PLK4_RAT
ID PLK4_RAT Reviewed; 924 AA.
AC B2GUY1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Serine/threonine-protein kinase PLK4 {ECO:0000305};
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:0000312|RGD:1305390}; Synonyms=Sak;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition,
CC leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central
CC role in centriole replication suggests a possible role in
CC tumorigenesis, centrosome aberrations being frequently observed in
CC tumors. Also involved in deuterosome-mediated centriole amplification
CC in multiciliated that can generate more than 100 centrioles. Also
CC involved in trophoblast differentiation by phosphorylating HAND1,
CC leading to disrupt the interaction between HAND1 and MDFIC and activate
CC HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of
CC STIL to the centriole and for STIL-mediated centriole amplification (By
CC similarity). Phosphorylates CEP131 and PCM1 which is essential for
CC proper organization and integrity of centriolar satellites (By
CC similarity). {ECO:0000250|UniProtKB:O00444,
CC ECO:0000250|UniProtKB:Q64702}.
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 (By similarity). Interacts with CEP152 (via N-
CC terminus) (By similarity). Interacts with CEP78; this interaction may
CC be important for proper PLK4 localization to the centriole and PLK4-
CC induced overduplication of centrioles (By similarity). Interacts with
CC CEP131 (By similarity). Interacts simultaneously with TENT5C and
CC CEP192. Interacts with TENT5C; this interaction leads to the TENT5C
CC recruitment in the centrosome (By similarity).
CC {ECO:0000250|UniProtKB:O00444, ECO:0000250|UniProtKB:Q64702}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000250|UniProtKB:O00444}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q64702}. Cleavage furrow
CC {ECO:0000250|UniProtKB:Q64702}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:O00444}.
CC Note=Associates with centrioles throughout the cell cycle. Component of
CC the deuterosome, a structure that promotes de novo centriole
CC amplification in multiciliated cells that can generate more than 100
CC centrioles (By similarity). {ECO:0000250|UniProtKB:O00444,
CC ECO:0000250|UniProtKB:Q64702}.
CC -!- DOMAIN: Cryptic POLO box 1 (CPB1) and Cryptic POLO box 2 (CPB2) domains
CC can simultaneously bind to both TENT5C and CEP192.
CC {ECO:0000250|UniProtKB:O00444}.
CC -!- PTM: Ubiquitinated; leading to its degradation by the proteasome.
CC {ECO:0000250}.
CC -!- PTM: Acetylation by KAT2A and KAT2B impairs kinase activity by shifting
CC the kinase to an inactive conformation. {ECO:0000250|UniProtKB:O00444}.
CC -!- PTM: Tyrosine-phosphorylated by TEC. {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; BC166450; AAI66450.1; -; mRNA.
DR RefSeq; XP_006232361.1; XM_006232299.3.
DR AlphaFoldDB; B2GUY1; -.
DR SMR; B2GUY1; -.
DR STRING; 10116.ENSRNOP00000016946; -.
DR PaxDb; B2GUY1; -.
DR PRIDE; B2GUY1; -.
DR GeneID; 310344; -.
DR CTD; 10733; -.
DR RGD; 1305390; Plk4.
DR VEuPathDB; HostDB:ENSRNOG00000011654; -.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_008726_1_0_1; -.
DR InParanoid; B2GUY1; -.
DR OMA; HSSWSEP; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; B2GUY1; -.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR PRO; PR:B2GUY1; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011654; Expressed in testis and 18 other tissues.
DR ExpressionAtlas; B2GUY1; baseline and differential.
DR Genevisible; B2GUY1; RN.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0120098; C:procentriole; ISO:RGD.
DR GO; GO:0120099; C:procentriole replication complex; ISO:RGD.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0001741; C:XY body; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:0060271; P:cilium assembly; 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; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; ISS:UniProtKB.
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 Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..924
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385281"
FT DOMAIN 12..265
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 546..659
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 660..773
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 846..910
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 329..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..831
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"
FT MOD_RES 45
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00444"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00444"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00444"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00444"
SQ SEQUENCE 924 AA; 103770 MW; F79ACD48E54412F1 CRC64;
MAACIGERIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK AGMVQRVQNE
VKIHCQLKHP SVLELYNYFE DNNYVYLVLE MCHNGEMNRY LKNRMKPFSE SEARHFMHQI
ITGMLYLHSH GILHRDLTLS NILLTRNMNI KIADFGLATQ LKMPHEKHYT LCGTPNYISP
EIATRSAHGL ESDIWSLGCM FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PAFLSREAQD
LIHQLLRRNP ADRLSLSSVL DHPFMSRNPS TKSKDLGTVE DSMDSGHATL STTITASSGT
SLSGSLLDRR RLLVGQPLPN KITVFQKNKN SSDFSSGDGS NFCTQWGNPE QEANNRGRGR
VIEDAEERPH SRYLRRAHSS DRSNPSNQSR AKTYSIERCH SVEMLSKPRR SSLDETKHSS
NHHCLGKTPF PFADQTPQME IVQQWFGNLQ MNGETSEHNT ISPNRDFQDY PDVQDTLRNT
WTDTRASKNS DNSANVHPAK QLSTMKYMTA HHHKPEIMQQ ELAIHPHSEQ NKSRSMESTL
GYRKPTLRSI TSPLVAHRLK PIRQKTKKAV VSILDSEEVC VELLKECTSE GHVKEVLQIS
SDGTTITVYY PNDGRGFPLA DRPPLPTDNI SRYSFDSLPE KYWRKYQYAS RFIQLVRSKT
PKITYFTRYA KCILMENSPG ADFEVWFYDG AKIHKTEDVI HIIEKTGLSY TLKNENDFTS
LKEEVKIYMD HANEGHRTCL ALESVISEEE KRSRGSSFFP IIVGRKPGTT SSPKALSPPP
VDPGYSKGEQ ASSSRLSANS AAFPTQTPVL SPSAVTVEGP GQTAATTGTS ISSSLPKSAQ
LLKSVFVKNV GWATQLTSGA VWVQFNDGSQ LVVQAGVSSI SYTSPDGQTT RYGENEKLPE
YIKQKLQCLS SILLMFSNPT PSFQ
