ID   DCLK1_MOUSE             Reviewed;         756 AA.
AC   Q9JLM8; Q6P207;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Serine/threonine-protein kinase DCLK1;
DE            EC=2.7.11.1;
DE   AltName: Full=Doublecortin-like and CAM kinase-like 1;
DE   AltName: Full=Doublecortin-like kinase 1;
GN   Name=Dclk1; Synonyms=Dcamkl1, Dclk;
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 [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10533048;
RX   DOI=10.1002/(sici)1097-4547(19991115)58:4<567::aid-jnr9>3.3.co;2-k;
RA   Burgess H.A., Martinez S., Reiner O.;
RT   "KIAA0369, doublecortin-like kinase, is expressed during brain
RT   development.";
RL   J. Neurosci. Res. 58:567-575(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-536, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-332 AND SER-337, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-36; THR-46; SER-305;
RP   SER-307; SER-330; SER-332; SER-334; SER-337; SER-347; SER-352; SER-355;
RP   SER-364; SER-392; SER-742; SER-751 AND SER-754, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-352; SER-353; SER-358 AND SER-362 (ISOFORM 2), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC   Spleen;
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: Probable kinase that may be involved in a calcium-signaling
CC       pathway controlling neuronal migration in the developing brain. May
CC       also participate in functions of the mature nervous system (By
CC       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=2.7.11.1;
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=2.7.11.1;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9JLM8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JLM8-2; Sequence=VSP_019593, VSP_019594;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR   EMBL; AF155819; AAF26673.1; -; mRNA.
DR   EMBL; BC064783; AAH64783.1; -; mRNA.
DR   CCDS; CCDS17359.1; -. [Q9JLM8-1]
DR   CCDS; CCDS50909.1; -. [Q9JLM8-2]
DR   RefSeq; NP_064362.1; NM_019978.3. [Q9JLM8-1]
DR   AlphaFoldDB; Q9JLM8; -.
DR   SMR; Q9JLM8; -.
DR   BioGRID; 199063; 13.
DR   IntAct; Q9JLM8; 11.
DR   MINT; Q9JLM8; -.
DR   STRING; 10090.ENSMUSP00000050034; -.
DR   GlyGen; Q9JLM8; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9JLM8; -.
DR   MetOSite; Q9JLM8; -.
DR   PhosphoSitePlus; Q9JLM8; -.
DR   SwissPalm; Q9JLM8; -.
DR   jPOST; Q9JLM8; -.
DR   MaxQB; Q9JLM8; -.
DR   PaxDb; 10090-ENSMUSP00000050034; -.
DR   PeptideAtlas; Q9JLM8; -.
DR   ProteomicsDB; 279838; -. [Q9JLM8-1]
DR   ProteomicsDB; 279839; -. [Q9JLM8-2]
DR   Pumba; Q9JLM8; -.
DR   Antibodypedia; 23046; 500 antibodies from 39 providers.
DR   DNASU; 13175; -.
DR   Ensembl; ENSMUST00000054237.14; ENSMUSP00000050034.8; ENSMUSG00000027797.16. [Q9JLM8-1]
DR   GeneID; 13175; -.
DR   KEGG; mmu:13175; -.
DR   UCSC; uc008pgl.2; mouse. [Q9JLM8-1]
DR   AGR; MGI:1330861; -.
DR   CTD; 9201; -.
DR   MGI; MGI:1330861; Dclk1.
DR   VEuPathDB; HostDB:ENSMUSG00000027797; -.
DR   eggNOG; KOG0032; Eukaryota.
DR   eggNOG; KOG3757; Eukaryota.
DR   GeneTree; ENSGT00940000154956; -.
DR   InParanoid; Q9JLM8; -.
DR   OrthoDB; 2956627at2759; -.
DR   PhylomeDB; Q9JLM8; -.
DR   TreeFam; TF318770; -.
DR   BRENDA; 2.7.11.1; 3474.
DR   BioGRID-ORCS; 13175; 2 hits in 80 CRISPR screens.
DR   ChiTaRS; Dclk1; mouse.
DR   PRO; PR:Q9JLM8; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9JLM8; Protein.
