KC1DA_DANRE
ID KC1DA_DANRE Reviewed; 403 AA.
AC Q7T2E3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Casein kinase I isoform delta-A;
DE Short=CKI-delta-A;
DE Short=CKId-A;
DE EC=2.7.11.1;
DE AltName: Full=Casein kinase I isoform delta-like;
GN Name=csnk1da; Synonyms=csnk1dl; ORFNames=si:ch211-234h8.6;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=18064361; DOI=10.4067/s0716-97602007000200015;
RA Albornoz A., Yanez J.M., Foerster C., Aguirre C., Pereiro L., Burzio V.,
RA Moraga M., Reyes A.E., Antonelli M.;
RT "The CK1 gene family: expression patterning in zebrafish development.";
RL Biol. Res. 40:251-266(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. Central component of the circadian clock. May act as a
CC negative regulator of circadian rhythmicity by phosphorylating per1 and
CC per2, which may lead to their degradation. Participates in wnt
CC signaling (By 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 -!- ACTIVITY REGULATION: Exhibits substrate-dependent heparin activation.
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with per1 and per2.
CC Component of the circadian core oscillator (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in embryos until eight
CC hours after fertilization. Detected throughout the embryo, but
CC particularly in the cephalic region, at 10 to 24 hours after
CC fertilization. Detected in retina, tegmentum and myencephalon at 38 and
CC 48 hours after fertilization. {ECO:0000269|PubMed:18064361}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; EU127826; ABV29338.1; -; mRNA.
DR EMBL; BX897685; CAQ15428.1; -; Genomic_DNA.
DR EMBL; BC054583; AAH54583.1; -; mRNA.
DR RefSeq; NP_955877.1; NM_199583.1.
DR AlphaFoldDB; Q7T2E3; -.
DR SMR; Q7T2E3; -.
DR STRING; 7955.ENSDARP00000003101; -.
DR PaxDb; Q7T2E3; -.
DR PRIDE; Q7T2E3; -.
DR Ensembl; ENSDART00000025326; ENSDARP00000003101; ENSDARG00000008370.
DR GeneID; 322106; -.
DR KEGG; dre:322106; -.
DR CTD; 322106; -.
DR ZFIN; ZDB-GENE-030131-825; csnk1da.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000153536; -.
DR HOGENOM; CLU_019279_2_2_1; -.
DR InParanoid; Q7T2E3; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; Q7T2E3; -.
DR TreeFam; TF354246; -.
DR Reactome; R-DRE-201688; WNT mediated activation of DVL.
DR Reactome; R-DRE-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-DRE-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-DRE-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-DRE-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-DRE-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-DRE-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-DRE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-DRE-8854518; AURKA Activation by TPX2.
DR PRO; PR:Q7T2E3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000008370; Expressed in mature ovarian follicle and 30 other tissues.
DR ExpressionAtlas; Q7T2E3; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0042752; P:regulation of circadian rhythm; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Wnt signaling pathway.
FT CHAIN 1..403
FT /note="Casein kinase I isoform delta-A"
FT /id="PRO_0000354087"
FT DOMAIN 9..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 315..340
FT /note="Autoinhibitory"
FT /evidence="ECO:0000250"
FT REGION 322..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 403 AA; 46243 MW; 58A49386B6DF6D70 CRC64;
MELRVGNRYR LGRKIGSGSF GDIYLGTDIT TGEEVAIKLE CVKTKHPQLH IESKIYKMMQ
GGVGIPTIKW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH
SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA
SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL
CKGYPSEFAT YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGGARE
DPERDRRDRE ERIRQGRIPL PRVMLPTSSG RPRGTQEVAP APPLTPDSHT GMERERKVSM
RLHRGAPVNV SSSDLTGRQD CSRISTSQAH SRVPSGLQSA VPR
