PLK4_XENTR
ID PLK4_XENTR Reviewed; 946 AA.
AC B3DL84;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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. Component of the deuterosome, a structure
CC that promotes de novo centriole amplification in multiciliated cells
CC that can generate more than 100 centrioles (By similarity).
CC {ECO:0000250}.
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; BC167348; AAI67348.1; -; mRNA.
DR RefSeq; NP_001122128.1; NM_001128656.1.
DR AlphaFoldDB; B3DL84; -.
DR SMR; B3DL84; -.
DR STRING; 8364.ENSXETP00000012645; -.
DR PRIDE; B3DL84; -.
DR GeneID; 100038180; -.
DR KEGG; xtr:100038180; -.
DR CTD; 10733; -.
DR Xenbase; XB-GENE-493608; plk4.
DR eggNOG; KOG0575; Eukaryota.
DR InParanoid; B3DL84; -.
DR OrthoDB; 507604at2759; -.
DR Reactome; R-XTR-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-XTR-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-XTR-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-XTR-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-XTR-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-XTR-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-XTR-8854518; AURKA Activation by TPX2.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098536; C:deuterosome; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
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:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0046601; P:positive regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
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..946
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385284"
FT DOMAIN 12..265
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 566..679
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 680..792
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 870..934
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 330..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..828
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 797..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..828
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 946 AA; 105883 MW; 4F688FA9ECACA665 CRC64;
MAGSIGERRE DFKVLNLLGK GSFACVYRAQ SINTGIDVAI KMIDKKAMQK VGMVQRVRNE
VEIHCQLKHP SILELYNYFE DSNYVYLILE MCHNGEMNRF LKNRKKPFSE DEARHFMHQI
VTGMLYLHSH GILHRDLTLS NLLLSSDMNI KIADFGLATQ LKMPNEKHFT MCGTPNYIAP
EIATRSAHGL ESDVWSLGCM LYTFLVGRPP FDTDTVKNTL NKIVLADYEM PDFVSREAKD
LIFQLLRKNP ADRLSLSSVL DHAFMTGFSN VQSKVMGAVE DSIDSGHATI STGFTGSSGV
SISGRFQEKR ILSGPSLPNK VNIFQFKDKH PAERSNGGSF HNTQRENNDF SEGNGRKTVA
CEDRPHSRYL RRAHSSDRSG TSQSQTYGKP SSFSERCHSV EMLAKPSNLK GYCTSSPPKS
YGDIPQMFTD ERSLERHTSP PVKEKTPSEF MCPAKQITPR SGDKCQAETV QQWFGAMQLN
GKFKNTPDTS SVSNMGGDFY SQQTMQNGAP QYAWNDVKRK KDTDSSVESV LRGISKLPSG
QHKAEKSQFG EQSKARVPQQ AFGSSTLRSI ISPLNAERLK PIRQKTKNAV VSILETGEVC
MEFLKEQNSQ ERVKEVLRIS CDGNLIYVYH PNEGKGFPLV ERPPSPPENM RSYTFDSLPE
KYWKKYQYAA KFIQLVRSKM PKVTYYTRYA KCMLMENGPN ADFEVCFYDG AKIHKTPDLI
RVIEKSGKSY TVEGSRLSTL SDQVRSYVNH ANESHCVCLS LESAINTEEK KGENISLFPI
TFGRRPAITE SPRTQLTVDS ARERKDEQSS ANRVLHSSAT SPPQIPNINP SLISYEGSVF
SATTAQPSPP TSNTLKTHAP DRAQVLKSVF VENVGWASQL NSGAVWVQFN DGSQLVVQPG
VSSIIYTAPN GQITRHGEND KLPEYIKSKL QCLSSILMLF ASSSSH
