ID   CDKL4_MOUSE             Reviewed;         342 AA.
AC   Q3TZA2; B2RSS7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 123.
DE   RecName: Full=Cyclin-dependent kinase-like 4;
DE            EC=2.7.11.22;
GN   Name=Cdkl4; Synonyms=Gm942;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The [NKR]KIAxRE motif seems to be a cyclin-binding region.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR   EMBL; AK157995; BAE34307.1; -; mRNA.
DR   EMBL; BC138986; AAI38987.1; -; mRNA.
DR   EMBL; BC138988; AAI38989.1; -; mRNA.
DR   CCDS; CCDS28992.1; -.
DR   RefSeq; NP_001028615.1; NM_001033443.4.
DR   RefSeq; XP_006524589.1; XM_006524526.1.
DR   RefSeq; XP_006524590.1; XM_006524527.3.
DR   RefSeq; XP_011244823.1; XM_011246521.2.
DR   AlphaFoldDB; Q3TZA2; -.
DR   SMR; Q3TZA2; -.
DR   STRING; 10090.ENSMUSP00000157063; -.
DR   iPTMnet; Q3TZA2; -.
DR   PhosphoSitePlus; Q3TZA2; -.
DR   MaxQB; Q3TZA2; -.
DR   PaxDb; 10090-ENSMUSP00000083732; -.
DR   ProteomicsDB; 281355; -.
DR   Antibodypedia; 29610; 214 antibodies from 25 providers.
DR   DNASU; 381113; -.
DR   Ensembl; ENSMUST00000086545.5; ENSMUSP00000083732.5; ENSMUSG00000033966.9.
DR   Ensembl; ENSMUST00000234349.2; ENSMUSP00000157316.2; ENSMUSG00000033966.9.
DR   Ensembl; ENSMUST00000234602.2; ENSMUSP00000157063.2; ENSMUSG00000033966.9.
DR   GeneID; 381113; -.
DR   KEGG; mmu:381113; -.
DR   UCSC; uc008dri.2; mouse.
DR   AGR; MGI:3587025; -.
DR   CTD; 344387; -.
DR   MGI; MGI:3587025; Cdkl4.
DR   VEuPathDB; HostDB:ENSMUSG00000033966; -.
DR   eggNOG; KOG0593; Eukaryota.
DR   GeneTree; ENSGT00940000161857; -.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; Q3TZA2; -.
DR   OMA; HNTPTPD; -.
DR   OrthoDB; 244018at2759; -.
DR   PhylomeDB; Q3TZA2; -.
DR   TreeFam; TF101031; -.
DR   BioGRID-ORCS; 381113; 0 hits in 81 CRISPR screens.
DR   ChiTaRS; Cdkl4; mouse.
DR   PRO; PR:Q3TZA2; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q3TZA2; Protein.
DR   Bgee; ENSMUSG00000033966; Expressed in otolith organ and 97 other cell types or tissues.
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; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07847; STKc_CDKL1_4; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF120; CYCLIN-DEPENDENT KINASE-LIKE 4; 1.
DR   Pfam; PF12330; Haspin_kinase; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q3TZA2; MM.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..342
FT                   /note="Cyclin-dependent kinase-like 4"
FT                   /id="PRO_0000085825"
FT   DOMAIN          4..286
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          295..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           45..51
FT                   /note="[NKR]KIAxRE"
FT   ACT_SITE        126
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   342 AA;  39446 MW;  384426A832F4D7C8 CRC64;
     MEKYEKLAKI GEGSYGVVFK CRNKSSGQVV AIKKFVESED DRVVRKIALR EIRMLKQLKH
     PNLVNLIEVF RRKRKMHLVF EYCDHTLLNE LERNPNGVSD GVIKSVLWQT LQALNFCHKH
     NCIHRDVKPE NILITKQGMI KICDFGFARI LIPGDAYTDY VATRWYRAPE LLVGDTKYGS
     SVDVWAVGCV FAELLTGQPL WPGKSDVDQL YLIIRTLGKL IPRHQSIFRS NQFFRGISIP
     EPEDMETLEE KFSNVQPVAL SFMKGCLKMN PDERLTCAQL LDSAYFESFQ EDQMKRKARS
     EGRSRRRQQN QLLPLIPGSH ISPTPDGRKQ VVQLKFDHLP NI
//