RBF_DROME
ID RBF_DROME Reviewed; 845 AA.
AC Q24472; O77272; Q961U8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Retinoblastoma family protein;
GN Name=Rbf; ORFNames=CG7413;
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.
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 GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-816, FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=8675008; DOI=10.1101/gad.10.10.1206;
RA Du W., Vidal M., Xie J.-E., Dyson N.;
RT "RBF, a novel RB-related gene that regulates E2F activity and interacts
RT with cyclin E in Drosophila.";
RL Genes Dev. 10:1206-1218(1996).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=15479636; DOI=10.1016/j.cell.2004.09.034;
RA Korenjak M., Taylor-Harding B., Binne U.K., Satterlee J.S., Stevaux O.,
RA Aasland R., White-Cooper H., Dyson N., Brehm A.;
RT "Native E2F/RBF complexes contain Myb-interacting proteins and repress
RT transcription of developmentally controlled E2F target genes.";
RL Cell 119:181-193(2004).
RN [7]
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=15545624; DOI=10.1101/gad.1255204;
RA Lewis P.W., Beall E.L., Fleischer T.C., Georlette D., Link A.J.,
RA Botchan M.R.;
RT "Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor
RT complex.";
RL Genes Dev. 18:2929-2940(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-356; THR-359; SER-760 AND
RP SER-771, AND IDENTIFICATION BY MASS 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 [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=18250149; DOI=10.1128/mcb.01839-07;
RA Murawska M., Kunert N., van Vugt J., Laengst G., Kremmer E., Logie C.,
RA Brehm A.;
RT "dCHD3, a novel ATP-dependent chromatin remodeler associated with sites of
RT active transcription.";
RL Mol. Cell. Biol. 28:2745-2757(2008).
CC -!- FUNCTION: Functions in cell cycle regulation. Component of the DREAM
CC complex, a multiprotein complex that can both act as a transcription
CC activator or repressor depending on the context. In follicle cells, the
CC complex plays a central role in the site-specific DNA replication at
CC the chorion loci. During development, the complex represses
CC transcription of developmentally controlled E2F target genes.
CC {ECO:0000269|PubMed:15479636, ECO:0000269|PubMed:8675008}.
CC -!- SUBUNIT: Forms a complex with the DRTF1/E2F transcription factor
CC through binding to a C-terminal region of E2F. This binding inhibits
CC the E2F-mediated transactivation activity. Component of the DREAM
CC complex at least composed of Myb, Caf1-55, mip40, mip120, mip130, E2f2,
CC Dp, Rbf, Rbf2, lin-52, HDAC1/Rpd3 and l(3)mbt.
CC {ECO:0000269|PubMed:15479636, ECO:0000269|PubMed:15545624,
CC ECO:0000269|PubMed:8675008}.
CC -!- INTERACTION:
CC Q24472; Q24318: Dp; NbExp=3; IntAct=EBI-145741, EBI-530830;
CC Q24472; Q27368: E2f1; NbExp=3; IntAct=EBI-145741, EBI-108384;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8675008}.
CC -!- DEVELOPMENTAL STAGE: Expressed at constant levels throughout embryo and
CC larval development (at protein level). {ECO:0000269|PubMed:18250149}.
CC -!- PTM: Phosphorylation by cyclin E-dependent kinases appears to
CC negatively regulate RBF activity. {ECO:0000269|PubMed:18327897}.
CC -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK77281.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA65661.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014298; AAF45551.1; -; Genomic_DNA.
DR EMBL; AL031583; CAA20903.1; -; Genomic_DNA.
DR EMBL; AY047549; AAK77281.1; ALT_INIT; mRNA.
DR EMBL; AY089532; AAL90270.1; -; mRNA.
DR EMBL; X96975; CAA65661.1; ALT_FRAME; mRNA.
DR PIR; T13480; T13480.
DR RefSeq; NP_525036.2; NM_080297.3.
DR AlphaFoldDB; Q24472; -.
DR SMR; Q24472; -.
DR BioGRID; 57595; 69.
DR DIP; DIP-34025N; -.
DR IntAct; Q24472; 15.
DR STRING; 7227.FBpp0070141; -.
DR iPTMnet; Q24472; -.
DR PaxDb; Q24472; -.
DR PRIDE; Q24472; -.
DR DNASU; 31027; -.
DR EnsemblMetazoa; FBtr0070146; FBpp0070141; FBgn0015799.
DR GeneID; 31027; -.
DR KEGG; dme:Dmel_CG7413; -.
