KIN20_CAEEL
ID KIN20_CAEEL Reviewed; 497 AA.
AC Q20471; A0A4V0IKI0; H9G2V4; H9G2V5; Q2PJ71; Q565A9; Q5MCN7; Q5MCN8; Q5WRP4;
AC Q8I4I6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Casein kinase I isoform delta;
DE EC=2.7.11.1 {ECO:0000305|PubMed:31910362};
DE AltName: Full=Protein kinase 20;
GN Name=kin-20 {ECO:0000312|WormBase:F46F2.2c};
GN ORFNames=F46F2.2 {ECO:0000312|WormBase:F46F2.2c};
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 [MRNA] (ISOFORMS A AND E), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=15691769; DOI=10.1016/j.devcel.2004.12.006;
RA Banerjee D., Kwok A., Lin S.-Y., Slack F.J.;
RT "Developmental timing in C. elegans is regulated by kin-20 and tim-1,
RT homologs of core circadian clock genes.";
RL Dev. Cell 8:287-295(2005).
RN [2]
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).
RN [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=29880558; DOI=10.1534/g3.118.200392;
RA Rhodehouse K., Cascino K., Aseltine L., Padula A., Weinstein R.,
RA Spina J.S., Olivero C.E., Van Wynsberghe P.M.;
RT "The Doubletime Homolog KIN-20 Mainly Regulates let-7 Independently of Its
RT Effects on the Period Homolog LIN-42 in Caenorhabditis elegans.";
RL G3 (Bethesda) 8:2617-2629(2018).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF 344-GLN--HIS-497.
RX PubMed=31910362; DOI=10.1016/j.devcel.2019.12.005;
RA LaBella M.L., Hujber E.J., Moore K.A., Rawson R.L., Merrill S.A.,
RA Allaire P.D., Ailion M., Hollien J., Bastiani M.J., Jorgensen E.M.;
RT "Casein Kinase 1delta Stabilizes Mature Axons by Inhibiting Transcription
RT Termination of Ankyrin.";
RL Dev. Cell 52:88-103(2020).
CC -!- FUNCTION: Essential serine/threonine-protein kinase that regulates
CC diverse cellular growth and survival processes including Wnt signaling,
CC DNA repair and circadian rhythms (By similarity). Casein kinases are
CC operationally defined by their preferential utilization of acidic
CC proteins (By similarity). Positively regulates the expression of
CC components of the heterochronic pathway, which regulate developmental
CC timing, such as the transcriptional repressor lin-42 and microRNAs such
CC as let-7 (PubMed:29880558). Negatively regulates cell cycle exit and
CC cell fusion to prevent the premature differentiation of hypodermal seam
CC cells into adult cells (PubMed:15691769). Plays a role in regulating
CC axon branching and subsequently, the maturation of the nervous system,
CC most likely by preventing the premature termination of transcripts for
CC proteins such as Ankyrin/unc-44, which are required for maintaining the
CC nervous system (PubMed:31910362). May phosphorylate ssup-72 to promote
CC nervous system maturation (Probable). {ECO:0000250|UniProtKB:P48730,
CC ECO:0000269|PubMed:15691769, ECO:0000269|PubMed:29880558,
CC ECO:0000269|PubMed:31910362, ECO:0000305|PubMed:31910362}.
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:0000305|PubMed:31910362};
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:0000305|PubMed:31910362};
CC -!- ACTIVITY REGULATION: Exhibits substrate-dependent heparin activation.
CC {ECO:0000250|UniProtKB:P48730}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48730}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48730}. Nucleus
CC {ECO:0000269|PubMed:31910362}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:P48730}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:31910362}. Note=Localizes to the nucleus of all
CC cell types and to adherens junctions in the spermatheca.
