BOP1_DANRE
ID BOP1_DANRE Reviewed; 777 AA.
AC A0JMQ0; Q1LXV3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ribosome biogenesis protein bop1 {ECO:0000255|HAMAP-Rule:MF_03027};
DE AltName: Full=Block of proliferation 1 protein {ECO:0000255|HAMAP-Rule:MF_03027};
GN Name=bop1; ORFNames=si:ch211-251g8.4;
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;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the PeBoW complex, which is required for
CC maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_03027}.
CC -!- SUBUNIT: Component of the PeBoW complex, composed of bop1, pes1 and
CC wdr12. The complex is held together by bop1, which interacts with pes1
CC via its N-terminal domain and with wdr12 via a high-affinity
CC interaction between the seven-bladed beta-propeller domains of the 2
CC proteins. The PeBoW complex associates with the 66S pre-ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_03027}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC Rule:MF_03027}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03027}.
CC -!- SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family.
CC {ECO:0000255|HAMAP-Rule:MF_03027}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK04774.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX255894; CAK04774.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC125962; AAI25963.1; -; mRNA.
DR RefSeq; NP_001071203.1; NM_001077735.1.
DR AlphaFoldDB; A0JMQ0; -.
DR SMR; A0JMQ0; -.
DR STRING; 7955.ENSDARP00000120969; -.
DR PaxDb; A0JMQ0; -.
DR PeptideAtlas; A0JMQ0; -.
DR GeneID; 777627; -.
DR KEGG; dre:777627; -.
DR CTD; 23246; -.
DR ZFIN; ZDB-GENE-030219-109; bop1.
DR eggNOG; KOG0650; Eukaryota.
DR InParanoid; A0JMQ0; -.
DR OrthoDB; 759498at2759; -.
DR PhylomeDB; A0JMQ0; -.
DR Reactome; R-DRE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:A0JMQ0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070545; C:PeBoW complex; ISS:UniProtKB.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:UniProtKB-UniRule.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03027; BOP1; 1.
DR InterPro; IPR028598; BOP1/Erb1.
DR InterPro; IPR012953; BOP1_N_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR17605; PTHR17605; 1.
DR Pfam; PF08145; BOP1NT; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM01035; BOP1NT; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Repeat; Ribosome biogenesis; rRNA processing;
KW WD repeat.
FT CHAIN 1..777
FT /note="Ribosome biogenesis protein bop1"
FT /id="PRO_0000370387"
FT REPEAT 441..480
FT /note="WD 1"
FT REPEAT 482..522
FT /note="WD 2"
FT REPEAT 562..605
FT /note="WD 3"
FT REPEAT 608..646
FT /note="WD 4"
FT REPEAT 649..688
FT /note="WD 5"
FT REPEAT 692..731
FT /note="WD 6"
FT REPEAT 747..777
FT /note="WD 7"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..92
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 88365 MW; D75332DE040CFC7B CRC64;
MSKLKNKKRH LEENEEEQLP IFDKDSGEDG HLDDGDEDPA DLSDSEESVF SGLEDSGSDD
EDDDEDDDED DDDKDGSEEK SSDAEEDKAD DDDGDLKLSA KDDVKPQVDS QNSKEKKKKK
RKGKSVLKDG GEEDVASGRD EALKITSQVD EYDHDTSDEE DIRNTVGNIP MEWYKDYPHI
GYDLDGKKIF KPIRNKDELD EFLDKMENPD YWRTVQDKMT GADIRLSDEQ VDLVHRLQQG
KFGDVNFNEY EPAVDFFSNE VMIHPVTNRP QDKRSFIPSL IEKEKVGKLV HAIKMGWIKP
RRPKETTPQY YDLWAKEDPN SILGRHKMHV PAPKMKLPGH EESYNPPPEY LLSEEERLAW
AAQDPEDRKL SFLPQKFSCL RAVPAFSRFI HERFERCLDL YLCPRQRKMR VNVNPEDLIP
KLPKPKDLQP FPTTQSLVYR GHSSLVRSIS VSPSGQWLVS GSDDCTVRFW EVSTARCLKT
VQVGGAVKGV AWNPNPSICL VAVSYEDSVL LLNPALGDRL LCTATDQLIS SYAEPEEVKE
QPVQWLVSEG EGHEQGHRLV LKHPKAVRQV TWHAKGDYLA CVLPDSSSSV QVLIHQVSKR
RTQNPFRKSK GLVQCVSFHP VRPYFFVATQ RYVRVYNLIK QELTKKLMAN CKWISSMAIH
PGGDNVICGS YDCRLAWFDL DLSTKPYKVL RHHKKALRSV SFHSHYPLLA SGSDDGSVIV
CHGMVYNDLL QNPLIVPVKV LKGHSITHDL GVLDVTFHPT QPWVFSSGAD ATIRLYT
