DCLK1_MOUSE
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 03-AUG-2022, entry version 192.
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>3.0.co;2-t;
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; 10.
DR MINT; Q9JLM8; -.
DR STRING; 10090.ENSMUSP00000050034; -.
DR iPTMnet; Q9JLM8; -.
DR PhosphoSitePlus; Q9JLM8; -.
DR jPOST; Q9JLM8; -.
DR MaxQB; Q9JLM8; -.
DR PaxDb; Q9JLM8; -.
DR PeptideAtlas; Q9JLM8; -.
DR PRIDE; Q9JLM8; -.
DR ProteomicsDB; 279838; -. [Q9JLM8-1]
DR ProteomicsDB; 279839; -. [Q9JLM8-2]
DR Antibodypedia; 23046; 438 antibodies from 39 providers.
DR DNASU; 13175; -.
DR Ensembl; ENSMUST00000054237; ENSMUSP00000050034; ENSMUSG00000027797. [Q9JLM8-1]
DR GeneID; 13175; -.
DR KEGG; mmu:13175; -.
DR UCSC; uc008pgl.2; mouse. [Q9JLM8-1]
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; 330091at2759; -.
DR PhylomeDB; Q9JLM8; -.
DR TreeFam; TF318770; -.
DR BRENDA; 2.7.11.1; 3474.
DR BioGRID-ORCS; 13175; 1 hit in 75 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 235 other tissues.
DR ExpressionAtlas; Q9JLM8; baseline and differential.
DR Genevisible; Q9JLM8; MM.
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:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR Gene3D; 3.10.20.230; -; 2.
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 Pfam; PF03607; DCX; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00537; DCX; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF89837; SSF89837; 2.
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.
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
