PLK4_BOVIN
ID PLK4_BOVIN Reviewed; 893 AA.
AC A2VDZ4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-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 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: Tyrosine-phosphorylated by TEC. {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 -!- 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; BC133488; AAI33489.1; -; mRNA.
DR RefSeq; NP_001076896.1; NM_001083427.2.
DR AlphaFoldDB; A2VDZ4; -.
DR SMR; A2VDZ4; -.
DR STRING; 9913.ENSBTAP00000048808; -.
DR PaxDb; A2VDZ4; -.
DR PRIDE; A2VDZ4; -.
DR Ensembl; ENSBTAT00000055868; ENSBTAP00000048808; ENSBTAG00000039552.
DR GeneID; 514405; -.
DR KEGG; bta:514405; -.
DR CTD; 10733; -.
DR VEuPathDB; HostDB:ENSBTAG00000039552; -.
DR VGNC; VGNC:33036; PLK4.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000156316; -.
DR HOGENOM; CLU_008726_1_0_1; -.
DR InParanoid; A2VDZ4; -.
DR OMA; HSSWSEP; -.
DR OrthoDB; 507604at2759; -.
DR TreeFam; TF101090; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000039552; Expressed in spermatid and 107 other tissues.
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; IEA:Ensembl.
DR GO; GO:0120099; C:procentriole replication complex; IEA:Ensembl.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0001741; C:XY body; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; 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 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..893
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385279"
FT DOMAIN 12..265
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 509..622
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 623..736
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 815..879
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 349..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..389
FT /note="Basic and acidic 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 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00444"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00444"
SQ SEQUENCE 893 AA; 100707 MW; 212E95B9FEA8E92B CRC64;
MATCIGEKIE DFRVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK AGMVQRVQNE
VKIHCQLKHP SILELYNYFE DNNYVYLVLE MCHNGEMNRY LKNRRKPFSE NEARHFMHQI
ITGMLYLHSH GILHRDLTLS NLLLTRNMNI KIADFGLAAQ LKMPHEKHYT LCGTPNYISP
EIATRSAHGL ESDIWSLGCM FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PTFLSREAKD
LIHQLLRRNP ADRLSLSSVL DHPFMSRNSS KKSKDLGTVE DSIDSGHATI STAITASSST
SISGSLFDRR RLLIEQPLPN KMTIFPKNKN PSDFSSSGDG ISFYTSWGNQ EQETSNSGRG
RVIQEAEERP HSRYLRRAHS SDRSETSHGQ SRVKTYTMER CYSAEMLSKS KRSGVEENER
YSPTNNDANI FHFFKEKTSN SSGSFEGPDN NQALSNHLCP GKTPFPFPEQ TPQTEMVQQW
FGNLQINDPS CEQSKTRGVE PPLVYQKRTL RSITSPLTAY RLKPIRQKTK KAVVSILDSE
EVCVELLKDY ASQEYVKEVL QISSDGSMIT IYYPNDGRGF LLADRPPSPT DNISRYSFDN
LPEKYWRKYQ YASRFVQLVR SKSPKITYFT RYAKCVLMEN SPGADFEVWF YDGAKIHKTE
DLIQVIEKTG RSYTLKGESE VNSLKEEVKM YMNHANEGHR ICLALESIIS EEEKKSGSAP
FFPIIVGRRP SSTSSPKALT PPPPVDPNYP MRETPSLNRM IINSAASPKQ APVLNPPVVT
NEGLGLMGAA SETNSSPRSL KDCLPKSAQL LKSVFVKNVG WATQLTSGAV WVQFNDGSQL
VVQAGVSSIS YTSPDGQTTR YGENEKLPEY IKQKLQCLSS ILLMFSNPTP SFH
