ID   CDK4_XENLA              Reviewed;         319 AA.
AC   Q91727;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Cyclin-dependent kinase 4;
DE            EC=2.7.11.22;
DE   AltName: Full=Cell division protein kinase 4;
GN   Name=cdk4;
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 [MRNA].
RA   Cockerill M.J., Hunt T.;
RT   "D-type cyclins in Xenopus laevis.";
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably involved in the control of the cell cycle.
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   -!- ACTIVITY REGULATION: Phosphorylation at Thr-172 is necessary for
CC       enzymatic activity. {ECO:0000250}.
CC   -!- SUBUNIT: Forms a stable complex with D-type G1 cyclins.
CC       {ECO:0000250|UniProtKB:P11802}.
CC   -!- INTERACTION:
CC       Q91727; P50755: ccnd1; NbExp=2; IntAct=EBI-7270544, EBI-7270567;
CC       Q91727; Q6GLD3: ccnd1; Xeno; NbExp=2; IntAct=EBI-7270544, EBI-7270670;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11802}.
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; X89477; CAA61666.1; -; mRNA.
DR   PIR; S57926; S57926.
DR   RefSeq; NP_001079719.1; NM_001086250.1.
DR   AlphaFoldDB; Q91727; -.
DR   SMR; Q91727; -.
DR   BioGRID; 97649; 1.
DR   IntAct; Q91727; 2.
DR   MINT; Q91727; -.
DR   DNASU; 379406; -.
DR   GeneID; 379406; -.
DR   KEGG; xla:379406; -.
DR   CTD; 379406; -.
DR   Xenbase; XB-GENE-5900736; cdk4.S.
DR   OrthoDB; 988547at2759; -.
DR   Proteomes; UP000186698; Chromosome 2S.
DR   Bgee; 379406; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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   ATP-binding; Cell cycle; Cell division; Cytoplasm; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..319
FT                   /note="Cyclin-dependent kinase 4"
FT                   /id="PRO_0000085782"
FT   DOMAIN          9..295
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        140
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         15..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         172
FT                   /note="Phosphothreonine; by CAK"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   319 AA;  35684 MW;  235329790C4022A7 CRC64;
     MSKEMKGQYE PVAEIGVGAY GTVYKARDLQ SGKFVALKNV RVQTNENGLP LSTVREVTLL
     KRLEHFDHPN IVKLMDVCAS ARTDRETKVT LVFEHVDQDL KTYLSKVPPP GLPLETIKDL
     MKQFLSGLEF LHLNCIVHRD LKPENILVTS GGQVKLADFG LARIYSCQMA LTPVVVTLWY
     RAPEVLLQST YATPVDVWSA GCIFAEMFKR KPLFCGNSEA DQLCKIFDII GLPSEEEWPV
     DVTLPRSAFS PRTQQPVDKF VPEIDAMGAD LLLAMLTFSP QKRISASDAL LHPFFADDPQ
     ACSKQEHFTH ICTATDEVK