PLK4_PONAB
ID PLK4_PONAB Reviewed; 970 AA.
AC Q5R9Z7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR859233; CAH91413.1; -; mRNA.
DR RefSeq; NP_001153257.1; NM_001159785.1.
DR AlphaFoldDB; Q5R9Z7; -.
DR BMRB; Q5R9Z7; -.
DR SMR; Q5R9Z7; -.
DR STRING; 9601.ENSPPYP00000016820; -.
DR GeneID; 100294540; -.
DR KEGG; pon:100294540; -.
DR CTD; 10733; -.
DR eggNOG; KOG0575; Eukaryota.
DR InParanoid; Q5R9Z7; -.
DR OrthoDB; 507604at2759; -.
DR Proteomes; UP000001595; Unplaced.
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; IEA:UniProtKB-KW.
DR GO; GO:0098536; C:deuterosome; ISS: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: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:0046601; P:positive regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
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..970
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385280"
FT DOMAIN 12..265
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 586..699
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 700..813
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 892..956
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 324..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..829
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 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00444"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00444"
SQ SEQUENCE 970 AA; 109042 MW; 2139C0B36593CFF4 CRC64;
MATCIGEKIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK AGMVQRVQNE
VKIHCQLKHP SILELYNYFE DSNYVYLVLE MCHNGEMNRY LKNRVKPFSE NEARHFMHQI
ITGMLYLHSH GILHRDLTLS NLLLTRNMNI KIADFGLATQ LKMPHEKHYT LCGTPNYISP
EIATRSAHGL ESDVWSLGCM FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PTFLSMEAKD
LIHQLLRRNP ADRLSLSSVL DHPFMSQNSS TKSKDLGTVE DSIDSGHATL STAITASSST
SISGSLFDKR RLLIGQPLPN KMTVFPKNKS SSDFSSSGDG NSFYTQWGNQ ETSNSGRGRV
IQDAEERPHS RYLRRAYSSD RSGTFNSPSQ AKTYTMERCH SAEMLSMSKR SGGGENEERY
SPTDNNANIF NFFKEKTSSS SGSFERPDNN QTLSNHLCPG KTPFPFADPT PQTETVQQWF
GNLQINAHLR KTTEYDSISP TRDFQGHPDL QKDTSKNAWT DTKVKKNSDA SDNAHSVKQP
NTMKYMTALH SKPEIVQQEC VFGSDPLSEQ SKTRGMEPPL GYQNRTLRSI TSPLVAHRLK
PIRQKTKKAV VSILDSEEVC VELLKEYASQ EYVKEVLQIS SDGNMITIYY PNGGRGFPLA
DRPPSPTDNI SRYSFDNLPE KYWRKYQYAS RFVQLVRSKS PKITYFTRYA KCILMENSPG
ADFEVWFYDG VKIHKTEDFI QVIEKTGKSY TLKSESEVNS LKEEIKMYMD HANEGHRICL
ALESIISEEE RKTRSAPFFP IIIGRKPGST SSPKALSPPP SVDSNYPTRD RASFNRMVMH
SAASPTQAPI LNPSMVTNEG LGLTTTASGT YISSNSLKDC LPKSVQLLKS VFVKNVGWAT
QLTSGAVWVQ FNDGSQLVVQ AGVSSISYTS PNGQTTRYGE NEKLPEYIKQ KLQCLSSILL
MFSNPTPNFH
