ID   CDKL3_MOUSE             Reviewed;         595 AA.
AC   Q8BLF2; A2ACR7; A2ACR8; A2ACR9; A2ACS0; A2ACS1; Q5M6W2; Q8BKR2; Q8BL49;
AC   Q8BLN9; Q8BVE0; Q8K134;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   24-JAN-2024, entry version 151.
DE   RecName: Full=Cyclin-dependent kinase-like 3 {ECO:0000305};
DE            EC=2.7.11.22;
GN   Name=Cdkl3 {ECO:0000312|MGI:MGI:2388268};
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] (ISOFORMS 1; 2; 5 AND 6), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-595 (ISOFORM 7).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Corpora quadrigemina, Embryo, and Embryonic lung;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=FVB/N; TISSUE=Kidney;
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:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=Q8BLF2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BLF2-2; Sequence=VSP_016154, VSP_016157;
CC       Name=3;
CC         IsoId=Q8BLF2-7; Sequence=VSP_016155, VSP_016156;
CC       Name=4;
CC         IsoId=Q8BLF2-4; Sequence=VSP_016150, VSP_016151;
CC       Name=5;
CC         IsoId=Q8BLF2-5; Sequence=VSP_016149, VSP_016155, VSP_016156;
CC       Name=6;
CC         IsoId=Q8BLF2-6; Sequence=VSP_016152;
CC       Name=7;
CC         IsoId=Q8BLF2-8; Sequence=VSP_030154;
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; AK043995; BAC31729.2; -; mRNA.
DR   EMBL; AK045356; BAC32324.1; -; mRNA.
DR   EMBL; AK046394; BAC32701.1; -; mRNA.
DR   EMBL; AK050990; BAC34488.1; -; mRNA.
DR   EMBL; AK078804; BAC37400.1; -; mRNA.
DR   EMBL; AL669920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC028871; AAH28871.1; -; mRNA.
DR   CCDS; CCDS24665.1; -. [Q8BLF2-1]
DR   CCDS; CCDS48788.1; -. [Q8BLF2-7]
DR   CCDS; CCDS48790.1; -. [Q8BLF2-2]
DR   CCDS; CCDS48791.1; -. [Q8BLF2-6]
DR   CCDS; CCDS48792.1; -. [Q8BLF2-4]
DR   RefSeq; NP_001160125.1; NM_001166653.1.
DR   RefSeq; NP_001160126.1; NM_001166654.1. [Q8BLF2-2]
DR   RefSeq; NP_001160127.1; NM_001166655.1. [Q8BLF2-6]
DR   RefSeq; NP_001160128.1; NM_001166656.1. [Q8BLF2-7]
DR   RefSeq; NP_001160129.1; NM_001166657.1. [Q8BLF2-4]
DR   RefSeq; NP_722480.3; NM_153785.4. [Q8BLF2-1]
DR   RefSeq; XP_011247178.1; XM_011248876.1.
DR   RefSeq; XP_011247179.1; XM_011248877.2.
DR   RefSeq; XP_011247180.1; XM_011248878.1. [Q8BLF2-2]
DR   RefSeq; XP_011247181.1; XM_011248879.1.
DR   RefSeq; XP_011247182.1; XM_011248880.2.
DR   RefSeq; XP_017169911.1; XM_017314422.1.
DR   AlphaFoldDB; Q8BLF2; -.
DR   SMR; Q8BLF2; -.
DR   BioGRID; 229399; 1.
DR   STRING; 10090.ENSMUSP00000113303; -.
DR   iPTMnet; Q8BLF2; -.
DR   PhosphoSitePlus; Q8BLF2; -.
DR   SwissPalm; Q8BLF2; -.
DR   MaxQB; Q8BLF2; -.
DR   PaxDb; 10090-ENSMUSP00000064315; -.
DR   ProteomicsDB; 281562; -. [Q8BLF2-1]
DR   ProteomicsDB; 281563; -. [Q8BLF2-2]
DR   ProteomicsDB; 281564; -. [Q8BLF2-7]
DR   ProteomicsDB; 281565; -. [Q8BLF2-4]
DR   ProteomicsDB; 281566; -. [Q8BLF2-5]
DR   ProteomicsDB; 281567; -. [Q8BLF2-6]
DR   ProteomicsDB; 281568; -. [Q8BLF2-8]
DR   Antibodypedia; 2061; 242 antibodies from 29 providers.
DR   DNASU; 213084; -.
DR   Ensembl; ENSMUST00000063303.11; ENSMUSP00000064315.5; ENSMUSG00000020389.20. [Q8BLF2-1]
DR   Ensembl; ENSMUST00000063321.13; ENSMUSP00000065128.7; ENSMUSG00000020389.20. [Q8BLF2-7]
DR   Ensembl; ENSMUST00000109076.2; ENSMUSP00000104704.2; ENSMUSG00000020389.20. [Q8BLF2-4]
DR   Ensembl; ENSMUST00000109077.9; ENSMUSP00000104705.3; ENSMUSG00000020389.20. [Q8BLF2-4]
DR   Ensembl; ENSMUST00000109078.8; ENSMUSP00000104706.2; ENSMUSG00000020389.20. [Q8BLF2-6]
DR   Ensembl; ENSMUST00000109079.9; ENSMUSP00000104707.3; ENSMUSG00000020389.20. [Q8BLF2-7]
DR   Ensembl; ENSMUST00000109081.9; ENSMUSP00000104709.3; ENSMUSG00000020389.20. [Q8BLF2-2]
DR   Ensembl; ENSMUST00000121591.8; ENSMUSP00000112477.2; ENSMUSG00000020389.20. [Q8BLF2-2]
DR   GeneID; 213084; -.