CC {ECO:0000269|PubMed:31910362}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=c {ECO:0000312|WormBase:F46F2.2c};
CC IsoId=Q20471-3; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F46F2.2a}; Synonyms=kin-20A
CC {ECO:0000303|PubMed:15691769}, kin-20C {ECO:0000303|PubMed:15691769};
CC IsoId=Q20471-1; Sequence=VSP_060796, VSP_060797;
CC Name=b {ECO:0000312|WormBase:F46F2.2b};
CC IsoId=Q20471-5; Sequence=VSP_007173;
CC Name=d {ECO:0000312|WormBase:F46F2.2d};
CC IsoId=Q20471-4; Sequence=VSP_016943;
CC Name=e {ECO:0000312|WormBase:F46F2.2e}; Synonyms=kin-20B
CC {ECO:0000303|PubMed:15691769};
CC IsoId=Q20471-2; Sequence=VSP_007173, VSP_060796, VSP_060797;
CC Name=f {ECO:0000312|WormBase:F46F2.2f};
CC IsoId=Q20471-6; Sequence=VSP_007173, VSP_060795, VSP_060798;
CC Name=g {ECO:0000312|WormBase:F46F2.2g};
CC IsoId=Q20471-8; Sequence=VSP_060794, VSP_060795, VSP_060798;
CC -!- TISSUE SPECIFICITY: Expressed throughout larval development and into
CC the adult stage in both hypodermal seam cells and the hermaphrodite
CC specific neuron. {ECO:0000269|PubMed:15691769}.
CC -!- DEVELOPMENTAL STAGE: Constant expression throughout development
CC (PubMed:15691769, PubMed:29880558). However, expression decreases prior
CC to the L2 larval stage, increases at the beginning of the L3 larval
CC stage, and then decreases and plateaus from the mid L3 larval stage
CC onwards (PubMed:31910362, PubMed:29880558). In the nervous system,
CC expressed as dim speckles in developing DD motor neurons from the 3-
CC fold stage of embryogenesis, then expression is dim in neurons of L1
CC stage larvae (PubMed:31910362). At the L2 larval stage, it is highly
CC expressed in epidermal cells and motor neurons (PubMed:31910362). At
CC the L4 laravl stage, it is expressed in all cell types and in the
CC spermatheca (PubMed:31910362). {ECO:0000269|PubMed:15691769,
CC ECO:0000269|PubMed:29880558, ECO:0000269|PubMed:31910362}.
CC -!- DEVELOPMENTAL STAGE: [Isoform a]: Expressed throughout development.
CC {ECO:0000269|PubMed:29880558}.
CC -!- DEVELOPMENTAL STAGE: [Isoform b]: Highly expressed throughout
CC development. {ECO:0000269|PubMed:29880558}.
CC -!- DEVELOPMENTAL STAGE: [Isoform c]: Highly expressed throughout
CC development. {ECO:0000269|PubMed:29880558}.
CC -!- DEVELOPMENTAL STAGE: [Isoform d]: Weakly expressed throughout
CC development. {ECO:0000269|PubMed:29880558}.
CC -!- DEVELOPMENTAL STAGE: [Isoform e]: Expressed throughout development.
CC {ECO:0000269|PubMed:29880558}.
CC -!- DEVELOPMENTAL STAGE: [Isoform f]: Weakly expressed throughout
CC development. {ECO:0000269|PubMed:29880558}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in precocious
CC seam cell fusion and the early exit of seam cell from the cell cycle
CC during the L4 larval stage (PubMed:15691769). RNAi-mediated knockdown
CC does not impair alae formation (PubMed:15691769). RNAi-mediated
CC knockdown results in a squat body statue, referred to as a dumpy
CC phenotype, and rescues the incomplete alae formation defect in the lin-
CC 42 (n1089) mutant (PubMed:29880558). RNAi-mediated knockdown increases
CC the survival rate and partially restores alae formation of let-7 n2853
CC mutants at 20 dgrees Celsius (PubMed:15691769). RNAi-mediated knockdown
CC rescues the lethal bursting phenotype that occurs after the L4 stage
CC molt in the let-7(n2853) mutant at 25 degrees Celsius
CC (PubMed:29880558). {ECO:0000269|PubMed:15691769,
CC ECO:0000269|PubMed:29880558}.
