ID PLK4_NEMVE Reviewed; 978 AA.
AC A7SNN5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
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;
GN ORFNames=v1g246408;
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6;
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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; DS469722; EDO34707.1; -; Genomic_DNA.
DR RefSeq; XP_001626807.1; XM_001626757.1.
DR AlphaFoldDB; A7SNN5; -.
DR SMR; A7SNN5; -.
DR STRING; 45351.A7SNN5; -.
DR EnsemblMetazoa; EDO34707; EDO34707; NEMVEDRAFT_v1g246408.
DR GeneID; 5506045; -.
DR KEGG; nve:5506045; -.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_008726_1_0_1; -.
DR InParanoid; A7SNN5; -.
DR OMA; NIVERCH; -.
DR OrthoDB; 5471704at2759; -.
DR PhylomeDB; A7SNN5; -.
DR Proteomes; UP000001593; Unassembled 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Gene3D; 2.40.50.930; -; 1.
DR Gene3D; 3.30.1120.120; -; 1.
DR Gene3D; 3.30.1120.130; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR047108; Plk4-like_POLO_box_2_sf.
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; IPR046437; Ser_Thr-PK_POLO_box_1_sf.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF94; SERINE_THREONINE-PROTEIN KINASE PLK4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18190; Plk4_PB1; 1.
DR Pfam; PF18409; Plk4_PB2; 1.
DR SUPFAM; SSF82615; Polo-box domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 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..978
FT /note="Serine/threonine-protein kinase PLK4"
FT /id="PRO_0000385285"
FT DOMAIN 13..266
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 565..678
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT DOMAIN 679..792
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT DOMAIN 895..973
FT /note="POLO box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 271..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 978 AA; 108146 MW; EDA2EF4144997608 CRC64;
MTTQYMGDSI EDFQVLDLLG KGGFACVYRG RCLATGQEVA IKMIDKKAMR TAGMVNRVCN
EVEIHCRLKH PSILELYTYF EDDNYVYLVL ELAENGEANR YLRKQGHTLK ESEVRRIMLQ
VVKGVLYLHS HGIIHRDLSL GNILLSSDMD AKIADFGLAT RLSLPDEKHY TMCGTPNYIS
PEIATRDPHG LESDVWSIGC MLFTLLVGKP PFDTEAVRST LNKVVLAEYD IPNHVSIEAR
DLISKLLKKN PQDRLTLSGI LDHPFITNQT LNTKYSSPTR QHLNPRAYEN SLDSGTGTMA
TISTGHAPFQ QDNRHAVKSS SAERTSDIWP RDPKHPPSPP VRQRPSSCPS TENVTTGSSS
HVRGSDVAQP AQYSGLKTRT SDSWLSDIHS SKIPKLPQKP LVGLDKMNGI QSKFKSYNAT
KYSSYYGSTL GDILHLAGQQ NGTNTSSSGF YSADTKSYSA NHGLKTSSTD HNNKESCQTR
DNHMYEKSIE QPSATKSEHS RAYSSQDSRP HSHHKRHGSD SVSKDFDASP QPSQGESRRR
QNHRSDSERQ TRRAEKSRSG GRDKSLGELT EPLNAERLRP IRQKTRNAVV SITDEAEVCL
EFLQQKGGQS IVTEVIRIAS NGMKISVYQP SEAEKVLGSE PPLPPSAGNG SYLFPSLPSK
YWKKYKYAAK FVQLVRKLTP KVTLYSKHAK CVLMENYPHA DFEVCFYNGA KVHQSQECTR
IIEPGGVSYT LESVGGIEGV PVEMRKLIQH VKAAYQQCVR LERIIMQEEK ESNGNQYFPF
IVGRRPPAWK NSSGKSEKQD QQGCSNGQSQ PVLPSSPSIA APAMTSLLSF DGTIASTAQT
TNPAFPGKSR KTSPSKTSRH KQSPAQPIPA EVANAKTDPS PHHYVEGSSP IPSAHVCKMA
FVDGVGWSSQ LTTGEVWIQY TDGSQIIFHA AAAAIKFTDS TGNVTRYGYA DRLPSVIKEK
LSHLPAVIKT LATTSKVS
//
