ID   CDKL3_RAT               Reviewed;         593 AA.
AC   Q9JM01; Q9JM02;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   24-JAN-2024, entry version 140.
DE   RecName: Full=Cyclin-dependent kinase-like 3 {ECO:0000305};
DE            EC=2.7.11.22;
DE   AltName: Full=Serine/threonine protein kinase NKIATRE;
GN   Name=Cdkl3 {ECO:0000312|RGD:619874};
GN   Synonyms=Nkiatre {ECO:0000303|PubMed:11161806};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Brain, and Jejunum;
RX   PubMed=11161806; DOI=10.1006/geno.2000.6424;
RA   Haq R., Randall S., Midmer M., Yee K., Zanke B.;
RT   "NKIATRE is a novel conserved cdc2-related kinase.";
RL   Genomics 71:131-141(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-158 AND TYR-160, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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: [Isoform 2]: Nucleus. Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9JM01-1; Sequence=Displayed;
CC       Name=2; Synonyms=NKIATRE alpha, p57 alpha isoform;
CC         IsoId=Q9JM01-2; Sequence=VSP_016159, VSP_016160;
CC       Name=3; Synonyms=NKIATRE beta, p52 beta isoform;
CC         IsoId=Q9JM01-3; Sequence=VSP_016158;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, and to a lower extent in
CC       heart and testis. {ECO:0000269|PubMed:11161806}.
CC   -!- DOMAIN: The [NKR]KIAxRE motif seems to be a cyclin-binding region.
CC   -!- MISCELLANEOUS: [Isoform 2]: Found in the nucleus and cytoplasm.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 3]: Found in the cytoplasm. {ECO:0000305}.
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; AF112183; AAF34870.1; -; mRNA.
DR   EMBL; AF112184; AAF34871.1; -; mRNA.
DR   EMBL; AABR03073386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03074822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03073552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_068540.1; NM_021772.2. [Q9JM01-3]
DR   AlphaFoldDB; Q9JM01; -.
DR   SMR; Q9JM01; -.
DR   STRING; 10116.ENSRNOP00000072310; -.
DR   iPTMnet; Q9JM01; -.
DR   PhosphoSitePlus; Q9JM01; -.
DR   PaxDb; 10116-ENSRNOP00000055819; -.
DR   Ensembl; ENSRNOT00000085895.2; ENSRNOP00000073449.2; ENSRNOG00000059485.2. [Q9JM01-1]
DR   Ensembl; ENSRNOT00055008499; ENSRNOP00055006450; ENSRNOG00055005280. [Q9JM01-1]
DR   Ensembl; ENSRNOT00060043779; ENSRNOP00060036323; ENSRNOG00060025117. [Q9JM01-1]
DR   Ensembl; ENSRNOT00065007990; ENSRNOP00065005577; ENSRNOG00065005389. [Q9JM01-1]
DR   GeneID; 60396; -.
DR   KEGG; rno:60396; -.
DR   UCSC; RGD:619874; rat. [Q9JM01-1]
DR   AGR; RGD:619874; -.
DR   CTD; 51265; -.
DR   RGD; 619874; Cdkl3.
DR   eggNOG; KOG0593; Eukaryota.
DR   GeneTree; ENSGT00940000161317; -.
DR   HOGENOM; CLU_000288_136_1_1; -.
DR   InParanoid; Q9JM01; -.
DR   OrthoDB; 5356570at2759; -.
DR   PhylomeDB; Q9JM01; -.
DR   PRO; PR:Q9JM01; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000054806; Expressed in testis and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA: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; Q9JM01; RN.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..593
FT                   /note="Cyclin-dependent kinase-like 3"
FT                   /id="PRO_0000085823"
FT   DOMAIN          4..286
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          368..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           45..51
FT                   /note="[NKR]KIAxRE"
FT   COMPBIAS        368..399
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..456
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:0007744|PubMed:22673903"
FT   MOD_RES         160
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   VAR_SEQ         458..593
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11161806"
FT                   /id="VSP_016158"
FT   VAR_SEQ         504..505
FT                   /note="DQ -> AK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11161806"
FT                   /id="VSP_016159"
FT   VAR_SEQ         506..593
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11161806"
FT                   /id="VSP_016160"
SQ   SEQUENCE   593 AA;  67553 MW;  40F8C846EA421E0B CRC64;
     MEMYETLGKV GEGSYGTVMK CKHKDTGRIV AIKIFYEKPE KSVNKIATRE IKFLKQFRHE
     NLVNLIEVFR QKKKIHLVFE FIDHTVLDEL QHYCHGLESK RLRKYLFQIL RAIEYLHNNN
     IIHRDIKPEN ILVSQSGITK LCDFGFARTL AAPGDVYTDY VATRWYRAPE LVLKDTTYGK
     PVDIWALGCM IIEMATGNPY LPSSSDLDLL HKIVLKVGNL TPHLHNIFSK SPIFAGVVLP
     QVQHPKNARK KYPKLNGLLA DIVHACLQID PAERISSTDL LHHDYFTRDG FIEKFIPELR
     AKLLQEAKVN SFIKPKENFK ENEPVRDEKK PVFTNPLLYG NPTLYGKEVD RDKRAKELKV
     RVIKAKGGKG DVPDLKKTES EGEHRQQGTA EDTHPTSLDR KPSVSELTNP VHPSANSDTV
     KEDPHSGGCM IMPPINLTSS NLLAANPSSN LSHPNSRLTE RTKKRRTSSQ TIGQTLSNSR
     QEDTGPTQVQ TEKGAFNERT GQNDQIASGN KRKLNFSKCD RKEFHFPELP FTIQAKEMKG
     MEVKQIKVLK RESKKTDSPK IPTLLSMDSN QEKQEVFNIF PGWCKRGNLN WPS
//