LOCUS       NP_766516                790 aa            linear   ROD 04-MAR-2025
DEFINITION  serine/threonine-protein kinase DCLK3 [Mus musculus].
ACCESSION   NP_766516 XP_916728
VERSION     NP_766516.2
DBSOURCE    REFSEQ: accession NM_172928.5
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 790)
  AUTHORS   de Longprez,L., Gaillard,M.C., Decraene,C., Perot,J.B., Keime,C.,
            Nadkarni,N., Louca,M., Jan,C., Liot,G., Auregan,G., Guillermier,M.,
            Mitja,J., Hantraye,P., Bertaux,F., Norbert,M., Bonvento,G.,
            Flament,J., Dhenain,M., Neri,C., Bemelmans,A.P., Merienne,K.,
            Cambon,K. and Brouillet,E.
  TITLE     Loss of the neuronal kinase DCLK3 leads to anxiety-like behaviour
            and memory deficits
  JOURNAL   Brain (2025) In press
   PUBMED   39908340
  REMARK    Publication Status: Available-Online prior to print
REFERENCE   2  (residues 1 to 790)
  AUTHORS   Galvan,L., Francelle,L., Gaillard,M.C., de Longprez,L., Carrillo-de
            Sauvage,M.A., Liot,G., Cambon,K., Stimmer,L., Luccantoni,S.,
            Flament,J., Valette,J., de Chaldee,M., Auregan,G., Guillermier,M.,
            Josephine,C., Petit,F., Jan,C., Jarrige,M., Dufour,N., Bonvento,G.,
            Humbert,S., Saudou,F., Hantraye,P., Merienne,K., Bemelmans,A.P.,
            Perrier,A.L., Deglon,N. and Brouillet,E.
  TITLE     The striatal kinase DCLK3 produces neuroprotection against mutant
            huntingtin
  JOURNAL   Brain 141 (5), 1434-1454 (2018)
   PUBMED   29534157
  REMARK    GeneRIF: This study suggest that the presence of DCLK3 in striatal
            neurons may play a key role in transcription regulation and
            chromatin remodelling in these brain cells, and show that reduced
            expression of the kinase in Huntington's disease could render the
            striatum highly vulnerable to neurodegeneration.
REFERENCE   3  (residues 1 to 790)
  AUTHORS   Molyneaux,B.J., Goff,L.A., Brettler,A.C., Chen,H.H., Hrvatin,S.,
            Rinn,J.L. and Arlotta,P.
  TITLE     DeCoN: genome-wide analysis of in vivo transcriptional dynamics
            during pyramidal neuron fate selection in neocortex
  JOURNAL   Neuron 85 (2), 275-288 (2015)
   PUBMED   25556833
  REMARK    Erratum:[Neuron. 2016 Jan 6;89(1):235]
REFERENCE   4  (residues 1 to 790)
  AUTHORS   Dijkmans,T.F., van Hooijdonk,L.W., Fitzsimons,C.P. and
            Vreugdenhil,E.
  TITLE     The doublecortin gene family and disorders of neuronal structure
  JOURNAL   Cent Nerv Syst Agents Med Chem 10 (1), 32-46 (2010)
   PUBMED   20236041
  REMARK    Review article
REFERENCE   5  (residues 1 to 790)
  AUTHORS   Reiner,O., Coquelle,F.M., Peter,B., Levy,T., Kaplan,A., Sapir,T.,
            Orr,I., Barkai,N., Eichele,G. and Bergmann,S.
  TITLE     The evolving doublecortin (DCX) superfamily
  JOURNAL   BMC Genomics 7, 188 (2006)
   PUBMED   16869982
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 790)
  AUTHORS   Ohmae,S., Takemoto-Kimura,S., Okamura,M., Adachi-Morishima,A.,
            Nonaka,M., Fuse,T., Kida,S., Tanji,M., Furuyashiki,T., Arakawa,Y.,
            Narumiya,S., Okuno,H. and Bito,H.
  TITLE     Molecular identification and characterization of a family of
            kinases with homology to Ca2+/calmodulin-dependent protein kinases
            I/IV
  JOURNAL   J Biol Chem 281 (29), 20427-20439 (2006)
   PUBMED   16684769
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BB617821.1, DQ286388.1 and
            AV341123.2.
            
            On Jun 2, 2009 this sequence version replaced NP_766516.1.
            
