PLK4_DROGR
ID PLK4_DROGR Reviewed; 762 AA.
AC B4J3F1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=GH16744;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916366; EDV97250.1; -; Genomic_DNA.
DR RefSeq; XP_001984902.1; XM_001984866.1.
DR AlphaFoldDB; B4J3F1; -.
DR SMR; B4J3F1; -.
DR STRING; 7222.FBpp0150650; -.
DR EnsemblMetazoa; FBtr0152158; FBpp0150650; FBgn0124215.
DR GeneID; 6556999; -.
DR KEGG; dgr:6556999; -.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_008726_2_0_1; -.
DR InParanoid; B4J3F1; -.
DR OMA; GNECFTH; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; B4J3F1; -.
DR ChiTaRS; SAK; fly.
DR Proteomes; UP000001070; 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: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:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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..762
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385290"
FT DOMAIN 14..268
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 383..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 662..728
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
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 762 AA; 85316 MW; D431E35877F9CC4B CRC64;
MLPFRNYGET IDEYEVQHLL GKGGFACVYK AKCLRTQQNV AIKMIDKKLI QGSGLSSRVR
QEVEIHSRLK HPSVLQLHTF FQDGNYVYLV LELADNGELH RYMNQQMKRP FTEQEASSIL
RQVVDGLLYL HSHNIMHRDI SLSNLLLSRD MHVKIADFGL ATQLKRPDER HMTMCGTPNY
ISPEVVSHMS HGLPADLWSV GCMLYTLLVG RPPFDTDAVQ STLNKVVLSD YTMPSHLSYE
ARDLIEKLLR KNPHERISLE QVLRHPFMVK AGGGSIISYT TTPGASDGYG QSIASGDSGI
VTFASNDSKN SQRHMLPQIQ EEFGYYQEQR KNYAPHPVYR QSSAEPLNST EMEWQRIGQS
NGHFLAHSTP ATGGQVAAKK NNAECISMPP LNTLRLQPTR YKTKNAIMSI MANGEVVIEF
IKCKSKMNED RIVDICRISG DGRRIIIYQP DPGRGLPIRD QPSAVQPENY AYNYDNLPSK
HWKKYVYAAR FVSLVKSKTP KVTYFSGLAK CHLMENMADF EMCYYSGAKL TKSPTDAVKL
YNKHGLLITD QTSGEAMRWI EHSNECFAHC LSICNALELA QTGSNTCFPV TIGRRPTPEV
MPSQQRADGL RDTTNFAYST PKSQQGSINF SISTISSMRS GNDLIGSQLL AAQQNVPIKR
LNVPGVGTAT ELSHGIVQVQ FYDGSVISII PETQGGGITY TQSSGLSTHF PDHDDLPIAV
RDRLSQLPQV QMKLKSAPLI GSKKFDCKTT TESAPWHNRM LI
