ID KC1D_XENLA Reviewed; 415 AA.
AC Q5BP74; Q7ZXL6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Casein kinase I isoform delta;
DE Short=CKI-delta;
DE Short=CKId;
DE EC=2.7.11.1 {ECO:0000269|PubMed:15893604};
DE AltName: Full=Tau-protein kinase CSNK1D;
DE EC=2.7.11.26 {ECO:0000250|UniProtKB:P48730};
GN Name=csnk1d;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, PHOSPHORYLATION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Embryo;
RX PubMed=15893604; DOI=10.1016/j.molbrainres.2005.02.009;
RA Constance C.M., Fan J.-Y., Preuss F., Green C.B., Price J.L.;
RT "The circadian clock-containing photoreceptor cells in Xenopus laevis
RT express several isoforms of casein kinase I.";
RL Brain Res. Mol. Brain Res. 136:199-211(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: [Isoform 1]: Casein kinases are operationally defined by
CC their preferential utilization of acidic proteins such as caseins as
CC substrates. Can phosphorylate a large number of proteins
CC (PubMed:15893604). Central component of the circadian clock. May act as
CC a negative regulator of circadian rhythmicity by phosphorylating per1
CC and per2, which may lead to their degradation. Participates in wnt
CC signaling (By similarity). {ECO:0000250|UniProtKB:P48730,
CC ECO:0000269|PubMed:15893604}.
CC -!- FUNCTION: [Isoform 2]: Has no kinase activity.
CC {ECO:0000269|PubMed:15893604}.
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:0000269|PubMed:15893604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:15893604};
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:0000269|PubMed:15893604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:15893604};
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). Interacts with per1 and per2.
CC Component of the circadian core oscillator (By similarity).
CC {ECO:0000250|UniProtKB:P48730, ECO:0000250|UniProtKB:Q9DC28}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:15893604}. Nucleus {ECO:0000269|PubMed:15893604}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:15893604}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5BP74-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BP74-2; Sequence=VSP_035782;
CC -!- TISSUE SPECIFICITY: Detected in retina photoreceptor cells.
CC {ECO:0000269|PubMed:15893604}.
CC -!- INDUCTION: Constitutively expressed in retina.
CC {ECO:0000269|PubMed:15893604}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC {ECO:0000269|PubMed:15893604}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY926534; AAX22002.1; -; mRNA.
DR EMBL; AY926535; AAX22003.1; -; mRNA.
DR EMBL; BC044700; AAH44700.1; -; mRNA.
DR RefSeq; NP_001080669.1; NM_001087200.1.
DR RefSeq; XP_018096015.1; XM_018240526.1. [Q5BP74-2]
DR AlphaFoldDB; Q5BP74; -.
DR SMR; Q5BP74; -.
DR DNASU; 380361; -.
DR GeneID; 380361; -.
DR KEGG; xla:380361; -.
DR AGR; Xenbase:XB-GENE-5734033; -.
DR CTD; 380361; -.
DR Xenbase; XB-GENE-5734033; csnk1d.S.
DR OrthoDB; 1534388at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 380361; Expressed in testis and 19 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd14125; STKc_CK1_delta_epsilon; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR11909:SF18; CASEIN KINASE I ISOFORM DELTA; 1.
DR PANTHER; PTHR11909; CASEIN KINASE-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Nucleus; Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Wnt signaling pathway.
FT CHAIN 1..415
FT /note="Casein kinase I isoform delta"
FT /id="PRO_0000354089"
FT DOMAIN 9..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 301..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..342
FT /note="Autoinhibitory"
FT /evidence="ECO:0000250"
FT COMPBIAS 301..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..415
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"
FT VAR_SEQ 189..246
FT /note="EQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVL
FT CKGYPS -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15893604, ECO:0000303|Ref.2"
FT /id="VSP_035782"
FT CONFLICT 57
FT /note="K -> N (in Ref. 1; AAX22003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47439 MW; B8B8765DB29EC9B5 CRC64;
MELRVGNRYR LGRKIGSGSF GDIYLGTDIA ASEEVAIKLE 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 NMLKFGASRA
AEDAERERRE REERLRHTRN PAVRGLPSTA SGRLRGTQEV TPSTPLTPTS HTANTSPRPV
SGMERERKVS MRLHRGAPVN VSSSDLTSRQ DTSRMSTSQI PSRVTSSGLP STVHR
//
