ID PLK4_DROSI Reviewed; 769 AA.
AC B4QK53;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Serine/threonine-protein kinase PLK4;
DE EC=2.7.11.21;
DE AltName: Full=Polo-like kinase 4;
DE Short=PLK-4;
DE AltName: Full=Serine/threonine-protein kinase SAK;
GN Name=SAK; ORFNames=GD12112;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Serine/threonine-protein kinase that plays a central role in
CC centriole duplication. Able to trigger procentriole formation on the
CC surface of the mother centriole cylinder, using mother centriole as a
CC platform, leading to the recruitment of centriole biogenesis proteins
CC such as sas-6. When overexpressed, it is able to induce centrosome
CC amplification through the simultaneous generation of multiple
CC procentrioles adjoining each parental centriole during S phase.
CC Centrosome amplification following overexpression can initiate
CC tumorigenesis, highlighting the importance of centrosome regulation in
CC cancers (By similarity). {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=2.7.11.21;
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=2.7.11.21;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading
CC to its degradation by the proteasome during interphase and regulating
CC centriole number and ensuring the block to centriole reduplication.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU01328,
CC ECO:0000255|PROSITE-ProRule:PRU01329}.
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DR EMBL; CM000363; EDX11390.1; -; Genomic_DNA.
DR RefSeq; XP_002085805.1; XM_002085769.2.
DR AlphaFoldDB; B4QK53; -.
DR SMR; B4QK53; -.
DR STRING; 7240.B4QK53; -.
DR EnsemblMetazoa; FBtr0212022; FBpp0210514; FBgn0183849.
DR GeneID; 6739010; -.
DR HOGENOM; CLU_008726_2_0_1; -.
DR OMA; LPSKHWK; -.
DR OrthoDB; 5471704at2759; -.
DR PhylomeDB; B4QK53; -.
DR ChiTaRS; SAK; fly.
DR Proteomes; UP000000304; Chromosome 3l.
DR Bgee; FBgn0183849; Expressed in embryo and 3 other cell types or tissues.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007099; P:centriole replication; IEA:EnsemblMetazoa.
DR GO; GO:0007140; P:male meiotic nuclear division; IEA:EnsemblMetazoa.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:0046599; P:regulation of centriole replication; IEA:EnsemblMetazoa.
DR GO; GO:0031647; P:regulation of protein stability; IEA:EnsemblMetazoa.
DR GO; GO:0007288; P:sperm axoneme assembly; IEA:EnsemblMetazoa.
DR GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IEA:EnsemblMetazoa.
DR CDD; cd13114; POLO_box_Plk4_1; 1.
DR CDD; cd13115; POLO_box_Plk4_2; 1.
DR CDD; cd13116; POLO_box_Plk4_3; 1.
DR Gene3D; 2.40.50.930; -; 1.
DR Gene3D; 3.30.1120.120; -; 1.
DR Gene3D; 3.30.1120.130; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR047108; Plk4-like_POLO_box_2_sf.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR033699; POLO_box_Plk4_1.
DR InterPro; IPR033698; POLO_box_Plk4_2.
DR InterPro; IPR033696; POLO_box_Plk4_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR046437; Ser_Thr-PK_POLO_box_1_sf.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF94; SERINE_THREONINE-PROTEIN KINASE PLK4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18190; Plk4_PB1; 1.
DR Pfam; PF18409; Plk4_PB2; 1.
DR SUPFAM; SSF82615; Polo-box domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51984; CPB1; 1.
DR PROSITE; PS51985; CPB2; 1.
DR PROSITE; PS50078; POLO_BOX; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT CHAIN 1..769
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385296"
FT DOMAIN 14..267
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 381..498
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 499..602
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 660..739
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 20..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 769 AA; 86012 MW; 0A6D501F8477C4BA CRC64;
MLSNRAFGET IEDYEVQHLL GKGGFATVYK ARCLHTHQDV AIKMIDKKLI QGTGLTSRVR
QEVEIHSRLK HPSVLQLYTF FQDANYVYLV LELAHNGELH RYMNHIARPF TETEAASILK
QVVAGLLYLH SHNIMHRDIS LSNLLLSREM HVKIADFGLA TQLKRPDERH MTMCGTPNYI
SPEVVSRSSH GLPADVWSVG CMLYTLLVGR PPFETDAVQS TLNKVVMSEY IMPAHLSYEA
QDLINKLLKK LPHERITLEA VLCHPFMLKC SNGVHSAPGA LNVFSQSMES GDSGIITFAS
SDSRNSQQIR SVENSGPQQV LPQIREEFKQ VHHKLPYEQP GLFGQASTGL AEPNWPGAAK
TSAFRMETGM VPNSKPASLK EDRISVPPLN TKRLLPTRYK TKNAIMSILR NGEVVLEFLK
FRPTYNEDRI NDICRISDDG QRIIIYQPDP GRGLPVREQP PDLQIPSGDC VYNYDNLPNK
HWKKYIYGAR FVGLVKSKTP KVTYFSTLGK CQLMETMTDF EIRFYSGAKL LKTPSEGLKV
YDRNGMLLSD HSCSESRSLI EHGNECFTHC VNISNALEVA QTKDNSCFPV TIGRRPITDV
QPAQRLDGLR DTTNIAFSTP KSNQGSINFS LSTISSTRNT SDFGTNCSRS NMLAAHQNIP
IKRINVPDIG IATELSHGVV QVQFYDGSVV SVIPSMQGGG ITYTQPNGTS THFGKDDDLP
FPVRDRVGQI PNIQLKLKTA PLLGSGRKTD YNNAMTPKTT TPYYNRMLL
//
