PLK4_XENLA
ID PLK4_XENLA Reviewed; 944 AA.
AC Q6PAD2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Serine/threonine-protein kinase PLK4 {ECO:0000250|UniProtKB:O00444};
DE EC=2.7.11.21 {ECO:0000250|UniProtKB:O00444};
DE AltName: Full=Polo-like kinase 4;
DE Short=PLK-4;
DE AltName: Full=Serine/threonine-protein kinase Sak;
GN Name=plk4 {ECO:0000250|UniProtKB:O00444}; Synonyms=sak;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=24075808; DOI=10.1016/j.devcel.2013.08.021;
RA Klos Dehring D.A., Vladar E.K., Werner M.E., Mitchell J.W., Hwang P.,
RA Mitchell B.J.;
RT "Deuterosome-mediated centriole biogenesis.";
RL Dev. Cell 27:103-112(2013).
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 parental centriole cylinder, leading to the recruitment
CC of centriole biogenesis proteins such as sass6, cenpj/cpap, ccp110,
CC cep135 and gamma-tubulin. When overexpressed, it is able to induce
CC centrosome amplification through the simultaneous generation of
CC multiple procentrioles adjoining each parental centriole during S
CC phase. Its central role in centriole replication suggests a possible
CC role in tumorigenesis, centrosome aberrations being frequently observed
CC in tumors. Also involved in deuterosome-mediated centriole
CC amplification in multiciliated that can generate more than 100
CC centrioles (By similarity). {ECO:0000250|UniProtKB:O00444}.
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, ECO:0000250|UniProtKB:Q64702}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:O00444}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:O00444}. Note=Associates with centrioles
CC throughout the cell cycle (By similarity). Component of the
CC deuterosome, a structure that promotes de novo centriole amplification
CC in multiciliated cells that can generate more than 100 centrioles.
CC {ECO:0000250, ECO:0000269|PubMed:24075808}.
CC -!- PTM: Ubiquitinated; leading to its degradation by the proteasome.
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; BC060363; AAH60363.1; -; mRNA.
DR RefSeq; NP_001083146.1; NM_001089677.1.
DR AlphaFoldDB; Q6PAD2; -.
DR SMR; Q6PAD2; -.
DR DNASU; 398770; -.
DR GeneID; 398770; -.
DR KEGG; xla:398770; -.
DR CTD; 398770; -.
DR Xenbase; XB-GENE-866273; plk4.L.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 398770; Expressed in testis and 17 other tissues.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0098536; C:deuterosome; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0007099; P:centriole replication; ISS:UniProtKB.
DR GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0046601; P:positive regulation of centriole replication; ISS:UniProtKB.
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; 1.
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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Ubl conjugation.
FT CHAIN 1..944
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385283"
FT DOMAIN 12..265
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 565..678
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 679..791
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 868..932
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 327..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 944 AA; 105640 MW; 720B3A3616F2EF37 CRC64;
MAGSIGERRE DFKVLNLLGK GSFACVYRAQ SINTGIDVAI KMIDKKAMQK VGMVQRVRNE
VEIHCQLKHP SILELYNYFE DSNYVYLILE MCHNGEVNRY LKNRKKPFAE DEARHFMHQI
VTGMLYLHSH GILHRDLTLS NLLLSSDMNI KIADFGLATQ LKMPNEKHFT MCGTPNYIAP
EIATRSAHGL ESDVWSLGCM LYTFLVGRPP FDTDTVKNTL NKIVLADYEM PDFVSREAKD
LIFQLLRKNP ADRLSLSSVL DHAFMTGFSN VQSKVMGAVE DSMDSGHATI STGFTGSSGV
SISGRFQEKR ILSGPSLPNK VNIFQFKDKH PTERSNGGSF HNTQRENNDF SEGNGRKPVA
CEDRPHSRYL RRAHSSDRSG TSQSQTYAKP SSYSERCHSV EMLAKPTHLK GYRTSSPPNS
YGDIPQMFTD ERSLERHTSP PVKEKTPSEF MGPAKQTAPR SNDKAETVQQ WFGAMQLNGQ
FKNTPDTSSV SNMGGDFYSQ QATQNGAPQY AWNDVKRKKN TDSSIESVLL GIKKNPGTGQ
RKAEKSQFGE QSKSRVPQQA FGSSTLRSII SPLNAERLKP IRQKTKNAVV SILESGEVCM
EFLKEQNSQE RVKEVLRISC DGNLIYVYHP NEGKGFPLVD RPPSPPENRL SYTFDSLPEK
YWKKYQYAAK FIKLVRSKTP KVTYYTRYAK CMLMENSPTA DVEVCFYDGA KIHKTSDVIR
VIEKSGRSYT LEGSRLSTLS DEVRSYLDHA NESHCVCLSL ESAINTEEKK GENISLFPIT
FGRRPALAES PKTQPTPSVD SARERKEEQS YVNRVLHGSA ASPPQMPNLN PSLISYDGSV
FSATTVQPSP TSNIHNTPDH AQVLKSVFVE NVGWASQLNS GAVWVQFNDG SQLVVQPGVS
SIIYTAPNGQ ITRHGENDKL PEYIKSKLQC LSSILMLFAS SSSR