DR   Bgee; ENSMUSG00000027797; Expressed in stria vascularis of cochlear duct and 237 other cell types or tissues.
DR   ExpressionAtlas; Q9JLM8; baseline and differential.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0048675; P:axon extension; IGI:MGI.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0007420; P:brain development; IGI:MGI.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IGI:MGI.
DR   GO; GO:0048813; P:dendrite morphogenesis; IGI:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:1900181; P:negative regulation of protein localization to nucleus; IDA:MGI.
DR   GO; GO:0001764; P:neuron migration; IGI:MGI.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0034504; P:protein localization to nucleus; IDA:MGI.
DR   GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR   CDD; cd17140; DCX1_DCLK1; 1.
DR   CDD; cd17069; DCX2; 1.
DR   CDD; cd14183; STKc_DCKL1; 1.
DR   Gene3D; 3.10.20.230; Doublecortin domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR003533; Doublecortin_dom.
DR   InterPro; IPR036572; Doublecortin_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24347:SF401; SERINE_THREONINE-PROTEIN KINASE DCLK1; 1.
DR   Pfam; PF03607; DCX; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00537; DCX; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF89837; Doublecortin (DC); 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50309; DC; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q9JLM8; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Developmental protein; Differentiation;
KW   Kinase; Neurogenesis; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..756
FT                   /note="Serine/threonine-protein kinase DCLK1"
FT                   /id="PRO_0000085920"
FT   DOMAIN          57..143
FT                   /note="Doublecortin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT   DOMAIN          186..269
FT                   /note="Doublecortin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT   DOMAIN          406..663
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          288..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        527
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         412..420
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         435
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         46
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15345747,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         330
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         334
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08875"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         364
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         392
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         536
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   MOD_RES         742
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         751
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         754
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         343..363
FT                   /note="KQRISQHGGSSTSLSSTKVCS -> RQRDLYRPLSSDDLDSVGDSV (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019593"
FT   VAR_SEQ         364..756
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019594"
FT   MOD_RES         Q9JLM8-2:352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q9JLM8-2:353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q9JLM8-2:358
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q9JLM8-2:362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   756 AA;  84153 MW;  3D1DBF18C23129F2 CRC64;
     MSFGRDMELE HFDERDKAQR YSRGSRVNGL PSPTHSAHCS FYRTRTLQTL SSEKKAKKVR
     FYRNGDRYFK GIVYAISPDR FRSFEALLAD LTRTLSDNVN LPQGVRTIYT IDGLKKISSL
     DQLVEGESYV CGSIEPFKKL EYTKNVNPNW SVNVKTTSAS RAVSSLATAK GGPSEVRENK
     DFIRPKLVTI IRSGVKPRKA VRILLNKKTA HSFEQVLTDI TDAIKLDSGV VKRLYTLDGK
     QVMCLQDFFG DDDIFIACGP EKFRYQDDFL LDESECRVVK STSYTKIASA SRRGTTKSPG
     PSRRSKSPAS TSSVNGTPGS QLSTPRSGKS PSPSPTSPGS LRKQRISQHG GSSTSLSSTK
     VCSSMDENDG PGEGDELGRR HSLQRGWRRE ESEEGFQIPA TITERYKVGR TIGDGNFAVV
     KECIERSTAR EYALKIIKKS KCRGKEHMIQ NEVSILRRVK HPNIVLLIEE MDVPTELYLV
     MELVKGGDLF DAITSTSKYT ERDASGMLYN LASAIKYLHS LNIVHRDIKP ENLLVYEHQD
     GSKSLKLGDF GLATIVDGPL YTVCGTPTYV APEIIAETGY GLKVDIWAAG VITYILLCGF
     PPFRGSGDDQ EVLFDQILMG QVDFPSPYWD NVSDSAKELI NMMLLVNVDQ RFSAVQVLEH
     PWVNDDGLPE NEHQLSVAGK IKKHFNTGPK PSSTAAGVSV IATTALDKER QVFRRRRNQD
     VRSRYKAQPA PPELNSESED YSPSSSETVR SPNSPF
//