CDK5_XENLA
ID CDK5_XENLA Reviewed; 292 AA.
AC P51166; Q6GQ54;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cyclin-dependent-like kinase 5;
DE EC=2.7.11.1;
DE AltName: Full=Cell division protein kinase 5;
DE AltName: Full=Neuronal cyclin-dependent kinase 5;
GN Name=cdk5;
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].
RC STRAIN=Periodic albino; TISSUE=Brain;
RX PubMed=8750877; DOI=10.1016/0169-328x(95)00109-6;
RA Gervasi C., Szaro B.G.;
RT "The Xenopus laevis homologue to the neuronal cyclin-dependent kinase
RT (cdk5) is expressed in embryos by gastrulation.";
RL Brain Res. Mol. Brain Res. 33:192-200(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Proline-directed serine/threonine-protein kinase essential
CC for neuronal cell cycle arrest and differentiation and may be involved
CC in apoptotic cell death in neuronal diseases by triggering abortive
CC cell cycle re-entry. Interacts with D1 and D3-type G1 cyclins.
CC Regulates several neuronal development and physiological processes
CC including neuronal survival, migration and differentiation, axonal and
CC neurite growth, synaptogenesis, oligodendrocyte differentiation,
CC synaptic plasticity and neurotransmission, by phosphorylating key
CC proteins. In the mature central nervous system (CNS), regulates
CC neurotransmitter movements by phosphorylating substrates associated
CC with neurotransmitter release and synapse plasticity; synaptic vesicle
CC exocytosis, vesicles fusion with the presynaptic membrane, and
CC endocytosis. May regulate endothelial cell migration and angiogenesis
CC via the modulation of lamellipodia formation. The complex p35/CDK5 may
CC participate in the regulation of the circadian clock.
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=2.7.11.1;
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=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Perikaryon {ECO:0000250}. Cell projection, growth cone {ECO:0000250}.
CC Cell projection, lamellipodium {ECO:0000250}. Postsynaptic density
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; U24397; AAB37091.1; -; mRNA.
DR EMBL; BC072894; AAH72894.1; -; mRNA.
DR RefSeq; NP_001084086.1; NM_001090617.1.
DR AlphaFoldDB; P51166; -.
DR SMR; P51166; -.
DR MaxQB; P51166; -.
DR PRIDE; P51166; -.
DR DNASU; 399296; -.
DR GeneID; 399296; -.
DR KEGG; xla:399296; -.
DR CTD; 399296; -.
DR Xenbase; XB-GENE-6254177; cdk5.L.
DR OrthoDB; 1010560at2759; -.
DR BRENDA; 2.7.11.22; 6725.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 399296; Expressed in oocyte and 19 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0030549; F:acetylcholine receptor activator activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005176; F:ErbB-2 class receptor binding; ISS:UniProtKB.
DR GO; GO:0043125; F:ErbB-3 class receptor binding; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0050321; F:tau-protein kinase activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; 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 Acetylation; ATP-binding; Biological rhythms; Cell cycle; Cell division;
KW Cell membrane; Cell projection; Cytoplasm; Kinase; Membrane; Neurogenesis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..292
FT /note="Cyclin-dependent-like kinase 5"
FT /id="PRO_0000085787"
FT DOMAIN 4..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 17
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 239
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 292 AA; 33339 MW; 7692C6B610DC7284 CRC64;
MQKYEKLEKI GEGTYGTVFK AKNRDTHEIV ALKRVRLDDD DEGVPSSALR EICLLKELKH
KNIVRLHDVL HSDKKLTLVF EFCDQDLKKY FDSCNGDLDP EIVKSFMYQL LKGLAFCHSR
NVLHRDLKPQ NLLINRNGEL KLADFGLARA FGIPVRCYSA EVVTLWYRPP DVLFGAKLYS
TSIDMWSAGC IFAELANAGR PLFPGNDVDD QLKRIFRLLG TPTEEQWPAM TKLPDYKPYP
MYPATMSLVN VVPKLNATGR DLLQNLLKCN PVQRICADEA LQHPYFADFC PP
