PLK4_DROWI
ID PLK4_DROWI Reviewed; 787 AA.
AC B4MXR8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=GK17621;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
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; CH963876; EDW76837.1; -; Genomic_DNA.
DR RefSeq; XP_002065851.1; XM_002065815.2.
DR AlphaFoldDB; B4MXR8; -.
DR SMR; B4MXR8; -.
DR STRING; 7260.FBpp0246764; -.
DR EnsemblMetazoa; FBtr0248272; FBpp0246764; FBgn0219620.
DR GeneID; 6642935; -.
DR KEGG; dwi:6642935; -.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_008726_2_0_1; -.
DR InParanoid; B4MXR8; -.
DR OMA; GNECFTH; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; B4MXR8; -.
DR ChiTaRS; SAK; fly.
DR Proteomes; UP000007798; 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 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; 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..787
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385298"
FT DOMAIN 14..268
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 386..505
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 506..613
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 680..747
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 311..336
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 787 AA; 88378 MW; 7B4700EB45E26A26 CRC64;
MLPVRNYGET IEEYEVQHLL GKGGFASVYK ARCRRTYQDV AIKMIDKKLI HGTGLSSRVR
QEVEIHSRLK HPSVLQLYTF FQDANYVYLV LELAHNGELH RYMNQQMSHP FTEADAATIL
QQVVAGLLYL HSHNIMHRDI SLSNLLLSKD MHVKIADFGL ATQLKRPDEK HMTMCGTPNF
ISPEVVSRLS HGLAADVWSV GCLLYTLVVG RPPFDTDAVQ STLNKVVMSE FIMPTHLSFE
ACDLIEKLLK KNPHERISLE QVLRHPFMSK RSAGAEEPQY NSSKPGACDF YMEAQGQSVA
SGDSGIVTFA SNESRSSQRL RSIEKSAQSS SNPQMLPQIQ EEYGYWQPST EHKPYPMPLS
SDNAEWERLG SKGNQPHTAA SVITEEQQMR VPPLNTIRLQ PTRYKTKNAI MSILRHGEVV
LEFVKFRSKL NEDRVTDICR ISGDGRRIII YQPDPGRGLP IREQPPPPES HIAGDKSVYN
YDSLPSKHWK KYLYAARFVG LVKSKTPKIT YFSSLAKCHL MENMIDFEMS YYSGAKYVKT
SPGEELKLYN NYGMLLSDLA CPEAKKMIEH GNECFSHCIN ICNALELAQQ SADSRNTCFP
VTIGRRPLTD VSHSQRFDGL RDTTNIAYST PKSHQGSINF SMSTISSVQN GSESVSSTHS
HASRAQIQAS QQNVPIKRIN IPDVGIATEL SHGIVQVQFY DGSMISLIPE IQGGGLTYTQ
CNGVSTYFPK YDGDLPLAVR DRLAQIPQVK LRLKCAPLLS NHRKADNIAM TPKSTTPSTP
CYNRIVL
