355; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Region          267..335
                     /region_name="C1"
                     /note="protein kinase C conserved region 1 (C1 domain)
                     superfamily; cl00040"
                     /db_xref="CDD:412127"
     Region          336..370
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            346
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15139; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            391
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15139; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            395
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15139; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Region          410..534
                     /region_name="PH_PKD"
                     /note="Protein kinase D (PKD/PKCmu) pleckstrin homology
                     (PH) domain; cd01239"
                     /db_xref="CDD:269945"
     Site            426
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q15139; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q15139; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            457
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9BZL6; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            535
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            539
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Region          572..831
                     /region_name="STKc_PKD"
                     /note="Catalytic domain of the Serine/Threonine kinase,
                     Protein Kinase D; cd14082"
                     /db_xref="CDD:270984"
     Site            order(582..586,590,603,605,636,652..655,658,660,698..699,
                     701,703..704,706,719..720,723,737..741,743)
                     /site_type="active"
                     /db_xref="CDD:270984"
     Site            order(582..585,590,603,605,636,652..655,658,703..704,706,
                     719..720)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270984"
     Site            order(586,658,660,698..699,701,703,723,737..741,743)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270984"
     Site            719..741
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:270984"
     Site            731
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKC.
                     /evidence=ECO:0000250|UniProtKB:Q15139; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            735
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:Q15139; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     Site            742
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q9BZL6; propagated from
                     UniProtKB/Swiss-Prot (Q8K1Y2.1)"
     CDS             1..890
                     /gene="Prkd3"
                     /gene_synonym="4930557O20Rik; 5730497N19Rik; Pkcnu; PKD3;
                     Prkcn"
                     /coded_by="NM_001171004.1:763..3435"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS50185.1"
                     /db_xref="GeneID:75292"
                     /db_xref="MGI:MGI:1922542"
ORIGIN      
        1 msannsppsa qksvfpatvs avlpapspcs spktglsarl sngsfsapsl tnsrgsvhtv
       61 sfllqigltr esvtieaqel slsavkdlvc sivyqkfpec gffgmydkil lfrhdmnsen
      121 ilqlitsade ihegdlvevv lsalatvedf qirphalyvh sykaptfcdy cgemlwglvr
      181 qglkcegcgl nyhkrcafki pnncsgvrkr rlsnvslpgp glsvprplqp ecvpllsees
      241 hthqepskri pswsgrpiwm ekmvmcrvkv phtfavhsyg rpticqyckr llkglfrqgm
      301 qckdckfnch krcaskvprd clgevtfnge pcsvgtdadm pmdidssdvn sdgsrgldds
      361 eepsppedkm ffldptdldv erdeetvkti spstsnnipl mrvvqsikht krrsstvvke
      421 gwmvhytsrd nlrkrhywrl dskcltlfqn esgskyykei plseilrvss pqdftsisqg
      481 snphcfeiit dtvvyfvgen ngssshnpvl aatgvgldva qswekairqa lmpvtpqasv
      541 ctspgqgkdh kdlatsisvs ncqvqenvdi ssvyqifade vlgsgqfgiv yggkhrktgr
      601 dvaikvidkm rfptkqesql rnevailqnl hhpgivnlec mfetpervfv vmeklhgdml
      661 emilsseksr lperitkfmv tqilvalrnl hfknivhcdl kpenvllasa epfpqvklcd
      721 fgfariigek sfrrsvvgtp aylapevlrs kgynrsldmw svgvivyvsl sgtfpfnede
      781 dindqiqnaa fmyppnpwre isseaidlin nllqvkmrkr ysvdkslshp wlqdyqtwld
      841 lrefetrige ryithesdda rweihaythn leypkhfima pnpddmeedp
//
