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PLK4_DROAN
ID   PLK4_DROAN              Reviewed;         770 AA.
AC   B3M6I4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=GF10707;
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(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, using mother centriole as a
CC       platform, leading to the recruitment of centriole biogenesis proteins
CC       such as sas-6. When overexpressed, it is able to induce centrosome
CC       amplification through the simultaneous generation of multiple
CC       procentrioles adjoining each parental centriole during S phase.
CC       Centrosome amplification following overexpression can initiate
CC       tumorigenesis, highlighting the importance of centrosome regulation in
CC       cancers (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 by the SCF(Slimb) ubiquitin ligase complex; leading
CC       to its degradation by the proteasome during interphase and regulating
CC       centriole number and ensuring the block to centriole reduplication.
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; CH902618; EDV40833.1; -; Genomic_DNA.
DR   RefSeq; XP_001958027.1; XM_001957991.2.
DR   AlphaFoldDB; B3M6I4; -.
DR   SMR; B3M6I4; -.
DR   STRING; 7217.FBpp0113899; -.
DR   EnsemblMetazoa; FBtr0115407; FBpp0113899; FBgn0087748.
DR   GeneID; 6493575; -.
DR   KEGG; dan:6493575; -.
DR   eggNOG; KOG0575; Eukaryota.
DR   HOGENOM; CLU_008726_2_0_1; -.
DR   InParanoid; B3M6I4; -.
DR   OMA; GNECFTH; -.
DR   OrthoDB; 507604at2759; -.
DR   PhylomeDB; B3M6I4; -.
DR   ChiTaRS; SAK; fly.
DR   Proteomes; UP000007801; 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:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
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:EnsemblMetazoa.
DR   GO; GO:0007140; P:male meiotic nuclear division; IEA:EnsemblMetazoa.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:EnsemblMetazoa.
DR   GO; GO:0046777; P:protein autophosphorylation; IEA:EnsemblMetazoa.
DR   GO; GO:0046599; P:regulation of centriole replication; IEA:EnsemblMetazoa.
DR   GO; GO:0031647; P:regulation of protein stability; IEA:EnsemblMetazoa.
DR   GO; GO:0007288; P:sperm axoneme assembly; IEA:EnsemblMetazoa.
DR   GO; GO:0035186; P:syncytial blastoderm mitotic cell cycle; IEA:EnsemblMetazoa.
DR   CDD; cd13114; POLO_box_Plk4_1; 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   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..770
FT                   /note="Serine/threonine-protein kinase PLK4"
FT                   /id="PRO_0000385288"
FT   DOMAIN          14..267
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          383..500
FT                   /note="Cryptic POLO box 1 (CPB1)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT   DOMAIN          501..604
FT                   /note="Cryptic POLO box 2 (CPB2)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT   DOMAIN          667..733
FT                   /note="POLO box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         20..28
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   770 AA;  87007 MW;  8E9641F9D8C8F7B6 CRC64;
     MLSNRAFGET IEEYEVQHLL GKGGFASVYK ARCLHTHQDV AIKMIDKKLI QGTGLTNRVR
     QEVEIHSRLK HPSVLQLYTF FQDANYVYLV LELAHNGELH RYMNHIGRPF TEAEAASILR
     QVVAGLLYLH SHNIMHRDIS LSNLLLSKEM HVKIADFGLA TQLKRPDERH VTMCGTPNYI
     SPEVVSRTSH GLPADVWSVG CMLYTLLVGR PPFETDAVQT TLNKVVLSEY IMPTHLSFEA
     QDLINKLLKK VPHERIALEH VLRHPFLTKR LENSSNGVYS TPGALNVFSQ SLESGDSGII
     TFASSDSRNS QRLRSVENTA PLQGLPQIQE EYMQDKYRPT YDQPGLFKQP SSTRMEHNWL
     TTEKDTPFRM DVPMKEKPAP LKEERISVPP LNTKRLLPTR YKTKNAIMSI LRNGEVVLEF
     LKYRPKFNED RVTDICRISD DGRRIIIYQP DPGRGLPIRD HPPELQIPNE DCVYNYDSLP
     SKHWKKYVYA DRFVGLVKSK TPKVTYFSAL GKCQLMETMT DFEIRFYSGA KLTKSPSEGL
     KVHNANGMLL SDHVGSEARS MIDHGNECFT HCVSISNALE MAQTKDNSCF PVTIGRRPVT
     EVQPSQRLDG LRDTTNFAYS TPKSNQGSIN FSVSTISSIR NTTDFGSNSS RTNMRASQQN
     IPIKRINLPD IGVATELSHG VVQVQFYDGS VVSIIPDIQG GGVTYTQSNG ISTHFGKDDD
     LPFTVREKLS QLPHIQLKLK TAPLLSNSRK IEFNAMTPKT TTPCYNRMLL
 
 
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