PLK4_DROPE
ID PLK4_DROPE Reviewed; 777 AA.
AC B4HBU3;
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=GL11903;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
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; CH479267; EDW39537.1; -; Genomic_DNA.
DR RefSeq; XP_002028322.1; XM_002028286.1.
DR AlphaFoldDB; B4HBU3; -.
DR SMR; B4HBU3; -.
DR STRING; 7234.FBpp0176010; -.
DR EnsemblMetazoa; FBtr0177518; FBpp0176010; FBgn0149511.
DR GeneID; 6603338; -.
DR KEGG; dpe:6603338; -.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_008726_2_0_1; -.
DR OMA; GNECFTH; -.
DR PhylomeDB; B4HBU3; -.
DR ChiTaRS; SAK; fly.
DR Proteomes; UP000008744; 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; 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..777
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385293"
FT DOMAIN 14..268
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 390..507
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 508..611
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 674..740
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 371..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
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 777 AA; 87311 MW; 4DF94DC3943CDE69 CRC64;
MMSTRTFGET IEEYEVQHLL GKGGFASVYK ARCLHSHQDV AIKMIDKKLI QGTGLTSRVR
QEVEIHSRLK HPSVLQLYTF FQDVNYVYLV LELAHNGELQ RYMKQHLLRP FTESEGATIL
RQVVAGLLYL HSHNIMHRDI SLSNLLLSKE MHIKIADFGL ATQLKRPDER HMTMCGTPNY
ISPEVVSRLS HGLPADVWSV GCMLYTLLVG RPPFETEGVE STLNKVVMSE FMMPSHLSFE
AQDLIHKLLK KSPHERITLE QVLRHPFLKR TVGGSSYSTT PGALNEFSQS LASSDSGIVT
FASSDSRKSH RLRSVDNSSG QSMPQIMEEY LPSSNLGYDS KEHRPIYEQH GSYLPTPGDQ
LENRDAKWPG TNNLAPFTSD SDMIPSPVGE KRLLMPPLET KRLQPTRYKT KNAIMSILRT
GEVVLEFVKF KVKYNEDRIT DICRISEDGR RIIIYQPDPG RGLPIREHPP DPLIPSENCV
YNYENLPNKH WKKYVYAARF VGLVKSKTPK ITFFSSLGKC QLMETMTDFE VRFYSGAKLL
KSSTDGVKVF NSNGAVLSDN GCAEARNLID HGNECFSHCV NISNALELAQ TKENTCFPVT
IGRRPAADMH AGQRFDGLRD TTNFAYSTPK SNQGSINFSV STISTTRSAS DYNSNTPRLN
MLAAHQNVPI KRITVPEIGI VTELSHGVVQ VQFYDGSMVS VIPKVQGGGI TYTQANGLST
HFGNNDDLPF AVRDRINQMP QLQMKLKCAP LLGNARSVDC HLMTPKTTTP FYNRMII
