PLK4_DROER
ID PLK4_DROER Reviewed; 766 AA.
AC B3NE99;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-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=GG13228;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
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; CH954178; EDV52663.1; -; Genomic_DNA.
DR RefSeq; XP_001973637.1; XM_001973601.2.
DR AlphaFoldDB; B3NE99; -.
DR SMR; B3NE99; -.
DR STRING; 7220.FBpp0131774; -.
DR EnsemblMetazoa; FBtr0133282; FBpp0131774; FBgn0105500.
DR GeneID; 6543822; -.
DR KEGG; der:6543822; -.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_008726_2_0_1; -.
DR OMA; GNECFTH; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; B3NE99; -.
DR ChiTaRS; SAK; fly.
DR Proteomes; UP000008711; 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 Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..766
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385289"
FT DOMAIN 14..267
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 379..496
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 497..600
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 663..732
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 766 AA; 85961 MW; 0E24EECA7873AB0B CRC64;
MLSNRAFGET IEDYEVQHLL GKGGFAIVYK ARCLHTHQDV AIKMIDKKLI QGTGLTNRVR
QEVEIHSRLK HPSVLQLYTF FQDANYVYLV LELAHNGELH RYMNHIARPF TETEAASILK
QVVAGLLYLH SHNIMHRDIS LSNLLLSKEM HVKIADFGLA TQLKRPDERH MTMCGTPNYI
SPEVVSRSSH GLPADVWSVG CMLYTLLVGR PPFETDAVQS TLNKVVMSEY IMPAHLSYEA
QDLINKLLKK LPHERITLEA VLCHPFMLKC SNGGHSTPGA LNMFSQSMES GDSGIITFAS
SDSRNSQQIR SVENSGPQQV LPQIQEEFKH HKLTYEQPGL FRQTSTGLAE PNWPGATKAS
SFRMEMGMVQ NSKPAPVKED RISVPPLNTK RLLPTRYKTK NAIMSILRNG EVVLEFFRFR
PTYNEDRITD ICRISDDGQR IIIYQPDPGR GLPVREQPPD LQIPSGDCVY NYENLPSKHW
KKYIYGARFV GLVKSKTPKV TYFSTLGKCQ LMETMTDFEI RFYSGAKLLK TPSEGLKVYD
RNGMFLSDHS CSESRSLIEH GNECFTHCVN ISNALEVAQT KENSCFPVTI GRRPLTDVQP
AQRLDGLRDT TNIAFSTPKS NQGSINFSVS TISSTRNTTG FETNCSRSNM LAAHQNIPIK
RISVPDVGIA TELSHGVVQV QFYDGSVVSV IPSMQGGGIT YTQPNGTSTH FGKDDDLPFP
VRDRVGQIPN IQLKLKTAPL LESGRKIDYN AMTPKTTTPC YNRMLL
