PLK2_CAEEL
ID PLK2_CAEEL Reviewed; 632 AA.
AC Q9N2L7;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Serine/threonine-protein kinase plk-2;
DE EC=2.7.11.21 {ECO:0000269|PubMed:22018921};
DE AltName: Full=Polo-like kinase 2;
GN Name=plk-2 {ECO:0000312|WormBase:Y71F9B.7};
GN ORFNames=Y71F9B.7 {ECO:0000312|WormBase:Y71F9B.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAF28314.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11092748; DOI=10.3109/10425170009033251;
RA Chase D., Golden A., Heidecker G., Ferris D.K.;
RT "Caenorhabditis elegans contains a third polo-like kinase gene.";
RL DNA Seq. 11:327-334(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND INTERACTION WITH NICOTINIC ACETYLCHOLINE RECEPTOR.
RX PubMed=15990870; DOI=10.1038/sj.emboj.7600741;
RA Gottschalk A., Almedom R.B., Schedletzky T., Anderson S.D., Yates J.R. III,
RA Schafer W.R.;
RT "Identification and characterization of novel nicotinic receptor-associated
RT proteins in Caenorhabditis elegans.";
RL EMBO J. 24:2566-2578(2005).
RN [4]
RP FUNCTION, INTERACTION WITH MEX-5 AND MEX-6, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18199581; DOI=10.1242/dev.013425;
RA Nishi Y., Rogers E., Robertson S.M., Lin R.;
RT "Polo kinases regulate C. elegans embryonic polarity via binding to DYRK2-
RT primed MEX-5 and MEX-6.";
RL Development 135:687-697(2008).
RN [5]
RP FUNCTION, INTERACTION WITH HIM-8; MEX-5 AND MEX-6, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22018922; DOI=10.1016/j.devcel.2011.09.001;
RA Harper N.C., Rillo R., Jover-Gil S., Assaf Z.J., Bhalla N., Dernburg A.F.;
RT "Pairing centers recruit a Polo-like kinase to orchestrate meiotic
RT chromosome dynamics in C. elegans.";
RL Dev. Cell 21:934-947(2011).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH SUN-1, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF PRO-197.
RX PubMed=22018921; DOI=10.1016/j.devcel.2011.07.011;
RA Labella S., Woglar A., Jantsch V., Zetka M.;
RT "Polo kinases establish links between meiotic chromosomes and cytoskeletal
RT forces essential for homolog pairing.";
RL Dev. Cell 21:948-958(2011).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30383754; DOI=10.1371/journal.pgen.1007653;
RA Janisiw E., Dello Stritto M.R., Jantsch V., Silva N.;
RT "BRCA1-BARD1 associate with the synaptonemal complex and pro-crossover
RT factors and influence RAD-51 dynamics during Caenorhabditis elegans
RT meiosis.";
RL PLoS Genet. 14:e1007653-e1007653(2018).
CC -!- FUNCTION: Serine/threonine-protein kinase which plays a role, during
CC oogenesis, in chromosome pairing and synapsis, by facilitating the
CC recruitment and attachment of meiotic chromosomes to the nuclear
CC envelope during prophase (PubMed:22018922, PubMed:22018921). Promotes
CC the localization of brc-1 to the short arm of homologous chromosomes
CC during meiotic prophase I (PubMed:30383754). Regulates the formation of
CC sun-1 patches along the nuclear envelope (PubMed:22018922,
CC PubMed:22018921). Promotes meiotic nuclei apoptosis in response to
CC chromosomal asynapsis (PubMed:22018922). Plays a redundant role with
CC plk-1 in the establishment of cell polarity downstream of mex-5 and
CC mex-6 during the first embryonic cell divisions (PubMed:18199581).
CC Plays a role in nicotinic acetylcholine receptor-mediated sensitivity
CC to nicotine but not levamisole (PubMed:15990870). Regulates motility
CC (PubMed:15990870). {ECO:0000269|PubMed:15990870,
CC ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:22018921,
CC ECO:0000269|PubMed:22018922, ECO:0000269|PubMed:30383754}.
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:0000269|PubMed:22018921};
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:0000269|PubMed:22018921};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22018921};
CC -!- SUBUNIT: Interacts (via POLO box domain) with mex-5 and mex-6
CC (PubMed:18199581, PubMed:22018922). Interacts (via POLO box domain)
CC with him-8 (via N-terminus); the interaction mediates plk-2 recruitment
CC to the pairing region of X chromosomes during meiosis
CC (PubMed:22018922). Interacts with sun-1 (PubMed:22018921). May interact
CC with nicotinic acetylcholine receptor (PubMed:15990870).
CC {ECO:0000269|PubMed:15990870, ECO:0000269|PubMed:18199581,
CC ECO:0000269|PubMed:22018921, ECO:0000269|PubMed:22018922}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22018921,
CC ECO:0000269|PubMed:22018922, ECO:0000269|PubMed:30383754}. Cytoplasm
CC {ECO:0000269|PubMed:18199581}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:22018922}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:22018922}.
CC Chromosome {ECO:0000269|PubMed:22018921, ECO:0000269|PubMed:22018922}.
CC Note=During meiosis I, localizes to chromosome pairing centers formed
CC at the nuclear envelope in early pachytene and then to the synaptonemal
CC complex in mid and late pachytene (PubMed:22018922, PubMed:22018921).
