ID G3WKI1_SARHA Unreviewed; 968 AA.
AC G3WKI1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 61.
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=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 Name=PLK4 {ECO:0000313|Ensembl:ENSSHAP00000015936.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000015936.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000015936.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000015936.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}.
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DR AlphaFoldDB; G3WKI1; -.
DR Ensembl; ENSSHAT00000016067.2; ENSSHAP00000015936.2; ENSSHAG00000013575.2.
DR GeneTree; ENSGT00940000156316; -.
DR HOGENOM; CLU_008726_1_0_1; -.
DR InParanoid; G3WKI1; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0098536; C:deuterosome; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0120098; C:procentriole; IEA:Ensembl.
DR GO; GO:0120099; C:procentriole replication complex; IEA:Ensembl.
DR GO; GO:0001741; C:XY body; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007099; P:centriole replication; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0046601; P:positive regulation of centriole replication; IEA:Ensembl.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IEA:Ensembl.
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; 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: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 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.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
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:0000256|ARBA:ARBA00022527};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 13..266
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 584..697
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000259|PROSITE:PS51984"
FT DOMAIN 698..811
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000259|PROSITE:PS51985"
FT DOMAIN 890..954
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 377..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 968 AA; 108060 MW; 4BC03F5BD88DEDAD CRC64;
MPCPRDASAI EDFRVGNLLG KGSFAGVYRA ESIHTGLEVA IKMIDKKAMH KAGMVQRVQN
EVKIHCQLKH PSILELYNYF EDSNYVYLVL EICHNGEMNR YLKNKMKPFS ESEARQFMHQ
ITTGMLYLHS HGILHRDLTL SNLLLTRNMN IKIADFGLAT QLKMPNEKHY TLCGTPNYIS
PEVATRSAHG LESDVWSLGC MFYTLLIGRP PFDTDTVKNT LNKVVLADYE MPTFLSLEAK
DLIHQLLRRN PAERLSLSSV LDHPFMCRSS SVRIKDLGTV EDSIDSGHAT ISTALTGSSS
ASISGCLPDK KRLLFGQPLP NKMTIFPKTK NVSNFSSGDG SSFYPQWGVQ GQETNHSGRG
RLLQDAEERP HSRYLRRAHS SDRSGISSGH SQAKPPAVER CHSADILSKP NRRGWPENER
FSPTDSNANM FQVFKENTSN ITGSFERPDK DQAHLLHPGK STFPLSEQTS HSETVQQWFG
NLQANAQLKE PTAHINITSG RNVQDHPDLQ DTRRNAWTDK MTNRDTDASD SACCVKQPNA
MKCIPAYRHE PETIQPATVF GSHPLSDPSR SRGREPQIGH QKCTLRSMTS PLNAHRLKPI
RQKTKKAVVS ILDTEEVCVE LLKEFASQEY VKEVLQVSSD GNSITIYYPN DGKGFPLDNR
PFPPPKDMIR YNFDSLPEKY WRKYQYASRF VQLVRSKTPK ITFFSKYAKC ILMENSPHAD
FEVWFYDGAK IHKTEDLINV IEKSGKSYTL KGEAEIESLK EEIKIYVDHA NEGHRLCLAL
ESVISVEETK SGSVPFFPII IGRKPGNPSS PQPMTPPSCV DSNSSVKDSA LLNRMMVSSS
ASSNQAPNIS PSIVPCEGSG LTAAVHETEG SSTSPKDYLP KSAQLLKSVF VKNVGWATQL
TSGAVWVQFN DGSQLVVQAG VHSISYTSPN GQTTRYGENE KLPEFIKEKL QCLSSILLMF
ANPASGSH
//
