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PLK4_DROSE
ID   PLK4_DROSE              Reviewed;         769 AA.
AC   B4IAQ8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=GM22133;
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25;
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; CH480826; EDW44371.1; -; Genomic_DNA.
DR   RefSeq; XP_002040818.1; XM_002040782.1.
DR   AlphaFoldDB; B4IAQ8; -.
DR   SMR; B4IAQ8; -.
DR   STRING; 7238.B4IAQ8; -.
DR   EnsemblMetazoa; FBtr0205118; FBpp0203610; FBgn0177004.
DR   GeneID; 6616457; -.
DR   KEGG; dse:6616457; -.
DR   HOGENOM; CLU_008726_2_0_1; -.
DR   OMA; GNECFTH; -.
DR   PhylomeDB; B4IAQ8; -.
DR   ChiTaRS; SAK; fly.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
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   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033700; Plk4.
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; IPR008266; Tyr_kinase_AS.
DR   PANTHER; PTHR24345:SF89; PTHR24345:SF89; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF18190; Plk4_PB1; 1.
DR   Pfam; PF18409; Plk4_PB2; 1.
DR   SUPFAM; SSF56112; SSF56112; 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_0000385295"
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          665..734
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;  86000 MW;  540A647AAAB62E0D CRC64;
     MLSNRAFGET IEDYEVQHLL GKGGFATVYK ARCLHTHQDV AIKMIDKKLI QGTGLTSRVR
     QEVEIHSRLK HPSVLQLYTF FQDANYVYLV LELAHNGELH RYMNHIARHF TETEAASILK
     QVVAGLLYLH SHNIMHRDIS LSNLLLSREM HVKIADFGLA TQLKRPDERH MTMCGTPNYI
     SPEVVSRSSH GLPADVWSVG CMLYTLLVGR PPFETDAVQS TLNKVVMSEY IMPAHLSYEA
     QDLINKLLKK LPHERITLEA VLCHPFMLKC SNGGHSAPGA LNMFSQSMES GDSGIITFAS
     SDSRNSQQIR SVENSGPQQV LPQIREEFKQ VHHKLPYEQP GLFGQASTGL AEPNWTGAAK
     TSAFRMETGM VPNSKPASLK EDRISVPPLN TKRLLPTRYK TKNAIMSILR NGEVVLEFLK
     FRPTYNEDRI NDICRISDDG QRIIIYQPDP GRGLPVREQP PDLQIPSGDC VYNYDNLPNK
     HWKKYIYGAR FVGLVKSKTP KVTYFSTLGK CQLMETMTDS EIRFYSGAKL LKAPTEGLKV
     YDRNGMLLSD HSCSESRSLI EHGNECFTHC VNISNALEVA QTKDNSCFPV TIGRRPITDV
     QPAQRLDGLR DTTNITFSTP KSNQGSINFS LSTISSTRNT SDFGTNCSRS NMLAAHQNIP
     IKRINVPDIG IATELSHGVV QVQFYDGSVV SVIPSMQGGG ITYTQPNGTS THFGKDDDLP
     FPVRDRVGQI PNIQLKLKTA PLLGSGRKTD YNNAMTPKTT TPYYNRMLL
 
 
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