CDKL1_CAEEL
ID CDKL1_CAEEL Reviewed; 353 AA.
AC Q9U2H1;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cyclin-dependent kinase-like 1 {ECO:0000305};
DE EC=2.7.11.22;
GN Name=cdkl-1 {ECO:0000312|WormBase:Y42A5A.4a};
GN ORFNames=Y42A5A.4 {ECO:0000312|WormBase:Y42A5A.4a};
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).
RN [2]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF
RP GLY-11; LYS-33; PRO-169 AND LEU-210.
RX PubMed=29420175; DOI=10.1016/j.celrep.2017.12.083;
RA Canning P., Park K., Goncalves J., Li C., Howard C.J., Sharpe T.D.,
RA Holt L.J., Pelletier L., Bullock A.N., Leroux M.R.;
RT "CDKL Family Kinases Have Evolved Distinct Structural Features and Ciliary
RT Function.";
RL Cell Rep. 22:885-894(2018).
CC -!- FUNCTION: Modulates cilium assembly. {ECO:0000269|PubMed:29420175}.
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=2.7.11.22;
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=2.7.11.22;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:29420175}. Note=Localizes to the ciliary
CC transitional zone in head and tail neurons.
CC {ECO:0000269|PubMed:29420175}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in head and tail ciliated
CC sensory neurons. {ECO:0000269|PubMed:29420175}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; BX284605; CAB63367.1; -; Genomic_DNA.
DR RefSeq; NP_001256291.1; NM_001269362.1.
DR AlphaFoldDB; Q9U2H1; -.
DR SMR; Q9U2H1; -.
DR STRING; 6239.Y42A5A.4b; -.
DR EnsemblMetazoa; Y42A5A.4a.1; Y42A5A.4a.1; WBGene00012779.
DR GeneID; 189841; -.
DR UCSC; Y42A5A.4; c. elegans.
DR CTD; 189841; -.
DR WormBase; Y42A5A.4a; CE20258; WBGene00012779; cdkl-1.
DR GeneTree; ENSGT00940000166615; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR PhylomeDB; Q9U2H1; -.
DR PRO; PR:Q9U2H1; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00012779; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q9U2H1; baseline and differential.
DR GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
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 ATP-binding; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..353
FT /note="Cyclin-dependent kinase-like 1"
FT /id="PRO_0000444245"
FT DOMAIN 4..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 331..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 11
FT /note="G->R: Does not localize to the ciliary transition
FT zone."
FT /evidence="ECO:0000269|PubMed:29420175"
FT MUTAGEN 33
FT /note="K->R: Increases cilium length. Affects localization
FT to the ciliary transition zone."
FT /evidence="ECO:0000269|PubMed:29420175"
FT MUTAGEN 169
FT /note="P->L: Does not affect localization to the ciliary
FT transition zone."
FT /evidence="ECO:0000269|PubMed:29420175"
FT MUTAGEN 210
FT /note="L->P: Does not localize to the ciliary transition
FT zonee."
FT /evidence="ECO:0000269|PubMed:29420175"
SQ SEQUENCE 353 AA; 40666 MW; 7E32260D9849CAC9 CRC64;
MDKYDRLSKL GEGSYGVVYK CKNRDTGQIV AIKKFVETED DPHIKKIALR EIRMLKQLKH
QNLVGLIEVF KRNRKLHLVF ELCDRTVLHE LEKNPHGVND ELIKKIIYQL LEALKFCHSH
KCIHRDVKPE NIFLTRNDQV KLGDFGFARI INTTEMYTDY VATRWYRSPE LLVGDVQYGP
PVDIWAVGCV YAELLTGEAL WPGRSDIDQL YHIRKTLGEF LPRHISIFRT NQFFFGLSIP
EPEHLEPLPS KLPNASSAQL DFLQKCFEMS PDRRFSCSEL MLHGIFSNWI LRIRQDESTP
TGLTSKRSPN YLPLLNGNSN NLVSKNFSLQ GGNHGNNNNN GNGINRNFLP TIS
