KC1A_CHICK
ID KC1A_CHICK Reviewed; 337 AA.
AC P67962; O57528; P70065; P79789; P79790;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CK1A; CK1A-L AND CK1A-LS).
RC TISSUE=Brain;
RX PubMed=9766967; DOI=10.1016/s0378-1119(98)00291-1;
RA Green C.L., Bennett G.S.;
RT "Identification of four alternatively spliced isoforms of chicken casein
RT kinase I alpha that are all expressed in diverse cell types.";
RL Gene 216:189-195(1998).
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. May play a role in segregating
CC chromosomes during mitosis. May play a role in keratin cytoskeleton
CC disassembly. {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 -!- 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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=CK1A;
CC IsoId=P67962-1, P70065-1;
CC Sequence=Displayed;
CC Name=CK1A-L;
CC IsoId=P67962-2, P70065-2;
CC Sequence=VSP_004747;
CC Name=CK1A-LS;
CC IsoId=P67962-3, P70065-3;
CC Sequence=VSP_004746;
CC -!- PTM: Autophosphorylated.
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; U80822; AAB95648.1; -; mRNA.
DR EMBL; U80823; AAB96334.1; -; mRNA.
DR EMBL; AF042863; AAC35749.1; -; mRNA.
DR RefSeq; NP_990384.1; NM_205053.1.
DR RefSeq; XP_015149158.1; XM_015293672.1.
DR RefSeq; XP_015149159.1; XM_015293673.1. [P67962-1]
DR AlphaFoldDB; P67962; -.
DR SMR; P67962; -.
DR STRING; 9031.ENSGALP00000002080; -.
DR Ensembl; ENSGALT00000041028; ENSGALP00000040233; ENSGALG00000001364. [P67962-1]
DR GeneID; 395924; -.
DR KEGG; gga:395924; -.
DR CTD; 1452; -.
DR VEuPathDB; HostDB:geneid_395924; -.
DR eggNOG; KOG1163; Eukaryota.
DR GeneTree; ENSGT00940000153700; -.
DR HOGENOM; CLU_019279_2_7_1; -.
DR InParanoid; P67962; -.
DR OrthoDB; 1097975at2759; -.
DR PhylomeDB; P67962; -.
DR BRENDA; 2.7.11.1; 1306.
DR Reactome; R-GGA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-GGA-196299; Beta-catenin phosphorylation cascade.
DR PRO; PR:P67962; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000001364; Expressed in spermatocyte and 12 other tissues.
DR ExpressionAtlas; P67962; baseline and differential.
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: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; 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cell projection; Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinase;
KW Kinetochore; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Wnt signaling pathway.
FT CHAIN 1..337
FT /note="Casein kinase I isoform alpha"
FT /id="PRO_0000192828"
FT DOMAIN 17..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 309..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 VAR_SEQ 151
FT /note="N -> KCLESPVGKRKRSMTVSTSQDPSFSGLNQ (in isoform CK1A-
FT LS)"
FT /evidence="ECO:0000303|PubMed:9766967"
FT /id="VSP_004746"
FT VAR_SEQ 325..337
FT /note="KQTDKSKSNMKGF -> F (in isoform CK1A-L)"
FT /evidence="ECO:0000303|PubMed:9766967"
FT /id="VSP_004747"
SQ SEQUENCE 337 AA; 38901 MW; 002085AE33CAFAC6 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 TPTGKQTDKS KSNMKGF
