ID   CDKL2_RAT               Reviewed;         507 AA.
AC   Q5XIT0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Cyclin-dependent kinase-like 2 {ECO:0000305};
DE            EC=2.7.11.22;
GN   Name=Cdkl2 {ECO:0000312|RGD:1309625};
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 [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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}. Nucleus {ECO:0000250}.
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; BC083590; AAH83590.1; -; mRNA.
DR   RefSeq; NP_001012035.1; NM_001012035.1.
DR   AlphaFoldDB; Q5XIT0; -.
DR   SMR; Q5XIT0; -.
DR   BioGRID; 258108; 1.
DR   iPTMnet; Q5XIT0; -.
DR   PhosphoSitePlus; Q5XIT0; -.
DR   PaxDb; Q5XIT0; -.
DR   PRIDE; Q5XIT0; -.
DR   Ensembl; ENSRNOT00000050038; ENSRNOP00000049130; ENSRNOG00000002506.
DR   GeneID; 305242; -.
DR   KEGG; rno:305242; -.
DR   UCSC; RGD:1309625; rat.
DR   CTD; 8999; -.
DR   RGD; 1309625; Cdkl2.
DR   eggNOG; KOG0593; Eukaryota.
DR   GeneTree; ENSGT00940000160368; -.
DR   InParanoid; Q5XIT0; -.
DR   PRO; PR:Q5XIT0; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000002506; Expressed in frontal cortex and 20 other tissues.
DR   ExpressionAtlas; Q5XIT0; baseline and differential.
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: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; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..507
FT                   /note="Cyclin-dependent kinase-like 2"
FT                   /id="PRO_0000085819"
FT   DOMAIN          4..289
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          365..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           45..51
FT                   /note="[NKR]KIAxRE"
FT   COMPBIAS        370..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   507 AA;  57135 MW;  576D9A4F45A01B81 CRC64;
     MEKYENLGLV GEGSYGMVMK CRNKDSGRIV AIKKFLESDD DKMVKKIAMR EIKLLKQLRH
     ENLVNLLEVC KKKKRWYLVF EFVDHTILDD LKLFPNGLDY QVVQKYLFQI INGIGFCHSH
     NIIHRDIKPE NILVSQSGVV KLCDFGFART LAAPGEVYTD YVATRWYRAP ELLVGDVKYG
     KAVDIWAIGC LVIEMLMGQP LFPGESDIDQ LHHIMTCLGN LIPRHQELFY KNPVFAGVRL
     PEIKDIEAEP LESRYPKLPE VVISLAKKCL HIDPDKRPLC ADLLHHDFFQ MDGFAERFSQ
     ELQLKIEKDA RNNSLPKKFQ IRKKEKDDAL GEERKTLVVQ DTNADPKTKD SKVLKVKGSK
     IDVEKTEKGT RASNGSCLHD NGTSHKGLSS TSLRDCSNVT IDHPRNPGTA IPPLTHNLSA
     VAPGINAAMG TIPGVQNYRV DEKTKKYCNP FVKPSQPSPS GIYNMNVSAS VSNCPLPRKS
     KHSPPLDLAV SMGARRVKLY LETESET