ID KC1A_RABIT Reviewed; 325 AA. AC P67828; P35506; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 130. DE RecName: Full=Casein kinase I isoform alpha; DE Short=CKI-alpha; DE EC=2.7.11.1; DE AltName: Full=CK1; GN Name=CSNK1A1; 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 [MRNA]. RC TISSUE=Skeletal muscle; RA Zhai L., DePaoli-Roach A.A., Roach P.J.; RT "Rabbit muscle casein kinase 1 alpha."; RL Submitted (JUL-1996) 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. Can phosphorylate a large number of proteins. Participates CC in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45' (By similarity). CC May phosphorylate PER1 and PER2 (By similarity). May play a role in CC segregating chromosomes during mitosis. May play a role in keratin CC cytoskeleton disassembly and thereby, it may regulate epithelial cell CC migration (By similarity). Acts as a positive regulator of mTORC1 and CC mTORC2 signaling in response to nutrients by mediating phosphorylation CC of DEPTOR inhibitor (By similarity). Acts as an inhibitor of NLRP3 CC inflammasome assembly by mediating phosphorylation of NLRP3 (By CC similarity). {ECO:0000250|UniProtKB:P48729, CC ECO:0000250|UniProtKB:Q8BK63}. 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 -!- SUBUNIT: Interacts with the Axin complex (By similarity). Interacts CC with TUT1, leading to TUT1 phosphorylation (By similarity). Interacts CC with FAM83H; recruits CSNK1A1 to keratin filaments (By similarity). CC Interacts with FAM83D (via N-terminus); in mitotic cells (By CC similarity). {ECO:0000250|UniProtKB:P48729}. CC -!- INTERACTION: CC P67828; P31946: YWHAB; Xeno; NbExp=3; IntAct=EBI-7540603, EBI-359815; CC P67828; P62260: Ywhae; Xeno; NbExp=2; IntAct=EBI-7540603, EBI-356462; CC P67828; P61981: YWHAG; Xeno; NbExp=3; IntAct=EBI-7540603, EBI-359832; CC P67828; Q04917: YWHAH; Xeno; NbExp=8; IntAct=EBI-7540603, EBI-306940; CC P67828; P27348: YWHAQ; Xeno; NbExp=2; IntAct=EBI-7540603, EBI-359854; CC P67828; P63104: YWHAZ; Xeno; NbExp=4; IntAct=EBI-7540603, EBI-347088; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48729}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000250|UniProtKB:P48729}. Chromosome, centromere, kinetochore CC {ECO:0000250|UniProtKB:P48729}. Nucleus speckle CC {ECO:0000250|UniProtKB:P48729}. Cytoplasm, cytoskeleton, cilium basal CC body {ECO:0000250|UniProtKB:Q8BK63}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000250|UniProtKB:Q8BK63}. Note=Localizes to the centrosome in CC interphase cells, and to kinetochore fibers during mitosis. Also CC recruited to the keratin cytoskeleton. {ECO:0000250|UniProtKB:P48729}. CC -!- PTM: Phosphorylated by MTOR in response to mitogenic stimulation, CC leading to its activation. {ECO:0000250|UniProtKB:P48729}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr CC protein kinase family. Casein kinase I subfamily. {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; U59166; AAB03992.1; -; mRNA. DR RefSeq; NP_001075842.1; NM_001082373.1. DR AlphaFoldDB; P67828; -. DR SMR; P67828; -. DR IntAct; P67828; 9. DR MINT; P67828; -. DR STRING; 9986.ENSOCUP00000037641; -. DR iPTMnet; P67828; -. DR PaxDb; 9986-ENSOCUP00000018081; -. DR GeneID; 100009227; -. DR KEGG; ocu:100009227; -. DR CTD; 1452; -. DR eggNOG; KOG1163; Eukaryota. DR HOGENOM; CLU_019279_2_7_1; -. DR InParanoid; P67828; -. DR OMA; PAEFPMY; -. DR OrthoDB; 1534388at2759; -. DR Proteomes; UP000001811; Unplaced. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. DR GO; GO:0005819; C:spindle; 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; ISS:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB. DR GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR CDD; cd14128; STKc_CK1_alpha; 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:SF20; CASEIN KINASE I ISOFORM ALPHA; 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 Acetylation; ATP-binding; Cell cycle; Cell division; Cell projection; KW Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinase; Kinetochore; KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P48729" FT CHAIN 2..325 FT /note="Casein kinase I isoform alpha" FT /id="PRO_0000192825" FT DOMAIN 17..285 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 136 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 23..31 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 46 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P48729" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48729" FT MOD_RES 8 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P48729" SQ SEQUENCE 325 AA; 37567 MW; B84DC84BDDC17854 CRC64; MASSSGSKAE FIVGGKYKLV RKIGSGSFGD IYLAINITNG EEVAVKLESQ KARHPQLLYE SKLYKILQGG VGIPHIRWYG QEKDYNVLVM DLLGPSLEDL FNFCSRRFTM KTVLMLADQM ISRIEYVHTK NFIHRDIKPD NFLMGIGRHC NKLFLIDFGL AKKYRDNRTR QHIPYREDKN LTGTARYASI NAHLGIEQSR RDDMESLGYV LMYFNRTSLP WQGLKAATKK QKYEKISEKK MSTPVEVLCK GFPAEFAMYL NYCRGLRFEE APDYMYLRQL FRILFRTLNH QYDYTFDWTM LKQKAAQQAA SSSGQGQQAQ TPTGF //