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Database: UniProt
Entry: L9KNC8_TUPCH
LinkDB: L9KNC8_TUPCH
Original site: L9KNC8_TUPCH 
ID   L9KNC8_TUPCH            Unreviewed;      1086 AA.
AC   L9KNC8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Serine/threonine-protein kinase PLK4 {ECO:0000256|ARBA:ARBA00020245};
DE            EC=2.7.11.21 {ECO:0000256|ARBA:ARBA00012424};
DE   AltName: Full=60S ribosomal protein L21 {ECO:0000256|ARBA:ARBA00035327};
DE   AltName: Full=Polo-like kinase 4 {ECO:0000256|ARBA:ARBA00030332};
DE   AltName: Full=Serine/threonine-protein kinase SAK {ECO:0000256|ARBA:ARBA00030429, ECO:0000256|ARBA:ARBA00030924};
GN   ORFNames=TREES_T100015076 {ECO:0000313|EMBL:ELW62652.1};
OS   Tupaia chinensis (Chinese tree shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX   NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW62652.1, ECO:0000313|Proteomes:UP000011518};
RN   [1] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhang G., Fan Y., Yao Y., Huang Z.;
RT   "Genome of the Chinese tree shrew, a rising model animal genetically
RT   related to primates.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23385571; DOI=10.1038/ncomms2416;
RA   Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA   Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA   Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA   Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA   Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT   "Genome of the Chinese tree shrew.";
RL   Nat. Commun. 4:1426-1426(2013).
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         Evidence={ECO:0000256|ARBA:ARBA00000540};
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; Evidence={ECO:0000256|ARBA:ARBA00000856};
CC   -!- SUBCELLULAR LOCATION: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC       centriole {ECO:0000256|ARBA:ARBA00004114}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family.
CC       {ECO:0000256|ARBA:ARBA00008427}.
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DR   EMBL; KB320806; ELW62652.1; -; Genomic_DNA.
DR   AlphaFoldDB; L9KNC8; -.
DR   STRING; 246437.L9KNC8; -.
DR   eggNOG; KOG0575; Eukaryota.
DR   InParanoid; L9KNC8; -.
DR   Proteomes; UP000011518; Unassembled WGS sequence.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; 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   CDD; cd14186; STKc_PLK4; 1.
DR   Gene3D; 2.40.50.930; -; 1.
DR   Gene3D; 3.30.1120.120; -; 1.
DR   Gene3D; 3.30.1120.130; -; 1.
DR   Gene3D; 6.10.250.3260; -; 1.
DR   Gene3D; 2.30.30.70; Ribosomal protein L21; 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; IPR001147; Ribosomal_eL21.
DR   InterPro; IPR036948; Ribosomal_eL21_sf.
DR   InterPro; IPR046437; Ser_Thr-PK_POLO_box_1_sf.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR   PANTHER; PTHR24345:SF89; SERINE/THREONINE-PROTEIN KINASE PLK4; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF18190; Plk4_PB1; 1.
DR   Pfam; PF18409; Plk4_PB2; 1.
DR   Pfam; PF01157; Ribosomal_L21e; 1.
DR   SUPFAM; SSF82615; Polo-box domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 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.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Kinase {ECO:0000313|EMBL:ELW62652.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000011518};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000313|EMBL:ELW62652.1}.
FT   DOMAIN          129..382
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          702..815
FT                   /note="Cryptic POLO box 1 (CPB1)"
FT                   /evidence="ECO:0000259|PROSITE:PS51984"
FT   DOMAIN          816..929
FT                   /note="Cryptic POLO box 2 (CPB2)"
FT                   /evidence="ECO:0000259|PROSITE:PS51985"
FT   DOMAIN          1008..1072
FT                   /note="POLO box"
FT                   /evidence="ECO:0000259|PROSITE:PS50078"
FT   REGION          459..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          926..945
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          961..992
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..538
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..645
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1086 AA;  123043 MW;  8B7AA1E7AE1D531F CRC64;
     MFSKPFRKHG VVPLTTYIRI YKQGNIVDIK RMGTVQKGMP HECYYGKTGR VYSVTQHAVG
     SVVNKQVKGK ILAKRINVRI EHIKHSKSRY SFLKCVKEND QKKKEAKQKG TWVQLKHQPA
     PHREAHFDFK VGNLLGKGSF AGVYRAESIH SGLEVAIKMI DKKAMYKAGM VQRVQNEVKI
     HCQLKHPSIL ELYNYFEDNN YVYLVLEMCH NGEMNRFLKN RMKPFTENEA RHFMHQIITG
     MLYLHSHGIL HRDLTLSNLL LTRNMNIKIA DFGLATQLKM PHEKHYTLCG TPNYISPEIA
     TRSAHGLESD IWSLGCMFYT LLIGRPPFDT DTVKNTLNKV VLADYEMPAF LSKEAKDLIH
     QLLRRNPADR LSLSSVLDHP FMSRNSSAKN KDLGTVEDSI DSGHATISTA ITASSSTSIS
     GSLYDRRRLL IGQPLPNKIT MFPKNKNFSD FSSSGDGSNF YTHWGNQEQE NNNSGRGRVF
     QDAEERPHSR YLRRAHSSDR SGTSNCQPRA KTHAMERCHS AEMLSKPTRS EGDENDERYS
     PTNSNVNIFQ VFKEKTSNNS RSFERPANDQ AFSNHLCPGK TPFPFPDQTP QTEMIQQWFG
     NLQINDHIRE TTEHNNPNRD FQGHPDLQDT SRNTWTDRRA PKNTDASDSA HPVKQTNTMK
     YTSARHSKPE IIQQESGFGL DALSEQTKTR GVEPPPSYEK RTLRSITSPL VARRLKPIRQ
     KTRKAVVSIL DSEEVCVELL KEYTSQEYVK EVLQISTDGN TITIYYPNDG RGFPLTDRPP
     SPTNSISRYT FDNLPEKYWR KYQYASRFVQ LVRSKSPKIT YFTRYAKCVL MENSPGADFE
     VWFYDGTKIH KTQDFIQMIE KTGKSYTLKG ESEVNILKEE IKVYMDHANE GHRICLALES
     IISEEEEKSR SASFFPIIVG RKPGSISSPK SLSPPPSVDP NYPVRERPSL SRMIVNNAAS
     PTQAPILNPS TAADEGPGLT TAASGASTSS NSVKDCLPKS AQLLKSVFVK NVGWATQLTS
     GAVWVQFNDG SQLVVQAGVS SISYTSPNGQ TTRYRENEKL PEYIKQKLQC LSSILLMFSN
     PTPSFP
//
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