BUCKY_DANRE
ID BUCKY_DANRE Reviewed; 639 AA.
AC H0WFA5;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Bucky ball {ECO:0000303|PubMed:19249209};
DE Short=buc {ECO:0000303|PubMed:19249209};
DE AltName: Full=Prion-like protein Bucky ball {ECO:0000305};
GN Name=buc {ECO:0000303|PubMed:19249209,
GN ECO:0000312|ZFIN:ZDB-GENE-070117-694};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=19249209; DOI=10.1016/j.cub.2009.01.038;
RA Bontems F., Stein A., Marlow F., Lyautey J., Gupta T., Mullins M.C.,
RA Dosch R.;
RT "Bucky ball organizes germ plasm assembly in zebrafish.";
RL Curr. Biol. 19:414-422(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18582455; DOI=10.1016/j.ydbio.2008.05.557;
RA Marlow F.L., Mullins M.C.;
RT "Bucky ball functions in Balbiani body assembly and animal-vegetal polarity
RT in the oocyte and follicle cell layer in zebrafish.";
RL Dev. Biol. 321:40-50(2008).
RN [4]
RP FUNCTION, AND INTERACTION WITH RBPMS2 AND DAZL.
RX PubMed=24496621; DOI=10.1242/dev.090449;
RA Heim A.E., Hartung O., Rothhaemel S., Ferreira E., Jenny A., Marlow F.L.;
RT "Oocyte polarity requires a Bucky ball-dependent feedback amplification
RT loop.";
RL Development 141:842-854(2014).
RN [5]
RP FUNCTION, INTERACTION WITH KIF5BA, AND SUBCELLULAR LOCATION.
RX PubMed=26253407; DOI=10.1242/dev.124586;
RA Campbell P.D., Heim A.E., Smith M.Z., Marlow F.L.;
RT "Kinesin-1 interacts with Bucky ball to form germ cells and is required to
RT pattern the zebrafish body axis.";
RL Development 142:2996-3008(2015).
RN [6]
RP FUNCTION, INTERACTION WITH TDRD6, DOMAIN, AND METHYLATION AT ARG-627 AND
RP ARG-629.
RX PubMed=30086300; DOI=10.1016/j.devcel.2018.07.009;
RA Roovers E.F., Kaaij L.J.T., Redl S., Bronkhorst A.W., Wiebrands K.,
RA de Jesus Domingues A.M., Huang H.Y., Han C.T., Riemer S., Dosch R.,
RA Salvenmoser W., Gruen D., Butter F., van Oudenaarden A., Ketting R.F.;
RT "Tdrd6a Regulates the Aggregation of Buc into Functional Subcellular
RT Compartments that Drive Germ Cell Specification.";
RL Dev. Cell 46:285-301(2018).
CC -!- FUNCTION: Prion-like protein required for the formation of Balbiani
CC body (electron-dense aggregates in the oocyte) and germ plasm assembly,
CC and for the establishment of oocyte polarity during early oogenesis
CC (PubMed:18582455, PubMed:19249209). Mobility and aggregation properties
CC are improved by tudor domain-containing protein tdrd6 through
CC interaction with dimethylated arginines Tri-RG domains
CC (PubMed:30086300). Establishes oocyte polarity through interactions
CC with RNA-binding proteins rbpms2 and dazl, initiating a positive
CC feedback loop amplification mechanism in the Balbiani body
CC (PubMed:24496621). Interaction of BUC protein and mRNA with rbpms2 and
CC dazl is required to mediate Balbiani body formation (PubMed:24496621).
CC Involved in recruitment of germ plasm to embryonic cleavage furrows and
CC dorsoventral patterning through interaction with Kinesin-1/KIF5BA
CC (PubMed:26253407). {ECO:0000269|PubMed:18582455,
CC ECO:0000269|PubMed:19249209, ECO:0000269|PubMed:24496621,
CC ECO:0000269|PubMed:26253407, ECO:0000269|PubMed:30086300}.
CC -!- SUBUNIT: Specifically interacts (when methylated) with tdrd6 (via Tudor
CC domain); interaction is responsible for recruitment of different
CC protein complexes to germ plasm (PubMed:30086300). Interacts with
CC rbpms2 and dazl; interaction mediates Balbiani body formation
CC (PubMed:24496621). Interacts with kif5ba; interaction leads to buc
CC enrichment at the embryonic cleavage furrows and mediates dorsoventral
CC patterning (PubMed:26253407). {ECO:0000269|PubMed:24496621,
CC ECO:0000269|PubMed:26253407, ECO:0000269|PubMed:30086300}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19249209,
CC ECO:0000269|PubMed:30086300}. Cleavage furrow
CC {ECO:0000269|PubMed:26253407}. Note=Localizes to nuage (a peri-nuclear
CC protein-RNA aggregate that associates closely with mitochondria), the
CC Balbiani body during oogenesis, and in the germ plasm upon
CC fertilization (PubMed:19249209, PubMed:30086300). Accumulates at
CC embryonic cleavage furrows (PubMed:26253407).