DR   KEGG; mmu:213084; -.
DR   UCSC; uc007iuv.2; mouse. [Q8BLF2-1]
DR   UCSC; uc007iux.2; mouse. [Q8BLF2-4]
DR   UCSC; uc007iuz.2; mouse. [Q8BLF2-2]
DR   UCSC; uc011xul.1; mouse. [Q8BLF2-7]
DR   AGR; MGI:2388268; -.
DR   CTD; 51265; -.
DR   MGI; MGI:2388268; Cdkl3.
DR   VEuPathDB; HostDB:ENSMUSG00000020389; -.
DR   eggNOG; KOG0593; Eukaryota.
DR   GeneTree; ENSGT00940000161317; -.
DR   HOGENOM; CLU_000288_136_1_1; -.
DR   InParanoid; Q8BLF2; -.
DR   OMA; GMEVKQV; -.
DR   OrthoDB; 5356570at2759; -.
DR   TreeFam; TF101031; -.
DR   BioGRID-ORCS; 213084; 3 hits in 81 CRISPR screens.
DR   ChiTaRS; Cdkl3; mouse.
DR   PRO; PR:Q8BLF2; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8BLF2; Protein.
DR   Bgee; ENSMUSG00000020389; Expressed in spermatid and 116 other cell types or tissues.
DR   ExpressionAtlas; Q8BLF2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
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:0097484; P:dendrite extension; IMP:MGI.
DR   GO; GO:0030517; P:negative regulation of axon extension; IMP:MGI.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:MGI.
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:SF177; CYCLIN-DEPENDENT KINASE-LIKE 3; 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; Q8BLF2; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..595
FT                   /note="Cyclin-dependent kinase-like 3"
FT                   /id="PRO_0000085822"
FT   DOMAIN          4..286
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          362..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           45..51
FT                   /note="[NKR]KIAxRE"
FT   COMPBIAS        362..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        125
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"
FT   MOD_RES         158
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JM01"
FT   MOD_RES         160
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JM01"
FT   VAR_SEQ         1..17
FT                   /note="MEMYETLGKVGEGSYGT -> MKPLEKWEREVMEP (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_016149"
FT   VAR_SEQ         295..353
FT                   /note="FIPELRAKLLQEAKVNSFIKPKENFKENEPVRDEKKSVFTNTLLYGNPSLYG
FT                   KEVDRDK -> KWTETKGPRSSKSESLRPKGAKEMSQTRRSQSMKATTASRAQLMTHSP
FT                   HHWTRSLLSWN (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016150"
FT   VAR_SEQ         354..595
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016151"
FT   VAR_SEQ         458..595
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_016152"
FT   VAR_SEQ         576..595
FT                   /note="GGDGDCEGKNLKRNRFFFSR -> QPVKQVNSNQ (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030154"
FT   VAR_SEQ         576..585
FT                   /note="GGDGDCEGKN -> QSARHLPGQC (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_016154"
FT   VAR_SEQ         576..581
FT                   /note="GGDGDC -> SLTMYL (in isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_016155"
FT   VAR_SEQ         582..595
FT                   /note="Missing (in isoform 3 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_016156"
FT   VAR_SEQ         586..595
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_016157"
FT   CONFLICT        12
FT                   /note="E -> Q (in Ref. 1; BAC32701)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="H -> Y (in Ref. 1; BAC37400)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        153
FT                   /note="P -> H (in Ref. 1; BAC32324)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        352
FT                   /note="D -> E (in Ref. 1; BAC37400)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   595 AA;  67739 MW;  3DB415A3EEBC7C4B CRC64;
     MEMYETLGKV GEGSYGTVMK CKHKDTGRIV AIKIFYEKPE KSVNKIATRE IKFLKQFRHE
     NLVNLIEVFR QKKKIHLVFE FIDHTVLDEL QHYCHGLESK RLRKYLFQIL RAIEYLHNNN
     IIHRDIKPEN ILVSQSGITK LCDFGFARTL AAPGDVYTDY VATRWYRAPE LVLKDTSYGK
     PVDIWALGCM IIEMATGHPF LPSSSDLDLL HKIVLKVGNL TPHLHNIFSK SPIFAGVVLP
     QVQHPKTARK KYPKLNGLLA DIVHACLQID PAERTSSTDL LRHDYFTRDG FIEKFIPELR
     AKLLQEAKVN SFIKPKENFK ENEPVRDEKK SVFTNTLLYG NPSLYGKEVD RDKRAKELKV
     RVIKAKGGKG DVPDQKKPEY EGDHRQQGTA DDTQPSSLDK KPSVLELTNP LNPSENSDGV
     KEDPHAGGCM IMPPINLTSS NLLAANLSSN LSHPNSRLTE RTKKRRTSSQ TIGQTLSNSR
     QEDTGPTQVQ TEKGAFNERT GQNDQISSGN KRKLNFPKCD RKEFHFPELP FTVQAKEMKG
     MEVKQIKVLK RESKKTDSSK IPTLLSMDPN QEKQEGGDGD CEGKNLKRNR FFFSR
//