DCLK3_MOUSE
ID DCLK3_MOUSE Reviewed; 790 AA.
AC Q8BWQ5; Q1A748;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Serine/threonine-protein kinase DCLK3;
DE EC=2.7.11.1;
DE AltName: Full=CLICK-I and II-related;
DE Short=CLr;
DE AltName: Full=Doublecortin-like and CAM kinase-like 3;
DE AltName: Full=Doublecortin-like kinase 3;
GN Name=Dclk3; Synonyms=Dcamkl3;
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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16684769; DOI=10.1074/jbc.m513212200;
RA Ohmae S., Takemoto-Kimura S., Okamura M., Adachi-Morishima A., Nonaka M.,
RA Fuse T., Kida S., Tanji M., Furuyashiki T., Arakawa Y., Narumiya S.,
RA Okuno H., Bito H.;
RT "Molecular identification and characterization of a family of kinases with
RT homology to Ca2+/calmodulin-dependent protein kinases I/IV.";
RL J. Biol. Chem. 281:20427-20439(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-790.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
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 -!- INTERACTION:
CC Q8BWQ5; O75528: TADA3; Xeno; NbExp=2; IntAct=EBI-16518538, EBI-473249;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16684769}. Nucleus
CC {ECO:0000269|PubMed:16684769}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and to a lower extent in
CC liver and kidney. {ECO:0000269|PubMed:16684769}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. CaMK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH56929.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC34182.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ286388; ABB89470.1; -; mRNA.
DR EMBL; AK050312; BAC34182.1; ALT_FRAME; mRNA.
DR EMBL; BC056929; AAH56929.1; ALT_INIT; mRNA.
DR CCDS; CCDS23585.2; -.
DR RefSeq; NP_766516.2; NM_172928.5.
DR AlphaFoldDB; Q8BWQ5; -.
DR SMR; Q8BWQ5; -.
DR IntAct; Q8BWQ5; 1.
DR STRING; 10090.ENSMUSP00000107510; -.
DR PhosphoSitePlus; Q8BWQ5; -.
DR MaxQB; Q8BWQ5; -.
DR PaxDb; Q8BWQ5; -.
DR PRIDE; Q8BWQ5; -.
DR ProteomicsDB; 279500; -.
DR Antibodypedia; 28151; 103 antibodies from 30 providers.
DR DNASU; 245038; -.
DR Ensembl; ENSMUST00000111879; ENSMUSP00000107510; ENSMUSG00000032500.
DR GeneID; 245038; -.
DR KEGG; mmu:245038; -.
DR UCSC; uc009rvv.2; mouse.
DR CTD; 85443; -.
DR MGI; MGI:3039580; Dclk3.
DR VEuPathDB; HostDB:ENSMUSG00000032500; -.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000159476; -.
DR HOGENOM; CLU_000288_94_2_1; -.
DR InParanoid; Q8BWQ5; -.
DR OMA; ELDMGKC; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q8BWQ5; -.
DR TreeFam; TF318770; -.
DR BioGRID-ORCS; 245038; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q8BWQ5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BWQ5; protein.
DR Bgee; ENSMUSG00000032500; Expressed in olfactory tubercle and 113 other tissues.
DR Genevisible; Q8BWQ5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; 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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IDA:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:MGI.
DR Gene3D; 3.10.20.230; -; 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 Pfam; PF03607; DCX; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00537; DCX; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF89837; SSF89837; 1.
DR PROSITE; PS50309; DC; 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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..790
FT /note="Serine/threonine-protein kinase DCLK3"
FT /id="PRO_0000252255"
FT DOMAIN 97..183
FT /note="Doublecortin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 514..771
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 635
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 520..528
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 790 AA; 88228 MW; 23A56EBD3453BBAD CRC64;
MPAAPVLRPP PPPATPAPPA PSRPAPPIPG HRGPCDHSLK CLSSKISERK LPGPWLPAGR
GPLEKPVLGP RGAVMPLFSP QSSLHSVRAE HSPLKPRVVT VVKLGGQPLR KATLLLNRRS
VQTFEQLLSD ISEALGFPRW KNDRVRKLFT LKGREVKSVS DFFREGDAFI AMGKEPLTLK
SIQLAMEELY PKNRALALAP HSRVPSPRLR SRLPSKLLKG SHRCGEAGSY SAEMESKAVS
RHQGKTSTVL APEDKARAQK WVRGKQESEP GGPPSPGAAT QEETHASGEK HLGVEIEKTS
GEIVRCEKCK RERELQLGLQ REPCPLGTSE LDLGRAQKRD SEKLVRTKSC RRPSEAKSTD
GEEGWKGDSH RGSPRDPPQE LRRPNSNSDK KEIRGSESQD SHPQGAPKAQ KDLVEGPPAV
EEGPIDMRRE DRHTCRSKHA AWLRREQQAE PPQLPRTRGE EKQAEHEKKP GGLGERRAPE
KESKRKLEEK RPERPSGRKP RPKGIISADV EKHYDIGGVI GDGNFATVKE CRHRETKQAY
AMKMIDKSQL KGKEDIVDSE ILIIQSLSHP NIVKLHEVYE TEAEIYLIME YVQGGDLFDA
IVENVKFPEP EAAVMITDLC KALVHMHDKN IVHRDVKPEN LLVQRNEDKS ITLKLADFGL
AKYVVRPIFT VCGTPTYVAP EILSEKGYGL EVDMWAAGVI LYILLCGFPP FRSPERDQDE
LFNIIQVGQF EFLSPYWDNI SDAAKDLVRN LLEVDPKKRY TAEQVLQHPW IEMVGHTNTG
NSQKEESPNS