            Summary: This gene encodes a member of the protein kinase
            superfamily and the doublecortin family. Differently from the other
            two closely related family members (DCLK1 and DCLK2), the protein
            encoded by this gene contains only one N-terminal doublecortin
            domain and is unable to bind microtubules and to regulate
            microtubule polymerization. The protein contains a C-terminal
            serine/threonine protein kinase domain, which shows substantial
            homology to Ca2+/calmoduline-dependent protein kinase, and a
            serine/proline-rich domain in between the doublecortin and the
            protein kinase domains, which mediates multiple protein-protein
            interactions. [provided by RefSeq, Sep 2010].
            
            CCDS Note: The coding region has been updated to extend the
            N-terminus to one that is supported by available conservation data.
            This would result in a protein that is 171 aa longer at the
            N-terminal.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK135010.1, DQ286388.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849380
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..790
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 61.33 cM"
     Protein         1..790
                     /product="serine/threonine-protein kinase DCLK3"
                     /EC_number="2.7.11.1"
                     /note="doublecortin and CaM kinase-like 3; CLr; CLICK-I
                     and II-related; doublecortin-like and CAM kinase-like 3;
                     Click-I, -II related"
                     /calculated_mol_wt=88097
     Region          1..37
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BWQ5.2)"
     Region          95..179
                     /region_name="DCX_DCLK3"
                     /note="Doublecortin-like domain found in doublecortin-like
                     kinase 3 (DCLK3); cd16111"
                     /db_xref="CDD:340528"
     Site            order(95,106..108,114,119..120,122,130,138..140,142..143,
                     146,173)
                     /site_type="other"
                     /note="putative DCX-stabilized microtubules [polypeptide
                     binding]"
                     /db_xref="CDD:340528"
     Site            order(110,154)
                     /site_type="other"
                     /note="key conserved lysines"
                     /db_xref="CDD:340528"
     Region          201..290
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BWQ5.2)"
     Region          315..506
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BWQ5.2)"
     Region          513..770
                     /region_name="Protein Kinases, catalytic domain"
                     /note="The protein kinase superfamily is mainly composed
                     of the catalytic domains of serine/threonine-specific and
                     tyrosine-specific protein kinases. It also includes RIO
                     kinases, which are atypical serine protein kinases,
                     aminoglycoside phosphotransferases; cl21453"
                     /db_xref="CDD:473864"
     Site            order(520..523,526,528,541,543,573,589..592,635,639..640,
                     642,656..657)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:270870"
     CDS             1..790
                     /gene="Dclk3"
                     /gene_synonym="C730036H08; Dcamkl3"
                     /coded_by="NM_172928.5:185..2557"
                     /db_xref="CCDS:CCDS23585.2"
                     /db_xref="GeneID:245038"
                     /db_xref="MGI:MGI:3039580"
ORIGIN      
        1 mpaapvlrpp pppatpappa psrpappipg hrgpcdhslk clsskiserk lpgpwlpagr
       61 gplekpvlgp rgavmplfsp qsslhsvrae hsplkprvvt vvklggqplr katlllnrrs
      121 vqtfeqllsd isealgfprw kndrvrklft lkgrevksvs dffregdafi amgkepltlk
      181 siqlameely pknralalap hsrvpsprlr srlpskllkg shrcgeagsy saemeskavs
      241 rhqgktstvl apedkaraqk wvrgkqesep ggppspgaat qeethasgek hlgveiekts
      301 geivrcekck rerelqlglq repcplgtse ldlgraqkrd seklvrtksc rrpseakstd
      361 geegwkgdsh rgsprdppqe lrrpnsnsdk keirgsesqd shpqgapkaq kdlvegppav
      421 eegpidmrre drhtcrskha awlrreqqae ppqlprtrge ekqaehekkp gglgerrape
      481 keskrkleek rperpsgrkp rpkgiisadv ekhydiggvi gdgnfatvke crhretkqay
      541 amkmidksql kgkedivdse iliiqslshp nivklhevye teaeiylime yvqggdlfda
      601 ivenvkfpep eaavmitdlc kalvhmhdkn ivhrdvkpen llvqrnedks itlkladfgl
      661 akyvvrpift vcgtptyvap eilsekgygl evdmwaagvi lyillcgfpp frsperdqde
      721 lfniiqvgqf eflspywdni sdaakdlvrn llevdpkkry taeqvlqhpw iemvghtntg
      781 nsqkeespns
//
