ID   CDK5_DROME              Reviewed;         294 AA.
AC   P48609; Q94878; Q9V7D8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   04-NOV-2026, entry version 200.
DE   RecName: Full=Cyclin-dependent kinase 5 homolog;
DE            EC=2.7.11.22;
DE   AltName: Full=Cell division protein kinase 5;
GN   Name=Cdk5; ORFNames=CG8203;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=Oregon-R;
RX   PubMed=7805863; DOI=10.1016/0014-5793(94)01298-9;
RA   Hellmich M.R., Kennison J.A., Hampton L.L., Battey J.F.;
RT   "Cloning and characterization of the Drosophila melanogaster CDK5
RT   homolog.";
RL   FEBS Lett. 356:317-321(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=8930898; DOI=10.1091/mbc.7.11.1759;
RA   Sauer K., Weigmann K., Sigrist S., Lehner C.F.;
RT   "Novel members of the cdc2-related kinase family in Drosophila: cdk4/6,
RT   cdk5, PFTAIRE, and PITSLRE kinase.";
RL   Mol. Biol. Cell 7:1759-1769(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=23720047; DOI=10.1242/dev.087338;
RA   Jauffred B., Llense F., Sommer B., Wang Z., Martin C., Bellaiche Y.;
RT   "Regulation of centrosome movements by numb and the collapsin response
RT   mediator protein during Drosophila sensory progenitor asymmetric
RT   division.";
RL   Development 140:2657-2668(2013).
CC   -!- FUNCTION: Probably involved in the control of the cell cycle. Interacts
CC       with D1 and D3-type G1 cyclins. Possible regulator of neuronal
CC       differentiation and/or development (By similarity). Regulates
CC       asymmetric centrosome movement during asymmetric cell division of
CC       sensory organ precursor cells (PubMed:23720047). {ECO:0000250,
CC       ECO:0000269|PubMed:23720047}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC   -!- INTERACTION:
CC       P48609; P25008: CycC; NbExp=4; IntAct=EBI-94216, EBI-195485;
CC   -!- DEVELOPMENTAL STAGE: Abundantly expressed in all adult tissues
CC       (PubMed:7805863, PubMed:8930898). Lower levels found in larvae and
CC       early embryos. Barely detectable in late embryos (PubMed:8930898).
CC       {ECO:0000269|PubMed:7805863, ECO:0000269|PubMed:8930898}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down in sensory organ
CC       precursor cells reduces the efficiency of centrosome polarization
CC       during asymmetric cell division. {ECO:0000269|PubMed:23720047}.
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; U21552; AAA63754.1; -; Genomic_DNA.
DR   EMBL; X99511; CAA67861.1; -; mRNA.
DR   EMBL; AE013599; AAF58119.1; -; Genomic_DNA.
DR   EMBL; AY061049; AAL28597.1; -; mRNA.
DR   PIR; S51008; S51008.
DR   RefSeq; NP_477080.1; NM_057732.4.
DR   AlphaFoldDB; P48609; -.
DR   SMR; P48609; -.
DR   BioGRID; 62461; 44.
DR   DIP; DIP-22131N; -.
DR   FunCoup; P48609; 870.
DR   IntAct; P48609; 41.
DR   STRING; 7227.FBpp0086483; -.
DR   iPTMnet; P48609; -.
DR   PaxDb; 7227-FBpp0086483; -.
DR   PeptideAtlas; P48609; -.
DR   DNASU; 36727; -.
DR   EnsemblMetazoa; FBtr0087350; FBpp0086483; FBgn0013762.
DR   GeneID; 36727; -.
DR   KEGG; dme:Dmel_CG8203; -.
DR   AGR; FB:FBgn0013762; -.
DR   CTD; 1020; -.
DR   FlyBase; FBgn0013762; Cdk5.
DR   VEuPathDB; VectorBase:FBgn0013762; -.
DR   eggNOG; KOG0662; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; P48609; -.
DR   OMA; AADDCMM; -.
DR   OrthoDB; 1732493at2759; -.
DR   PhylomeDB; P48609; -.
DR   BRENDA; 2.7.11.22; 1994.
DR   Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-DME-9841922; MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis.
DR   SignaLink; P48609; -.
DR   BioGRID-ORCS; 36727; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 36727; -.
DR   PRO; PR:P48609; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0013762; Expressed in embryonic/larval hemocyte (Drosophila) and 105 other cell types or tissues.
DR   GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016533; C:protein kinase 5 complex; IPI:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:FlyBase.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR   GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR   GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR   GO; GO:0007629; P:flight behavior; IMP:FlyBase.
DR   GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IGI:FlyBase.
DR   GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR   GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR   GO; GO:0051402; P:neuron apoptotic process; IBA:GO_Central.
DR   GO; GO:1901987; P:regulation of cell cycle phase transition; IBA:GO_Central.
DR   GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR   GO; GO:0048489; P:synaptic vesicle transport; IBA:GO_Central.
DR   CDD; cd07839; STKc_CDK5; 1.
DR   FunFam; 3.30.200.20:FF:000144; Cyclin-dependent kinase 5; 1.
DR   FunFam; 1.10.510.10:FF:000184; cyclin-dependent kinase 5 homolog; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR050108; CDK.
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   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF46; CYCLIN-DEPENDENT KINASE 5; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..294
FT                   /note="Cyclin-dependent kinase 5 homolog"
FT                   /id="PRO_0000085788"
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         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        25
FT                   /note="D -> A (in Ref. 1; AAA63754)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166
FT                   /note="W -> L (in Ref. 1; AAA63754)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   294 AA;  33180 MW;  E6B7B37B2410AA23 CRC64;
     MQKYDKMEKI GEGTYGTVFK GRNRDTMEIV ALKRVRLDED DEGVPSSALR EICLLKELKH
     KNIVRLIDVL HSDKKLTLVF EHCDQDLKKY FDSLNGEIDM AVCRSFMLQL LRGLAFCHSH
     NVLHRDLKPQ NLLINKNGEL KLADFGLARA FGIPVKCYSA EVVTLWYRPP DVLFGAKLYT
     TSIDMWSAGC ILAELADAGR PLFPGSDVLD QLMKIFRVLG TPNEDSWPGV SHLSDYVALP
     SFPAITSWSQ LVPRLNSKGR DLLQKLLICR PNQRISAEAA MQHPYFTDSS SSGH
//