BOREA_DROME
ID BOREA_DROME Reviewed; 315 AA.
AC Q9VLD6; Q8I0R3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Borealin;
DE AltName: Full=Aurora borealis protein;
DE AltName: Full=Borealin-related;
GN Name=borr; ORFNames=CG4454;
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 [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 [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
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 [4]
RP FUNCTION, MEMBER OF THE CPC COMPLEX, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16224046; DOI=10.1242/dev.02057;
RA Hanson K.K., Kelley A.C., Bienz M.;
RT "Loss of Drosophila borealin causes polyploidy, delayed apoptosis and
RT abnormal tissue development.";
RL Development 132:4777-4787(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-146; SER-152; SER-163;
RP SER-205; THR-209; SER-218; SER-220 AND SER-244, 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).
CC -!- FUNCTION: Component of the chromosomal passenger complex (CPC), a
CC complex that acts as a key regulator of embryonic mitosis. The CPC
CC complex has essential functions at the centromere for ensuring sister
CC chromatid cohesion, recruitment of the CPC to kinetochores, and
CC chromosome alignment and segregation. There is no function in meiotic
CC histone phosphorylation or spindle formation.
CC {ECO:0000269|PubMed:16224046}.
CC -!- SUBUNIT: Component of the CPC complex.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16224046}.
CC Chromosome, centromere {ECO:0000269|PubMed:16224046}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:16224046}. Note=Localizes on
CC chromosome arms and inner centromeres from prophase through metaphase
CC and then transferring to the spindle midzone and midbody from anaphase
CC through cytokinesis. Colocalizes with and is required for the correct
CC localization of the CPC components Aurora B kinase and Incenp in
CC mitotic cells. Is absent from spermatocytes undergoing meiosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9VLD6-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9VLD6-2; Sequence=VSP_019925;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in the early embryo.
CC Expression is restricted to the ventral nerve cord and brain during
CC later embryonic stages.
CC -!- DISRUPTION PHENOTYPE: Flies show multiple mitotic defects, including
CC multipolar spindles that result in large polyploid cells and often in
CC delayed apoptosis. The developmental consequences of these defects
CC include cell-autonomous and non-autonomous defects in cell-type
CC specification and tissue architecture. Flies also display a drastic
CC decrease in histone H3 'Ser-10' phosphorylation, suggesting that the
CC CPC complex mediates phosphorylation of 'Ser-10' of histone H3.
CC {ECO:0000269|PubMed:16224046}.
CC -!- SIMILARITY: Belongs to the borealin family. {ECO:0000305}.
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DR EMBL; AE014134; AAF52757.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10690.1; -; Genomic_DNA.
DR EMBL; AY061432; AAL28980.1; -; mRNA.
DR EMBL; BT001609; AAN71364.1; -; mRNA.
DR RefSeq; NP_609279.1; NM_135435.5. [Q9VLD6-1]
DR RefSeq; NP_723450.1; NM_164850.4. [Q9VLD6-2]
DR AlphaFoldDB; Q9VLD6; -.
DR SMR; Q9VLD6; -.
DR BioGRID; 60352; 19.
DR IntAct; Q9VLD6; 1.
DR STRING; 7227.FBpp0079417; -.
DR iPTMnet; Q9VLD6; -.
DR PaxDb; Q9VLD6; -.
DR PRIDE; Q9VLD6; -.
DR DNASU; 34245; -.
DR EnsemblMetazoa; FBtr0079817; FBpp0079416; FBgn0032105. [Q9VLD6-1]
DR EnsemblMetazoa; FBtr0079818; FBpp0079417; FBgn0032105. [Q9VLD6-2]
DR GeneID; 34245; -.
DR KEGG; dme:Dmel_CG4454; -.
DR UCSC; CG4454-RA; d. melanogaster. [Q9VLD6-1]
DR CTD; 34245; -.
DR FlyBase; FBgn0032105; borr.
DR VEuPathDB; VectorBase:FBgn0032105; -.
DR eggNOG; ENOG502SAXQ; Eukaryota.
DR InParanoid; Q9VLD6; -.
DR OMA; RPRQGEM; -.
DR PhylomeDB; Q9VLD6; -.
DR Reactome; R-DME-4615885; SUMOylation of DNA replication proteins.
DR SignaLink; Q9VLD6; -.
DR BioGRID-ORCS; 34245; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34245; -.
DR PRO; PR:Q9VLD6; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032105; Expressed in ovary and 22 other tissues.
DR Genevisible; Q9VLD6; DM.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0032133; C:chromosome passenger complex; IDA:FlyBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR GO; GO:1990385; C:meiotic spindle midzone; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
DR GO; GO:1902889; P:protein localization to spindle microtubule; IMP:UniProtKB.
DR InterPro; IPR018867; Cell_div_borealin.
DR Pfam; PF10512; Borealin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Cytoplasm; Cytoskeleton; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..315
FT /note="Borealin"
FT /id="PRO_0000247083"
FT REGION 103..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 117
FT /note="E -> EGYLT (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_019925"
SQ SEQUENCE 315 AA; 34681 MW; AC1DF9F5960C9F2A CRC64;
MPRTKIPKNS KRNREVANRE EKVRLYELKM DSRLISIDSL ETKFLSAVDH QVKTLLGQVQ
KELANLKMPE VLRLFEELDR FSDFKASDQT QLLASMSMSG SAIEGHAPSA TGSRNDEEDS
SIGASGGSIL AAHTGSLLRS TKAMRTPGPL HSARARRARR SRSACGDLNI LHSAKPPSIS
SSSSSSRNSR SKLRTPMASR AKAFSADRTP LKQKQMRSGS PTTPPMAFLR YPKPGEVALS
KYGSPMVAQV MPDKFANVNI PIRNGVLSLR PKKLDADEVE SNLLENLDED TLNQIKTLHE
NLQMIVNKAS QAVFK
