KC1A_PIG
ID KC1A_PIG Reviewed; 125 AA.
AC O19175;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Casein kinase I isoform alpha;
DE Short=CKI-alpha;
DE EC=2.7.11.1;
DE AltName: Full=CK1;
DE Flags: Fragment;
GN Name=CSNK1A1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. It can phosphorylate a large number of proteins.
CC Participates in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May
CC phosphorylate PER1 and PER2. May play a role in segregating chromosomes
CC during mitosis. May play a role in keratin cytoskeleton disassembly and
CC thereby, it may regulate epithelial cell migration.
CC {ECO:0000250|UniProtKB:P48729}.
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 -!- 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 -!- 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; F22872; CAA23396.1; -; mRNA.
DR AlphaFoldDB; O19175; -.
DR SMR; O19175; -.
DR STRING; 9823.ENSSSCP00000015364; -.
DR BindingDB; O19175; -.
DR ChEMBL; CHEMBL1781858; -.
DR PaxDb; O19175; -.
DR PeptideAtlas; O19175; -.
DR PRIDE; O19175; -.
DR eggNOG; KOG1163; Eukaryota.
DR HOGENOM; CLU_019279_2_0_1; -.
DR InParanoid; O19175; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; 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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Cell projection; Centromere;
KW Chromosome; Cytoplasm; Cytoskeleton; Kinase; Kinetochore; Mitosis;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT CHAIN <1..>125
FT /note="Casein kinase I isoform alpha"
FT /id="PRO_0000192824"
FT DOMAIN <1..>125
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 7
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT NON_TER 1
FT NON_TER 125
SQ SEQUENCE 125 AA; 14633 MW; EB44429E8A2FC7A5 CRC64;
GEEVAVKLES QKARHPQLLY ESKLYKILQG GVGIPHIRWY GQEKDYNVLV MDLLGPSLED
LFNFCSRRFT MKTVLMLADQ MISRIEYVHT KNFIHRDIKP DNFLMGIGRH CNKLFLIDFG
LAKKY
