POLO_DROME
ID POLO_DROME Reviewed; 576 AA.
AC P52304; A4V258; Q9VWB2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Serine/threonine-protein kinase polo;
DE EC=2.7.11.21;
GN Name=polo; ORFNames=CG12306;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo;
RX PubMed=1660828; DOI=10.1101/gad.5.12a.2153;
RA Llamazares S., Moreira A., Tavares A., Girdham C., Spruce B.A.,
RA Gonzalez C., Karess R.E., Glover D.M., Sunkel C.E.;
RT "Polo encodes a protein kinase homolog required for mitosis in
RT Drosophila.";
RL Genes Dev. 5:2153-2165(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182; THR-186; SER-299;
RP THR-302; SER-306; THR-323; SER-327 AND THR-328, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP FUNCTION.
RX PubMed=24829288; DOI=10.1098/rsob.140047;
RA Savoian M.S., Glover D.M.;
RT "Differing requirements for Augmin in male meiotic and mitotic spindle
RT formation in Drosophila.";
RL Open Biol. 4:140047-140047(2014).
CC -!- FUNCTION: May play a role in regulating both nuclear and cytoplasmic
CC aspects of the mitotic cycle (PubMed:1660828). Regulates localization
CC of the augmin complex during mitosis by ensuring its location on
CC mitotic spindles (PubMed:24829288). Also regulates augmin complex
CC localization during male meiosis by promoting its placement at
CC kinetochores while preventing its association with spindle microtubules
CC (PubMed:24829288). {ECO:0000269|PubMed:1660828,
CC ECO:0000269|PubMed:24829288}.
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 -!- INTERACTION:
CC P52304; Q23973: mtrm; NbExp=4; IntAct=EBI-163922, EBI-166563;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1660828}.
CC -!- TISSUE SPECIFICITY: Larval disks, brain and testis.
CC {ECO:0000269|PubMed:1660828}.
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; X63361; CAA44963.1; -; mRNA.
DR EMBL; AE014296; AAF49036.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52738.1; -; Genomic_DNA.
DR EMBL; AY095028; AAM11356.1; -; mRNA.
DR PIR; S22127; S22127.
DR RefSeq; NP_001014592.1; NM_001014592.2.
DR RefSeq; NP_524179.2; NM_079455.4.
DR AlphaFoldDB; P52304; -.
DR SMR; P52304; -.
DR BioGRID; 65494; 84.
DR DIP; DIP-18462N; -.
DR IntAct; P52304; 5.
DR MINT; P52304; -.
DR STRING; 7227.FBpp0074608; -.
DR iPTMnet; P52304; -.
DR PaxDb; P52304; -.
DR PRIDE; P52304; -.
DR EnsemblMetazoa; FBtr0074839; FBpp0074608; FBgn0003124.
DR EnsemblMetazoa; FBtr0100318; FBpp0099722; FBgn0003124.
DR GeneID; 40232; -.
DR KEGG; dme:Dmel_CG12306; -.
DR CTD; 40232; -.
DR FlyBase; FBgn0003124; polo.
DR VEuPathDB; VectorBase:FBgn0003124; -.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000157752; -.
DR HOGENOM; CLU_000288_46_1_1; -.
DR InParanoid; P52304; -.
DR OMA; LKHFERY; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; P52304; -.
DR BRENDA; 2.7.11.21; 1994.
DR Reactome; R-DME-156711; Polo-like kinase mediated events.
DR Reactome; R-DME-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-DME-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DME-176412; Phosphorylation of the APC/C.
DR Reactome; R-DME-176417; Phosphorylation of Emi1.
DR Reactome; R-DME-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DME-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DME-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-DME-68881; Mitotic Metaphase/Anaphase Transition.
DR Reactome; R-DME-68884; Mitotic Telophase/Cytokinesis.
DR Reactome; R-DME-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-DME-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; P52304; -.
DR BioGRID-ORCS; 40232; 1 hit in 3 CRISPR screens.
DR ChiTaRS; polo; fly.
DR GenomeRNAi; 40232; -.
DR PRO; PR:P52304; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003124; Expressed in egg cell and 19 other tissues.
DR ExpressionAtlas; P52304; baseline and differential.
DR Genevisible; P52304; DM.
DR GO; GO:0005814; C:centriole; IDA:FlyBase.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:FlyBase.
DR GO; GO:0005874; C:microtubule; IDA:FlyBase.
DR GO; GO:0030496; C:midbody; IDA:FlyBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:FlyBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000940; C:outer kinetochore; IDA:FlyBase.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:0000922; C:spindle pole; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IMP:FlyBase.
DR GO; GO:0030954; P:astral microtubule nucleation; IMP:FlyBase.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IDA:CACAO.
DR GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:FlyBase.
DR GO; GO:0007147; P:female meiosis II; IMP:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0030726; P:male germline ring canal formation; IMP:FlyBase.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0051257; P:meiotic spindle midzone assembly; IMP:FlyBase.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0048600; P:oocyte fate commitment; IMP:FlyBase.
DR GO; GO:0007344; P:pronuclear fusion; IMP:FlyBase.
DR GO; GO:0035046; P:pronuclear migration; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:0035044; P:sperm aster formation; IMP:FlyBase.
DR GO; GO:0007058; P:spindle assembly involved in female meiosis II; IMP:FlyBase.
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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..576
FT /note="Serine/threonine-protein kinase polo"
FT /id="PRO_0000086578"
FT DOMAIN 25..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 398..461
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 496..564
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 186
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 302
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 323
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 187
FT /note="P -> A (in Ref. 1; CAA44963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 66974 MW; 5022B9AC0E888FAD CRC64;
MAAKPEDKST DIPDRLVDIN QRKTYKRMRF FGKGGFAKCY EIIDVETDDV FAGKIVSKKL
MIKHNQKEKT AQEITIHRSL NHPNIVKFHN YFEDSQNIYI VLELCKKRSM MELHKRRKSI
TEFECRYYIY QIIQGVKYLH DNRIIHRDLK LGNLFLNDLL HVKIGDFGLA TRIEYEGERK
KTLCGTPNYI APEILTKKGH SFEVDIWSIG CVMYTLLVGQ PPFETKTLKD TYSKIKKCEY
RVPSYLRKPA ADMVIAMLQP NPESRPAIGQ LLNFEFLKGS KVPMFLPSSC LTMAPRIGSN
DTIEDSMHRK PLMEMNGIRP DDTRLESTFL KANLHDAITA SAQVCRHSED YRSDIESLYQ
QLTNLINGKP RILQGNLGDE NTDPAAQPLF WISKWVDYSD KYGFGYQLCD EGIGVMFNDT
TKLILLPNQI NVHFIDKDGK ETYMTTTDYC KSLDKKMKLL SYFKRYMIEH LVKAGANNVN
IESDQISRMP HLHSWFRTTC AVVMHLTNGS VQLNFSDHMK LILCPRMSAI TYMDQEKNFR
TYRFSTIVEN GVSKDLYQKI RYAQEKLRKM LEKMFT
