ID A0A060WXU8_ONCMY Unreviewed; 924 AA.
AC A0A060WXU8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=GSONMT00015919001 {ECO:0000313|EMBL:CDQ69420.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ69420.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ69420.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ69420.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR904668; CDQ69420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060WXU8; -.
DR STRING; 8022.A0A060WXU8; -.
DR PaxDb; 8022-A0A060WXU8; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; 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 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:UP000193380};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 12..265
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 558..671
FT /note="Cryptic POLO box 1 (CPB1)"
FT /evidence="ECO:0000259|PROSITE:PS51984"
FT DOMAIN 672..785
FT /note="Cryptic POLO box 2 (CPB2)"
FT /evidence="ECO:0000259|PROSITE:PS51985"
FT DOMAIN 847..911
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 924 AA; 102064 MW; 0B60550A05C6769C CRC64;
MSVSIGNKIE DFKVLTLLGK GSFACVYRAK SVNTGLEVAI KMIDKKAMHK SGMVQRVSNE
VEIQCRLKHP SILELYTYFE DSNYVYLVLE MCHNGEMSRY LKDRKMPFSE GEARHFMHQI
VKGMLYLHTH GIMHRDLTLS NLLLSGNMNL KIADFGLATK LKLPSEKHFT MCGTPNYISP
EVATHSAHGL ESDVWSLGCM FYAFLMGRPP FDTDTVKHTL NKVVLGEYDM PSHVSQEAQD
LIHQLLRKDP AQRPSLSAVL EHPFMTQSLL ARTKELSLGE PGSMDSGIAT ISTACTSSTS
GSSSSSSSRL QRRTRRVMGP ALPNRMMPIP TLPRPPSNAC FEGVEQWQQQ HSDRVGRSRA
APGGESGRPH SRYPRRAHSS DRSSSSVTPA QGMGQATLER CHSEEMLTVS GRLAFPMSSS
YKDTTQPFAE HGRLPLPPVK QTASSGCSYS TQPPRPLNLQ LEESEGVQNW FSKEGPFPRP
TDVSSHSSSG SFHSSREPLG VHNYWSDKPA GRGTSSHRNH NQHHPSNTES YWENGQRVHG
GELQSLSKPK PSIAKEKSLR NVLPPLCASR LKPIRQKTKN AVVSILDTGE VCMELLKGQG
PQERVKEVLR ISCDGSMVTI YQPNEGKGFP VLERPPAPPE DILICSYEDL PEKYWRKYQY
ASKFVLLVKS KTPKVTLYTK SAKCMLMENS PNADLEVCFY DGAKIHKTSE LVRVVKSGKS
YTVKGEVGLS GLSPESRLYV ELSDEGHSMC LSLEAAITAE EQHSAKSTPF FPITIGRRPA
NPDSSCPSSQ PATADVASLP QPPCFTPSRI SYEESDITSA SVNKNCSPLS VKQDHSANAG
KVLKSVFVPN IGWASQLTSG EVWVQFKDGS QLVVQAGVSC IIYTSPEGRT TRYKENEKLP
ELVKEKLHCL STILGLLASP AARR
//