CC {ECO:0000269|PubMed:19249209, ECO:0000269|PubMed:26253407,
CC ECO:0000269|PubMed:30086300}.
CC -!- DEVELOPMENTAL STAGE: Expressed exclusively in the ovary, and protein
CC localizes to the Balbiani body during oogenesis and with the germ plasm
CC during early embryogenesis (PubMed:19249209). Accumulates at embryonic
CC cleavage furrows (PubMed:26253407). {ECO:0000269|PubMed:19249209,
CC ECO:0000269|PubMed:26253407}.
CC -!- DOMAIN: The dimethylated RG motifs (RG[X0-4]RG[X0-4]RG) motif mediates
CC interaction with TDRD6 and is required for Balbiani body formation.
CC {ECO:0000269|PubMed:30086300}.
CC -!- PTM: Symmetric dimethylarginine modification promotes interaction with
CC tdrd6. {ECO:0000269|PubMed:30086300}.
CC -!- DISRUPTION PHENOTYPE: Mutant fails to form Balbiani body, and vegetal
CC mRNAs are not localized in oocytes. {ECO:0000269|PubMed:18582455}.
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DR EMBL; CU693487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; JQ316532; AFA26704.1; -; mRNA.
DR RefSeq; NP_001243709.1; NM_001256780.1.
DR AlphaFoldDB; H0WFA5; -.
DR STRING; 7955.ENSDARP00000125536; -.
DR PaxDb; H0WFA5; -.
DR Ensembl; ENSDART00000150330; ENSDARP00000125536; ENSDARG00000096095.
DR Ensembl; ENSDART00000175159; ENSDARP00000144393; ENSDARG00000096095.
DR GeneID; 334375; -.
DR KEGG; dre:334375; -.
DR CTD; 334375; -.
DR ZFIN; ZDB-GENE-070117-694; buc.
DR eggNOG; ENOG502QUT7; Eukaryota.
DR GeneTree; ENSGT00940000171744; -.
DR HOGENOM; CLU_428216_0_0_1; -.
DR InParanoid; H0WFA5; -.
DR OMA; RPYMAPY; -.
DR OrthoDB; 365325at2759; -.
DR PRO; PR:H0WFA5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000096095; Expressed in cleaving embryo and 21 other tissues.
DR ExpressionAtlas; H0WFA5; baseline and differential.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016333; P:morphogenesis of follicular epithelium; IMP:ZFIN.
DR GO; GO:0060832; P:oocyte animal/vegetal axis specification; IMP:ZFIN.
DR GO; GO:0007314; P:oocyte anterior/posterior axis specification; IMP:ZFIN.
DR GO; GO:0007315; P:pole plasm assembly; IMP:ZFIN.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cytoplasm; Differentiation; Methylation; Oogenesis; Reference proteome;
KW Spermatogenesis.
FT CHAIN 1..639
FT /note="Bucky ball"
FT /id="PRO_0000448684"
FT REGION 178..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 627..628
FT /note="RG Motif 1"
FT /evidence="ECO:0000269|PubMed:30086300"
FT MOTIF 629..630
FT /note="RG Motif 2"
FT /evidence="ECO:0000269|PubMed:30086300"
FT MOTIF 635..636
FT /note="RG Motif 3"
FT /evidence="ECO:0000269|PubMed:30086300"
FT COMPBIAS 223..242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 627
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:30086300"
FT MOD_RES 629
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:30086300"
SQ SEQUENCE 639 AA; 72011 MW; BF1C43B064BC1E47 CRC64;
MEGINNNSQP MGVGQPHHPV NHTRPFFYVQ PPSQPYFMYQ WPMNPYGHYG FPGPALHFGR
PYMAPYQFMQ YPGYVIPHAP MQPIDYRRIN PHYPSVASYD LRVRHHFQNA GMHRETACSE
VQTDPSDSVN KLIDKIESLK ACELGSDKGP NNVVSSTPDV VQGEKLTRLN EDSNLEVATK
ECKEDPVTRP TTYSDSAYDA ESSQGRLDEC VFSDVLPLDS SSVHEEEEEE EKDVNEEDEP
QTVADEICSQ NEMSASTTSN VFCSGVQSIA DPTECHDLEK LGDEQKQDIP SADAAAVIEP
LISLSEDFDL PYQILRLPCN KTTTGLSLER EIDPLVYFDS PSTLLPPQNY LSSIGSAYSY
SYYPQVTQER QSVLSPSIDE LSSRDEMFST DVEDLEVVPG HVYVGGGRLA EASDMPVRSR
KELPSVDKTC SVCQKTCACC GSTLQDEVGM CKMAEHSHPE RDEMSDQDCD YDLEAEVRSN
CESPRVSKRK CCSRHALPSC GHHCAKHRHR KLLCEGQESC DLREQARVHP KGECCEEYGA
LAKADKRIQK GALCRPCIEQ QWREGVVSDQ ENWASCGAKP RSWRQVTGPQ DQGRTPLRRS
TCKSIHQQRP RSEYNDYDET EFTYCQRGRG SMKKRGSRY
