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PLK4_DROVI
ID   PLK4_DROVI              Reviewed;         781 AA.
AC   B4LDJ6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=GJ11832;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
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; CH940647; EDW69957.1; -; Genomic_DNA.
DR   RefSeq; XP_002047615.1; XM_002047579.2.
DR   AlphaFoldDB; B4LDJ6; -.
DR   SMR; B4LDJ6; -.
DR   STRING; 7244.FBpp0226249; -.
DR   EnsemblMetazoa; FBtr0227757; FBpp0226249; FBgn0199086.
DR   GeneID; 6624728; -.
DR   KEGG; dvi:6624728; -.
DR   eggNOG; KOG0575; Eukaryota.
DR   HOGENOM; CLU_008726_2_0_1; -.
DR   InParanoid; B4LDJ6; -.
DR   OMA; GNECFTH; -.
DR   OrthoDB; 507604at2759; -.
DR   PhylomeDB; B4LDJ6; -.
DR   ChiTaRS; SAK; fly.
DR   Proteomes; UP000008792; 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:0007099; P:centriole replication; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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   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..781
FT                   /note="Serine/threonine-protein kinase PLK4"
FT                   /id="PRO_0000385297"
FT   DOMAIN          14..268
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          397..514
FT                   /note="Cryptic POLO box 1 (CPB1)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01328"
FT   DOMAIN          515..618
FT                   /note="Cryptic POLO box 2 (CPB2)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01329"
FT   DOMAIN          677..743
FT                   /note="POLO box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT   REGION          463..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        139
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   781 AA;  87271 MW;  31E7D1C3B46FABD3 CRC64;
     MLPFRTYGET IDEYEVQHLL GKGGFACVYK AKCLRSHQNV AIKMIDKKLI QGSGLSNRVR
     QEVEIHSRLK HPSVLQLYTF FQDANYVYLI LELADNGELH RYMNQQMKRP FTEQEAASIL
     RQVVDGLLYL HSHNIMHRDI SMSNLLLSKD MHVKIADFGL ATQLKRPDER HMTMCGTPNY
     ISPEVVSHQS HGLPADLWSV GCMLYTLLVG RPPFDTDAVQ STLNKVVQSD YTIPGHLSYE
     ARDLIDKLLR KNPHERISLE QVLRHPFMVK AGGSTISYTT NGASDGYGQS IVSGDSGIVT
     FASNDSKNSH RLRSVEQQAT PQMMPQIQEE YGYYQDHRQK YAPHAAYRQS SAETLDSTEM
     DWQRMGQNAQ KANFLAHSTP AAPVPAPVIR KAGKHNTEHI SVPPLNTLRL QPTRYKTKNA
     IMSIVANGEV VIEFIKSKSK MNEDRIIDIC RISGDGRRII IHQPDPGRGL PIQEQTSETH
     SSGTDNVYNY DNLPSKHWKK YVYAARFVGL VKSKTPKVTY FSALAKCHLM ENMTDFEMNY
     YSGAKLTKSP SEGIKVFDIH GVQLLDQSSS EAKRLIEHSN ECFAHCLSIC NALELAQTGS
     NTCFPVTIGR RPVVEVLPSH RPEGLRDTTN FAYSTPKSQQ GSINFSISTI SSMRSGSDNI
     GSQLLAAQQN VPIKRLNVPG VGTATELSHG IVQVQFVDGS VISVIPEAQG GGITYTQSNG
     VSTHFPDHDD LPLSVRDRLS HLPQVQMKLR CAPLISSKKF DCNAMNAKST ASAPWYNRML
     I
 
 
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