DCLK1_RAT
ID DCLK1_RAT Reviewed; 433 AA.
AC O08875;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine/threonine-protein kinase DCLK1;
DE EC=2.7.11.1;
DE AltName: Full=Calcium/calmodulin-dependent protein kinase type I-like CPG16;
DE AltName: Full=Doublecortin-like and CAM kinase-like 1;
DE AltName: Full=Doublecortin-like kinase 1;
GN Name=Dclk1; Synonyms=Cpg16, Dcamkl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=9699150; DOI=10.1007/bf02737120;
RA Hevroni D., Rattner A., Bundman M., Lederfein D., Gabarah A., Mangelus M.,
RA Silverman M.A., Kedar H., Naor C., Kornuc M., Hanoch T., Seger R.,
RA Theill L.E., Nedivi E., Richter-Levin G., Citri Y.;
RT "Hippocampal plasticity involves extensive gene induction and multiple
RT cellular mechanisms.";
RL J. Mol. Neurosci. 10:75-98(1998).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-30; SER-45; SER-46
RP AND SER-419, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
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DR EMBL; U78857; AAC99476.1; -; mRNA.
DR RefSeq; NP_445795.1; NM_053343.3.
DR AlphaFoldDB; O08875; -.
DR SMR; O08875; -.
DR BioGRID; 249852; 1.
DR IntAct; O08875; 2.
DR MINT; O08875; -.
DR STRING; 10116.ENSRNOP00000019748; -.
DR iPTMnet; O08875; -.
DR PhosphoSitePlus; O08875; -.
DR PaxDb; O08875; -.
DR PRIDE; O08875; -.
DR GeneID; 83825; -.
DR KEGG; rno:83825; -.
DR UCSC; RGD:68437; rat.
DR CTD; 9201; -.
DR RGD; 68437; Dclk1.
DR VEuPathDB; HostDB:ENSRNOG00000032922; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; O08875; -.
DR PhylomeDB; O08875; -.
DR BRENDA; 2.7.11.1; 5301.
DR PRO; PR:O08875; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000032922; Expressed in frontal cortex and 20 other tissues.
DR ExpressionAtlas; O08875; baseline and differential.
DR Genevisible; O08875; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; ISO:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0030900; P:forebrain development; ISO:RGD.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR GO; GO:0009615; P:response to virus; ISO:RGD.
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; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
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 ATP-binding; Developmental protein; Differentiation; Kinase; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..433
FT /note="Serine/threonine-protein kinase DCLK1"
FT /id="PRO_0000085921"
FT DOMAIN 83..340
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 89..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLM8"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLM8"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLM8"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLM8"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLM8"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLM8"
FT MOD_RES 213
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLM8"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLM8"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLM8"
SQ SEQUENCE 433 AA; 47681 MW; 0CE5E06E152A557D CRC64;
MLELIEVNGT PGSQLSTPRS GKSPSPSPTS PGSLRKQRIS QHGGSSTSLS STKVCSSMDE
NDGPGEEESD EGFQIPATIT ERYKVGRTIG DGNFAVVKEC IERSTAREYA LKIIKKSKCR
GKEHMIQNEV SILRRVKHPN IVLLIEEMDV PTELYLVMEL VKGGDLFDAI TSTSKYTERD
ASGMLYNLAS AIKYLHSLNI VHRDIKPENL LVYEHQDGSK SLKLGDFGLA TIVDGPLYTV
CGTPTYVAPE IIAETGYGLK VDIWAAGVIT YILLCGFPPF RGSGDDQEVL FDQILMGQVD
FPSPYWDNVS DSAKELINMM LLVNVDQRFS AVQVLEHPWV NDDGLPENEH QLSVAGKIKK
HFNTGPKPSS TAAGVSVIAT TALDKERQVF RRRRNQDVRG RYKAQPAPPE LNSESEDYSP
SSSETVRSPN SPF
