KC1A_CAEEL
ID KC1A_CAEEL Reviewed; 341 AA.
AC P42168;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Casein kinase I isoform alpha;
DE Short=CKI-alpha;
DE EC=2.7.11.1;
DE AltName: Full=CK1;
GN Name=kin-19; ORFNames=C03C10.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR EMBL; Z35637; CAA84685.1; -; Genomic_DNA.
DR PIR; T18873; T18873.
DR RefSeq; NP_497818.1; NM_065417.5.
DR AlphaFoldDB; P42168; -.
DR SMR; P42168; -.
DR BioGRID; 40761; 3.
DR STRING; 6239.C03C10.1.1; -.
DR iPTMnet; P42168; -.
DR EPD; P42168; -.
DR PaxDb; P42168; -.
DR PeptideAtlas; P42168; -.
DR EnsemblMetazoa; C03C10.1.1; C03C10.1.1; WBGene00002202.
DR EnsemblMetazoa; C03C10.1.2; C03C10.1.2; WBGene00002202.
DR EnsemblMetazoa; C03C10.1.3; C03C10.1.3; WBGene00002202.
DR UCSC; C03C10.1.1; c. elegans.
DR WormBase; C03C10.1; CE00872; WBGene00002202; kin-19.
DR eggNOG; KOG1163; Eukaryota.
DR GeneTree; ENSGT00940000153700; -.
DR HOGENOM; CLU_019279_2_0_1; -.
DR InParanoid; P42168; -.
DR OMA; PAEFPMY; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; P42168; -.
DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-CEL-196299; Beta-catenin phosphorylation cascade.
DR SignaLink; P42168; -.
DR PRO; PR:P42168; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002202; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005813; C:centrosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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; ISS:WormBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:WormBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:WormBase.
DR GO; GO:0060069; P:Wnt signaling pathway, regulating spindle positioning; IMP:WormBase.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..341
FT /note="Casein kinase I isoform alpha"
FT /id="PRO_0000192867"
FT DOMAIN 16..284
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 306..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 22..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 341 AA; 39037 MW; 17AD6E173551BABC CRC64;
MAGVMSVKDF IVATKYKLIR KIGSGSFGDI YVSINVTNGE EVAIKLESNR ARHPQLLYES
KVYRILQGGV GIPHIRWYGT EREYNVLVMD LLGPSLEDLF NFCSRRFTMK TVLMLADQMI
GRIEYVHVKN FIHRDIKPDN FLMGIGRHCN KLFLIDFGLA KKYRDSRTRT HIPYREDKNL
TGTARYASIN AHLGIEQSRR DDMESLGYVL MYFNRGTLPW QGLKAATKKQ KYEKISEKKM
TTSVEHLCKG FPAEFPMYLS YTRGLRFDES PDYMYLRQLF RILFRTLNHQ YDYTFDWTML
KQKAQQSQSS GVPGTNTTTQ GATVPSAGVP AGVAPGGTTP Q