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; AY836556; AAW21314.1; -; mRNA.
DR EMBL; AY836557; AAW21315.1; -; mRNA.
DR EMBL; AY836558; AAW21316.1; -; mRNA.
DR EMBL; BX284606; CAA93775.3; -; Genomic_DNA.
DR EMBL; BX284606; CAD56585.4; -; Genomic_DNA.
DR EMBL; Z81031; CAD56585.4; JOINED; Genomic_DNA.
DR EMBL; BX284606; CAH60762.2; -; Genomic_DNA.
DR EMBL; BX284606; CAI79241.1; -; Genomic_DNA.
DR EMBL; BX284606; CCG28198.1; -; Genomic_DNA.
DR EMBL; Z69903; CCG28199.1; -; Genomic_DNA.
DR EMBL; BX284606; VTW47572.1; -; Genomic_DNA.
DR PIR; T22311; T22311.
DR RefSeq; NP_001024669.1; NM_001029498.3. [Q20471-3]
DR RefSeq; NP_001024670.1; NM_001029499.2.
DR RefSeq; NP_001257258.1; NM_001270329.1.
DR RefSeq; NP_001257259.1; NM_001270330.1.
DR RefSeq; NP_510533.3; NM_078132.4.
DR RefSeq; NP_872247.4; NM_182447.6. [Q20471-5]
DR AlphaFoldDB; Q20471; -.
DR SMR; Q20471; -.
DR BioGRID; 46517; 9.
DR IntAct; Q20471; 5.
DR MINT; Q20471; -.
DR STRING; 6239.F46F2.2c.1; -.
DR EPD; Q20471; -.
DR PaxDb; Q20471; -.
DR EnsemblMetazoa; F46F2.2a.1; F46F2.2a.1; WBGene00002203. [Q20471-1]
DR EnsemblMetazoa; F46F2.2b.1; F46F2.2b.1; WBGene00002203. [Q20471-5]
DR EnsemblMetazoa; F46F2.2c.1; F46F2.2c.1; WBGene00002203. [Q20471-3]
DR EnsemblMetazoa; F46F2.2d.1; F46F2.2d.1; WBGene00002203. [Q20471-4]
DR EnsemblMetazoa; F46F2.2e.1; F46F2.2e.1; WBGene00002203. [Q20471-2]
DR EnsemblMetazoa; F46F2.2f.1; F46F2.2f.1; WBGene00002203. [Q20471-6]
DR EnsemblMetazoa; F46F2.2f.2; F46F2.2f.2; WBGene00002203. [Q20471-6]
DR EnsemblMetazoa; F46F2.2g.1; F46F2.2g.1; WBGene00002203. [Q20471-8]
DR GeneID; 181620; -.
DR KEGG; cel:CELE_F46F2.2; -.
DR UCSC; F46F2.2a.1; c. elegans. [Q20471-1]
DR CTD; 181620; -.
DR WormBase; F46F2.2a; CE38356; WBGene00002203; kin-20. [Q20471-1]
DR WormBase; F46F2.2b; CE47149; WBGene00002203; kin-20. [Q20471-5]
DR WormBase; F46F2.2c; CE38358; WBGene00002203; kin-20. [Q20471-3]
DR WormBase; F46F2.2d; CE38359; WBGene00002203; kin-20. [Q20471-4]
DR WormBase; F46F2.2e; CE38357; WBGene00002203; kin-20. [Q20471-2]
DR WormBase; F46F2.2f; CE32422; WBGene00002203; kin-20. [Q20471-6]
DR WormBase; F46F2.2g; CE53444; WBGene00002203; kin-20. [Q20471-8]
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000153536; -.
DR HOGENOM; CLU_040585_0_0_1; -.
DR InParanoid; Q20471; -.
DR OMA; LYRIMLG; -.
