PLK4_CULQU
ID PLK4_CULQU Reviewed; 761 AA.
AC B0WAU8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-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=CPIJ004252;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB;
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) 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 mother centriole cylinder, leading to the recruitment of
CC centriole biogenesis proteins. When overexpressed, it is able to induce
CC centrosome amplification through the simultaneous generation of
CC multiple procentrioles adjoining each parental centriole during S phase
CC (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; 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; DS231875; EDS41814.1; -; Genomic_DNA.
DR RefSeq; XP_001845832.1; XM_001845780.1.
DR AlphaFoldDB; B0WAU8; -.
DR SMR; B0WAU8; -.
DR STRING; 7176.CPIJ004252-PA; -.
DR GeneID; 6035698; -.
DR KEGG; cqu:CpipJ_CPIJ004252; -.
DR VEuPathDB; VectorBase:CPIJ004252; -.
DR VEuPathDB; VectorBase:CQUJHB015681; -.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_008726_2_0_1; -.
DR InParanoid; B0WAU8; -.
DR OMA; GNECFTH; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; B0WAU8; -.
DR Proteomes; UP000002320; Partially assembled 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; cd13116; POLO_box_Plk4_3; 1.
DR Gene3D; 3.30.1120.30; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033700; Plk4.
DR InterPro; IPR036947; POLO_box_dom_sf.
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; 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..761
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385287"
FT DOMAIN 12..265
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 376..493
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 494..598
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 653..722
FT /note="POLO box"
FT REGION 595..616
FT /note="Disordered"
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 761 AA; 84648 MW; 7296EEF91ED6AB10 CRC64;
MLNNFGECIE DFEVFELLGK GGFASVYRAK CCRTGILVAI KMIDKKLMQS SGMANRVRQE
VSIHSRLKHP SILELYTFFE DANFVYLVLE LAENGELQRY LRDTKKTFNE YEAATVLKQV
VEGLLYLHSH QILHRDMSLA NLLLTKEMTV KICDFGLATQ LSRPDEKHMT LCGTPNYISP
EVASRASHGL PADVWGLGCM LYTFLVGRPP FDTDGVKSTL TKVVMSNYTL PSHISQEARD
LIDRLLKKNP AERIKLDQVP LHPFMQKASS FEKCQGGTLA SSDSGIMTIS SGNRSNIPSN
YSQERYQPPV QMPLRYQPIS EDFQESILPT RPQSAAYGRP QTSDFYSGFS GDQQQRPSTA
QPPFVHHMNQ ISLLQHKRID IPPLTTARLQ PNRHKTKNAI LSIQPNGEVV LEFIKYKSRA
KADRVVDVCR ISSDGLRFVL YHPDGGKGVA VKDEPPDLPP GGADAIFSYE NLPEKHWKKY
AYAARFVQMV KAKTPKITYY SERAKCQLME TLEDYEANFY SGTKVIKSLH EGTKIVDSTG
RTFKDTTATL NTALTMEFEH FQQTFDHCLN IEQALSAIHT GNTFPLIIGR RPATATSNHE
NSVSTPQTPH HNPHQLSSFA MSVNSAATTN SRRLPCPKAA PSFSSNVATK KCTIPGVGTA
VQLSQGVVQV QFVDGATLSL IPIEQGGGVT FSPCFGTPLQ HYSAQQQQDD PASLPGTLRD
KLGQMSLVLR ELNAAPVPSI PFNFLEGTAL SPRTPLTRFL R
