PLK3_RAT
ID PLK3_RAT Reviewed; 647 AA.
AC Q9R011;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Serine/threonine-protein kinase PLK3;
DE EC=2.7.11.21;
DE AltName: Full=Cytokine-inducible serine/threonine-protein kinase;
DE AltName: Full=FGF-inducible kinase;
DE AltName: Full=Polo-like kinase 3;
DE Short=PLK-3;
GN Name=Plk3; Synonyms=Cnk, Fnk;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CIB1, TISSUE SPECIFICITY,
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10523297; DOI=10.1093/emboj/18.20.5528;
RA Kauselmann G., Weiler M., Wulff P., Jessberger S., Konietzko U.,
RA Scafidi J., Staubli U., Bereiter-Hahn J., Strebhardt K., Kuhl D.;
RT "The polo-like protein kinases Fnk and Snk associate with a Ca(2+)- and
RT integrin-binding protein and are regulated dynamically with synaptic
RT plasticity.";
RL EMBO J. 18:5528-5539(1999).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in cell cycle
CC regulation, response to stress and Golgi disassembly. Polo-like kinases
CC act by binding and phosphorylating proteins are that already
CC phosphorylated on a specific motif recognized by the POLO box domains.
CC Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN,
CC p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle
CC regulation: required for entry into S phase and cytokinesis.
CC Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and
CC progression to cytokinesis during mitosis. Plays a key role in response
CC to stress: rapidly activated upon stress stimulation, such as ionizing
CC radiation, reactive oxygen species (ROS), hyperosmotic stress, UV
CC irradiation and hypoxia. Involved in DNA damage response and G1/S
CC transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73.
CC Phosphorylates p53/TP53 in response to reactive oxygen species (ROS),
CC thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in
CC response to DNA damage, promoting the G2/M transition checkpoint.
CC Phosphorylates the transcription factor p73/TP73 in response to DNA
CC damage, leading to inhibit p73/TP73-mediated transcriptional activation
CC and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response
CC to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in
CC corneal epithelium. Also involved in Golgi disassembly during the cell
CC cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi
CC fragmentation during mitosis by mediating phosphorylation of VRK1. May
CC participate in endomitotic cell cycle, a form of mitosis in which both
CC karyokinesis and cytokinesis are interrupted and is a hallmark of
CC megakaryocyte differentiation, via its interaction with CIB1 (By
CC 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: Interacts with GOLGB1 (By similarity). Interacts (via the
CC POLO-box domain) with CIB1; leading to inhibit PLK3 kinase activity.
CC {ECO:0000250, ECO:0000269|PubMed:10523297}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000269|PubMed:10523297}. Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Note=Translocates to the nucleus upon
CC cisplatin treatment. Localizes to the Golgi apparatus during interphase
CC (By similarity). When induced, it translocates into the dendrites of
CC activated neurons. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in post-mitotic neurons.
CC {ECO:0000269|PubMed:10523297}.
CC -!- INDUCTION: By the intense activity associated with seizures.
CC {ECO:0000269|PubMed:10523297}.
CC -!- DOMAIN: The POLO box domains act as phosphopeptide-binding module that
CC recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X)
CC motifs. PLK3 recognizes and binds docking proteins that are already
CC phosphorylated on these motifs, and then phosphorylates them. The POLO
CC box domains mediates localization to the centrosome (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated in an ATM-dependent manner following DNA damage.
CC Phosphorylated as cells enter mitosis and dephosphorylated as cells
CC exit mitosis (By similarity). {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}.
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DR EMBL; AF136584; AAF08367.1; -; mRNA.
DR RefSeq; NP_071523.1; NM_022187.1.
DR AlphaFoldDB; Q9R011; -.
DR SMR; Q9R011; -.
DR BioGRID; 248673; 1.
DR STRING; 10116.ENSRNOP00000025197; -.
DR PhosphoSitePlus; Q9R011; -.
DR PaxDb; Q9R011; -.
DR PRIDE; Q9R011; -.
DR Ensembl; ENSRNOT00000025197; ENSRNOP00000025197; ENSRNOG00000018484.
DR GeneID; 58936; -.
DR KEGG; rno:58936; -.
DR UCSC; RGD:62039; rat.
DR CTD; 1263; -.
DR RGD; 62039; Plk3.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000159121; -.
DR HOGENOM; CLU_000288_46_1_1; -.
DR InParanoid; Q9R011; -.
DR OMA; KKSKNHA; -.
DR OrthoDB; 507604at2759; -.
DR TreeFam; TF101089; -.
DR Reactome; R-RNO-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR PRO; PR:Q9R011; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000018484; Expressed in esophagus and 19 other tissues.
DR Genevisible; Q9R011; RN.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; TAS:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0090166; P:Golgi disassembly; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0044819; P:mitotic G1/S transition checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:1904716; P:positive regulation of chaperone-mediated autophagy; ISO:RGD.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:2000777; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:RGD.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; NAS:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; TAS:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; ISS:UniProtKB.
DR GO; GO:0009314; P:response to radiation; ISS:UniProtKB.
DR GO; GO:0000302; P:response to reactive oxygen species; ISS:UniProtKB.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR CDD; cd14189; STKc_PLK3; 1.
DR Gene3D; 3.30.1120.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR042703; PLK3_STKc.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR020658; Ser/Thr_kinase_PLK3.
DR PANTHER; PTHR24345:SF42; PTHR24345:SF42; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50078; POLO_BOX; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Cell cycle; Cell projection; Cytoplasm;
KW Cytoskeleton; DNA damage; Golgi apparatus; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..647
FT /note="Serine/threonine-protein kinase PLK3"
FT /id="PRO_0000414709"
FT DOMAIN 62..314
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 471..534
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 568..638
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 68..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 647 AA; 71768 MW; 44FAFD446E5F9999 CRC64;
MEPAAGFLSP RPFPRAAAPS SPPAGPGPPA SASPRSEPGV LAGPQTPDAS RLITDPRSGR
TYIKGRLLGK GGFARCYEAT DTETSIAYAV KVIPQSRVAK PHQREKIINE IELHRDLQHR
HIVRFSHHFE DADNIYIFLE LCSRKSLAHI WKARHTLLEP EVRYYLRQIL SGLKYLHQRG
ILHRDLKLGN FFITDNMELK VGDFGLAARL EPPEQRKKTI CGTPNYVAPE VLLRQGHGPE
ADVWSLGCVM YTLLCGSPPF ETADLKETYR CIKQVHYTLP ASLSLPARQL LAAILRASPR
DRPSIEQILR HDFFTKGYTP DRLPVSSCVT VPDLTPPNPA RSLFAKVTKS LFGRRKSKNK
NHSEEQDNVS CLVSGLMRTS IGHPDVRPEA PAASALAPVS LVETAAEDSS PRGTLASSGD
GFEEGLTVTT VVESALCALR NCVAFMPPAE QNPAPLAQPE PLVWVSKWVD YSNKFGFGYQ
LSSRRVAVLF NDGTHMALSA NRKTVHYNPT STKHFSFSVG SVPRALQPQL GILRYFASYM
EQHLMKGGDL PSVEEVEVPA PPLLLQWVKT DQALLMLFSD GTVQVNFYGD HTKLILSGWE
PLLVTFVARN RSACTYLASH LRQLGCSPDL RQRLRYALRL LRDRSPA
