KC1D_RABIT
ID KC1D_RABIT Reviewed; 81 AA.
AC P81123;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Casein kinase I isoform delta;
DE Short=CKI-delta;
DE Short=CKId;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P48730};
DE AltName: Full=Tau-protein kinase CSNK1D;
DE EC=2.7.11.26 {ECO:0000250|UniProtKB:P48730};
DE Flags: Fragment;
GN Name=CSNK1D; Synonyms=HCKID;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE OF 5-81, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Reticulocyte, and Testis;
RX PubMed=1729698; DOI=10.1073/pnas.89.1.28;
RA Robinson L.C., Hubbard E.J.A., Graves P.R., dePaoli-Roach A.A., Roach P.J.,
RA Kung C., Haas D.W., Hagedorn C.H., Goebl M., Culbertson M.R., Carlson M.;
RT "Yeast casein kinase I homologues: an essential gene pair.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:28-32(1992).
CC -!- FUNCTION: Essential serine/threonine-protein kinase that regulates
CC diverse cellular growth and survival processes including Wnt signaling,
CC DNA repair and circadian rhythms. It can phosphorylate a large number
CC of proteins. Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU,
CC TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1,
CC PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In
CC balance with PP1, determines the circadian period length through the
CC regulation of the speed and rhythmicity of PER1 and PER2
CC phosphorylation. Controls PER1 and PER2 nuclear transport and
CC degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3
CC ubiquitin ligase-mediated ubiquitination and subsequent degradation.
CC DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation
CC of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation.
CC Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that
CC controls neurite outgrowth. EIF6 phosphorylation promotes its nuclear
CC export. Triggers down-regulation of dopamine receptors in the
CC forebrain. Activates DCK in vitro by phosphorylation. TOP2A
CC phosphorylation favors DNA cleavable complex formation. May regulate
CC the formation of the mitotic spindle apparatus in extravillous
CC trophoblast. Modulates connexin-43/GJA1 gap junction assembly by
CC phosphorylation. Probably involved in lymphocyte physiology. Regulates
CC fast synaptic transmission mediated by glutamate (By similarity).
CC Interacts with DDX3X; this interaction enhances CSNK1D kinase activity
CC in vitro, but it is unclear whether this interaction is physiologically
CC relevant (By similarity). {ECO:0000250|UniProtKB:P48730}.
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 Evidence={ECO:0000250|UniProtKB:P48730};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:P48730};
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; Evidence={ECO:0000250|UniProtKB:P48730};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000250|UniProtKB:P48730};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC Evidence={ECO:0000250|UniProtKB:P48730};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12802;
CC Evidence={ECO:0000250|UniProtKB:P48730};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.26; Evidence={ECO:0000250|UniProtKB:P48730};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53905;
CC Evidence={ECO:0000250|UniProtKB:P48730};
CC -!- ACTIVITY REGULATION: Exhibits substrate-dependent heparin activation.
CC {ECO:0000250|UniProtKB:P48730}.
CC -!- SUBUNIT: Monomer (By similarity). Component of the circadian core
CC oscillator, which includes the CRY proteins, CLOCK, or NPAS2,
CC ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER
CC proteins (By similarity). Interacts with DNMT1 and MAP1A (By
CC similarity). Interacts directly with PER1 and PER2 which may lead to
CC their degradation (By similarity). Interacts with MAPT/TAU, SNAPIN,
CC DBNDD2, AIB1/NCOA3 and ESR1 (By similarity). Interacts with
CC AKAP9/AKAP450; this interaction promotes centrosomal subcellular
CC location (By similarity). Binds to tubulins in mitotic cells upon DNA
CC damage (By similarity). Interacts with GJA1 (By similarity).
CC {ECO:0000250|UniProtKB:P48730, ECO:0000250|UniProtKB:Q06486,
CC ECO:0000250|UniProtKB:Q9DC28}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC -!- PTM: Autophosphorylated on serine and threonine residues; this
CC autophosphorylation represses activity. Reactivated by phosphatase-
CC mediated dephosphorylation. May be dephosphorylated by PP1 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR STRING; 9986.ENSOCUP00000006410; -.
DR ChEMBL; CHEMBL3309063; -.
DR eggNOG; KOG1164; Eukaryota.
DR InParanoid; P81123; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
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:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR030509; CK1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR040976; Pkinase_fungal.
DR InterPro; IPR000719; Prot_kinase_dom.
DR PANTHER; PTHR11909:SF409; PTHR11909:SF409; 1.
DR Pfam; PF17667; Pkinase_fungal; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT CHAIN <1..>81
FT /note="Casein kinase I isoform delta"
FT /id="PRO_0000192835"
FT DOMAIN <1..>81
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 11
FT /note="L -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="N -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="T -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 81
SQ SEQUENCE 81 AA; 9405 MW; 4908A3367EF24E67 CRC64;
XIFPDNFLMG LGKKGNLVYI IDFGLAKKYR DARTHQHIPY RENKNLTGTA RYASINTHLG
IEQSRRDDLE SLGYVLMYFN L
