CDKL3_RAT
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 03-AUG-2022, entry version 135.
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.ENSRNOP00000055819; -.
DR iPTMnet; Q9JM01; -.
DR PhosphoSitePlus; Q9JM01; -.
DR PaxDb; Q9JM01; -.
DR PRIDE; Q9JM01; -.
DR Ensembl; ENSRNOT00000085895; ENSRNOP00000073449; ENSRNOG00000059485. [Q9JM01-1]
DR GeneID; 60396; -.
DR KEGG; rno:60396; -.
DR UCSC; RGD:619874; rat. [Q9JM01-1]
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; 398098at2759; -.
DR PhylomeDB; Q9JM01; -.
DR PRO; PR:Q9JM01; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000054806; Expressed in testis and 19 other tissues.
DR Genevisible; Q9JM01; RN.
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; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0097484; P:dendrite extension; IMP:MGI.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:MGI.
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 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
