CDK20_DANRE
ID CDK20_DANRE Reviewed; 344 AA.
AC A8WIP6; Q5PRE2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cyclin-dependent kinase 20;
DE EC=2.7.11.22;
DE AltName: Full=Cell cycle-related kinase;
DE AltName: Full=Cell division protein kinase 20;
GN Name=cdk20; Synonyms=ccrk; ORFNames=si:dkeyp-77f7.1, zgc:101530;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=20159594; DOI=10.1016/j.devcel.2009.12.014;
RA Ko H.W., Norman R.X., Tran J., Fuller K.P., Fukuda M., Eggenschwiler J.T.;
RT "Broad-minded links cell cycle-related kinase to cilia assembly and
RT hedgehog signal transduction.";
RL Dev. Cell 18:237-247(2010).
CC -!- FUNCTION: Involved in cell growth. Activates cdk2, a kinase involved in
CC the control of the cell cycle, by phosphorylating residue 'Thr-160' (By
CC similarity). Required for high-level Shh responses in the developing
CC neural tube. Together with tbc1d32, controls the structure of the
CC primary cilium by coordinating assembly of the ciliary membrane and
CC axoneme, allowing gli2 to be properly activated in response to SHH
CC signaling. {ECO:0000250, ECO:0000269|PubMed:20159594}.
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 -!- SUBUNIT: Monomer. Interacts with tbc1d32. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell projection, cilium {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Fish lacking cdk20 are viable during
CC embryogenesis and early larval stages, but exhibit curvature of the
CC body axis and curled cilia in distal kidney tubules.
CC {ECO:0000269|PubMed:20159594}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH86697.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BX571687; CAP19557.1; -; Genomic_DNA.
DR EMBL; BC086697; AAH86697.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001008655.1; NM_001008655.1.
DR RefSeq; XP_005166746.1; XM_005166689.3.
DR AlphaFoldDB; A8WIP6; -.
DR SMR; A8WIP6; -.
DR STRING; 7955.ENSDARP00000113146; -.
DR PaxDb; A8WIP6; -.
DR Ensembl; ENSDART00000140098; ENSDARP00000113146; ENSDARG00000003867.
DR GeneID; 494112; -.
DR KEGG; dre:494112; -.
DR CTD; 23552; -.
DR ZFIN; ZDB-GENE-041212-84; cdk20.
DR eggNOG; KOG0659; Eukaryota.
DR GeneTree; ENSGT00940000159128; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; A8WIP6; -.
DR OMA; KITFPYH; -.
DR OrthoDB; 1367115at2759; -.
DR PhylomeDB; A8WIP6; -.
DR TreeFam; TF327240; -.
DR PRO; PR:A8WIP6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000003867; Expressed in testis and 15 other tissues.
DR ExpressionAtlas; A8WIP6; baseline.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0006468; P:protein phosphorylation; 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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Cell projection; Cilium; Cytoplasm;
KW Developmental protein; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..344
FT /note="Cyclin-dependent kinase 20"
FT /id="PRO_0000393616"
FT DOMAIN 4..288
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
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"
SQ SEQUENCE 344 AA; 39025 MW; D4C820FAF9C7FB62 CRC64;
MDQYSILGRI GEGAHGIVFK AKHIETGETV ALKKVALRRL EDGIPNQALR EIKALQEIED
NQYVVKLKDV FPHGTGFVLV FEYMLSDLSE VIRNSQRPLT ASQVKSYMMM LLKGVAFCHE
NSIMHRDLKP ANLLISSTGH LKIADFGLAR LFSNEGDRLY SHQVATRWYR APELLYGARK
YDEGVDLWAV GCIFGELLNN SPLFPGENDI EQLCCVLRVL GTPNQKVWPE ITELPDYNKI
TFKENPPIPL EEIVPDTSPQ AVDLLKKFLV YPSKQRISAR QALLHPYFFT DPLPAHHSEL
PIPQRGGKHS RQRMQPPHEF TVDRPLHESV VDPSLIQKHA MSCS