DR OrthoDB; 889559at2759; -.
DR PhylomeDB; Q20471; -.
DR Reactome; R-CEL-201688; WNT mediated activation of DVL.
DR SignaLink; Q20471; -.
DR PRO; PR:Q20471; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002203; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q20471; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA: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; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0048670; P:regulation of collateral sprouting; IMP:UniProtKB.
DR GO; GO:0040012; P:regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Biological rhythms; Cell junction;
KW Centromere; Chromosome; Cytoplasm; Developmental protein; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..497
FT /note="Casein kinase I isoform delta"
FT /id="PRO_0000192866"
FT DOMAIN 191..458
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 197..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..182
FT /note="Missing (in isoform b, isoform e and isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_007173"
FT VAR_SEQ 1..181
FT /note="MATMSNDAAAAATWHNNTSTPMDTTEPATNSHNPGETAVIGGPEALLLPSGS
FT GPEEMNRHPLLMAQAHGEHHQPRLLHNFPVIPPPIQQHQQPPLLQQAQPSQIPHPTQPQ
FT IDPTMFTQQSGFNWPPIDPNTIAALAQAQLASSHAQFVSLALTLDPTLLSHFLATQQIP
FT PVPQPLVHKKA -> MLFVPGKGLS (in isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_060794"
FT VAR_SEQ 477..497
FT /note="YNESLEARNNFQQAVPNQRRH -> DLPF (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_016943"
FT VAR_SEQ 477..480
FT /note="YNES -> DLPF (in isoform f and isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_060795"
FT VAR_SEQ 477..479
FT /note="YNE -> RRN (in isoform a and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_060796"
FT VAR_SEQ 480..497
FT /note="Missing (in isoform a and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_060797"
FT VAR_SEQ 481..497
FT /note="Missing (in isoform f and isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_060798"
FT MUTAGEN 344..497
FT /note="Missing: In ox423; egg-laying defects, dumpy and
FT uncoordinated phenotypes, and progressive paralysis. Highly
FT disorganized nervous system due to axon sprouting defects
FT in late larval stage and adult animals whereby VD and DD
FT motor neurons exhibit extra commissures, misrouted or
FT branched axons, persistent growth cones, and spindly axons.
FT Axon defects accumulate with age. No defects in axon
FT guidance or synapse formation, but there is failure to
FT repress the emergence of new growth cones after they have
FT reached their target. Regeneration of cut axons at the L4
FT larval stage is improved compared to wild-type. Reduces
FT expression of the long isoform of unc-44 in embryos.
FT Locomotion defects are restored in a ssup-72 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:31910362"
SQ SEQUENCE 497 AA; 56809 MW; 52B69F83CA1F8A9A CRC64;
MATMSNDAAA AATWHNNTST PMDTTEPATN SHNPGETAVI GGPEALLLPS GSGPEEMNRH
PLLMAQAHGE HHQPRLLHNF PVIPPPIQQH QQPPLLQQAQ PSQIPHPTQP QIDPTMFTQQ
SGFNWPPIDP NTIAALAQAQ LASSHAQFVS LALTLDPTLL SHFLATQQIP PVPQPLVHKK
AEMELRVGNR FRLGRKIGSG SFGDIYLGQN IQTNEEVAVK LECVKSKHPQ LHIESRLYRI
MLGGIGIPEI RWCGQEGDYN VMVMELLGPS LEDLFNFCQR KFSLKTVLLL ADQMLSRVEF
IHCRDYIHRD IKPDNFLMGL GKRGNLVYII DFGLAKRYRD SKHQHIAYRE NKNLTGTARY
ASINTHRGIE QSRRDDIESL GYVFMYFNRG TLPWQGLKAV TKRQKYELIS EKKISTRVDD
LCAGYPEAFA QYLNYCRSLG FEEQPDYGYL RNLFRTLFHR QQFCYDYVFD WNTYKFYNES
LEARNNFQQA VPNQRRH