CC Co-localizes at pairing centers with him-8, zim-3, zyg-12 and sun-1 and
CC partially with plk-1 in early prophase (PubMed:22018922,
CC PubMed:22018921). Co-localizes with syp-1 in synapsed chromosomes at
CC pachytene (PubMed:22018921). Co-localizes with brc-1 in pachytene
CC nuclei (PubMed:30383754). Localizes asymmetrically in the 1-cell embryo
CC which results in higher levels in the somatic cell AB than in the
CC germline blastomere P1 (PubMed:18199581). {ECO:0000269|PubMed:18199581,
CC ECO:0000269|PubMed:22018921, ECO:0000269|PubMed:22018922,
CC ECO:0000269|PubMed:30383754}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes. {ECO:0000269|PubMed:22018921,
CC ECO:0000269|PubMed:22018922}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the early stages of embryogenesis.
CC {ECO:0000269|PubMed:18199581}.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable and fertile but about 30-
CC percent of the progeny die at the embryonic stage. Surviving adults are
CC mostly male (PubMed:22018922). Impaired chromosome pairing and synapsis
CC during meiotic prophase. Asymmetric disassembly of the synaptonemal
CC complex fails at the diplotene stage. Partial mis-segregation of
CC chromosomes. Increased germline apoptosis (PubMed:22018922).
CC Simultaneous knockdown of plk-1 and plk-2 causes a loss in pie-1
CC polarization in the 1-cell embryo, an increased association with the
CC oocyte pronuclei and a decrease in pie-1 degradation in embryonic
CC somatic cells (PubMed:18199581). {ECO:0000269|PubMed:18199581,
CC ECO:0000269|PubMed:22018922}.
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; AF194964; AAF28314.1; -; mRNA.
DR EMBL; BX284601; CCD70415.1; -; Genomic_DNA.
DR RefSeq; NP_491036.1; NM_058635.6.
DR AlphaFoldDB; Q9N2L7; -.
DR SMR; Q9N2L7; -.
DR BioGRID; 37319; 20.
DR IntAct; Q9N2L7; 2.
DR MINT; Q9N2L7; -.
DR STRING; 6239.Y71F9B.7; -.
DR iPTMnet; Q9N2L7; -.
DR EPD; Q9N2L7; -.
DR PaxDb; Q9N2L7; -.
DR PeptideAtlas; Q9N2L7; -.
DR PRIDE; Q9N2L7; -.
DR EnsemblMetazoa; Y71F9B.7.1; Y71F9B.7.1; WBGene00004043.
DR GeneID; 171838; -.
DR KEGG; cel:CELE_Y71F9B.7; -.
DR UCSC; Y71F9B.7.1; c. elegans.
DR CTD; 171838; -.
DR WormBase; Y71F9B.7; CE22877; WBGene00004043; plk-2.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000166918; -.
DR HOGENOM; CLU_000288_46_1_1; -.
DR InParanoid; Q9N2L7; -.
DR OMA; HPPFESK; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; Q9N2L7; -.
DR BRENDA; 2.7.11.21; 1045.
DR Reactome; R-CEL-156711; Polo-like kinase mediated events.
DR Reactome; R-CEL-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-CEL-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-CEL-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-CEL-68884; Mitotic Telophase/Cytokinesis.
DR Reactome; R-CEL-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-CEL-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q9N2L7; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004043; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0060631; P:regulation of meiosis I; IMP:WormBase.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR Gene3D; 3.30.1120.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 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 ATP-binding; Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinase;
KW Kinetochore; Meiosis; Nucleotide-binding; Nucleus; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..632
FT /note="Serine/threonine-protein kinase plk-2"
FT /id="PRO_0000086570"
FT DOMAIN 36..287
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 412..476
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 511..580
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 42..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 197
FT /note="P->L: In vv44; Loss of proper chromosome pairing and
FT early initiation of synapsis resulting in a loss of chiasma
FT formation and chromosome segregation during oocyte meiosis
FT I. Severe embryonic lethality and the few surviving adults
FT are mostly male. Loss of sun-1 and zyg-12 patch formation
FT along the nuclear envelope and of sun-1 phosphorylation at
FT 'Thr-12' during early prophase."
FT /evidence="ECO:0000269|PubMed:22018921"
SQ SEQUENCE 632 AA; 72071 MW; 1B2EBB58C15ABBD9 CRC64;
MQRVQPSAAR VKSQKKEKAP PDVPDVILDG ERKTRYEKGK FLGKGGFAHC YELRNKSTGE
LFAGKVVPKA LLIKQYQRDK MAQEVQIHRN LQHRNVVKLY HFFEDKSNVY ITLELCPRRS
LMELHKRRKA VTEPEARYFT YQIVEGVLYL HNLKIVHRDL KLGNLFLNDE LQVKIGDFGL
ATTCDNDERK KTLCGTPNYI APEVLNKIGH SFEVDLWAIG CILYILLFGH PPFESKSLEE
TYSRIKNNNY VIPTSASAAA SQLIRVLLDP VPSRRPNARA VCRDHFFKSG FMPARLPVSC
LTMVPHLNDD EYAEENVSPS GTIDQRGPHQ AGRSGLSAIP AHLVSRNSER QQTHRMEAYR
QPTDCYLSNL LAQVNDLLAT PTADIDDAEA ALDSYQSPEA LPVFWISKWV DYSDKYGIGY
QLCDNSVGVL FNDNSRIMLD TAGTQLTYIE KTEKEHYFDM ESAIPSGLQK KMTLLKYFRS
YMNDHLLQAG QQVTRKVGDD LARLPTLRVW FRTKSAIVLH LSNGTVQINF FNDHIKMVLC
PLMQAVTFID ENKRMFTYKF SHLAENGCPE KFLHRIQYAK CMIQRLVEEH TKEETKHNAP
AANAVRLPST SSNVRLESAA DIQPAYPSSS RR
