ID   CDK14_XENLA             Reviewed;         435 AA.
AC   Q6DJM7;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Cyclin-dependent kinase 14;
DE            EC=2.7.11.22;
DE   AltName: Full=Cell division protein kinase 14;
GN   Name=cdk14; Synonyms=pftk1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine/threonine-protein kinase involved in the control of
CC       the eukaryotic cell cycle, whose activity is controlled by an
CC       associated cyclin. Acts as a cell-cycle regulator of Wnt signaling
CC       pathway during G2/M phase by mediating the phosphorylation of lrp6,
CC       leading to the activation of the Wnt signaling pathway (By similarity).
CC       {ECO:0000250}.
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   -!- SUBUNIT: Interacts with ccny; ccny mediates its recruitment to the
CC       plasma membrane and promotes phosphorylation of lrp6. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Note=Recruited to the cell membrane by CCNY.
CC       {ECO:0000250}.
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; BC075148; AAH75148.1; -; mRNA.
DR   RefSeq; NP_001086352.1; NM_001092883.1.
DR   AlphaFoldDB; Q6DJM7; -.
DR   SMR; Q6DJM7; -.
DR   DNASU; 444781; -.
DR   GeneID; 444781; -.
DR   CTD; 444781; -.
DR   Xenbase; XB-GENE-943254; cdk14.L.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 444781; Expressed in internal ear and 15 other tissues.
DR   GO; GO:0000308; C:cytoplasmic cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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; Cell cycle; Cell division; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Wnt signaling pathway.
FT   CHAIN           1..435
FT                   /note="Cyclin-dependent kinase 14"
FT                   /id="PRO_0000391903"
FT   DOMAIN          101..385
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          75..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        222
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         107..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         130
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   435 AA;  49230 MW;  1EECF4593408FD2C CRC64;
     MCDMIESQPA QKIGKMKKLR RTLSDSFSRI ALKKDENAID EICVTKMSTR NCQGIDSVIK
     HLDPIPEDKK VRVQRTQSSF DPFEKTSNQP TSPKFGKADS YEKLEKLGEG SYATVFKGKS
     KVNGKLVALK VIRLQEEEGT PFTAIREASL LKGLKHANIV LLHDIIHTKE TLTLVFEYVH
     TDLCQYMDKH PGGLNPENVK LFLFQLLRGL SYIHQGHILH RDLKPQNLLI SDTGELKLAD
     FGLARAKSVP SHTYSNEVVT LWYRPPDVLL GSTDYSTCLD MWGVGCIFVE MIQGVAAFPG
     MKDIQDQLER IFLILGTPIE ETWPAVHSLP HFEPERFTLY GPKNLRQAWN KLSYVNHAED
     LASKLLQCFP KNRLSAQAAL NHDYFSDLPP RLWELSDMSS IFTVPNVKLQ PEAGESMRVF
     GKNNSFSKSL SNSKH