DR CTD; 31027; -.
DR FlyBase; FBgn0015799; Rbf.
DR VEuPathDB; VectorBase:FBgn0015799; -.
DR eggNOG; KOG1010; Eukaryota.
DR GeneTree; ENSGT00950000183202; -.
DR HOGENOM; CLU_008943_1_0_1; -.
DR InParanoid; Q24472; -.
DR OMA; AILCELH; -.
DR OrthoDB; 113612at2759; -.
DR PhylomeDB; Q24472; -.
DR Reactome; R-DME-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-DME-1538133; G0 and Early G1.
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-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-DME-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DME-69200; Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
DR Reactome; R-DME-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-DME-69231; Cyclin D associated events in G1.
DR Reactome; R-DME-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR BioGRID-ORCS; 31027; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 31027; -.
DR PRO; PR:Q24472; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0015799; Expressed in cleaving embryo and 74 other tissues.
DR Genevisible; Q24472; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0031523; C:Myb complex; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0035189; C:Rb-E2F complex; IDA:FlyBase.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:FlyBase.
DR GO; GO:0007307; P:eggshell chorion gene amplification; TAS:FlyBase.
DR GO; GO:0007113; P:endomitotic cell cycle; TAS:FlyBase.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:FlyBase.
DR GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; IMP:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0008156; P:negative regulation of DNA replication; IMP:FlyBase.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0010941; P:regulation of cell death; IMP:FlyBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0008361; P:regulation of cell size; IMP:FlyBase.
DR GO; GO:0051983; P:regulation of chromosome segregation; IMP:BHF-UCL.
DR GO; GO:0071922; P:regulation of cohesin loading; IMP:BHF-UCL.
DR GO; GO:0051101; P:regulation of DNA binding; IDA:FlyBase.
DR GO; GO:1900117; P:regulation of execution phase of apoptosis; IMP:FlyBase.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR002720; RB_A.
DR InterPro; IPR002719; RB_B.
DR InterPro; IPR028309; RB_fam.
DR InterPro; IPR024599; RB_N.
DR PANTHER; PTHR13742; PTHR13742; 2.
DR Pfam; PF11934; DUF3452; 1.
DR Pfam; PF01858; RB_A; 1.
DR Pfam; PF01857; RB_B; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SMART; SM01367; DUF3452; 1.
DR SMART; SM01368; RB_A; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW Activator; Cell cycle; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..845
FT /note="Retinoblastoma family protein"
FT /id="PRO_0000167844"
FT REGION 376..706
FT /note="Pocket"
FT REGION 376..560
FT /note="Domain A"
FT REGION 580..706
FT /note="Domain B"
FT REGION 720..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 359
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 845 AA; 96826 MW; C7AF38592C14FAD2 CRC64;
MSEPDPQELG AEVVSGLVAT SDDRLEMINA EYTNLCRDLN MDRQTELQGY ETYLEVSQRC
SMEGTASHWM CCAIYTACRR TSTPTVTGQN AVVKGNCVSL NNLLRCCKMS IYEFKTKIKQ
WCDMANLPQE FVNEIEDLDR KFSITFMLHK RFRIIMDMIF SCPPNEKKHS KYISLHGNHA
HGKCSYIKLD DICWRLFLCA KNQKPSNTVD LVTSYNLMIC CIDLIYNNVL AEKRTDLINP
KFEGLPSNWT ELDFRHNPHC ILSNFCDMTE EAKAMKATTF RQIMSSFFQA STIYGNKDTM
LGLLANENFE RNLKSLNISY EQYVLSVGEF DERILSAYDA GEHTALNDQS LRPPVTPLTR
KQDLPAQPAM AGDKFEPVRN ATNNVKQLSA FGRITEPTDF VKQAGEEVIA KLLSIIEEIE
QKFLAKYPST EAKSRFQLAK SFFFYLLDQI LQAEIRNKPD IDLKRLLVQK VSLVIFNITL
MACCVELVLE AYKTELKFPW VLDCFSISAF EFQKIIEIVV RHGSHEGCLN RSLIKHLNSI
EETCLERLAW ARNSTVWEMI ASAQLPLPTW LMVNLDRAAG PLQIFLRKVY LLGWLRIQKL
CSELSLCEKT PESIWHIFEH SITHETELMK DRHLDQNIMC AIYIYIRVKR MEDPKFSDIM
RAYRNQPQAV NSVYREVFID INEDGEPKVK DIIHFYNHTY VPLMRQFVID YLNVTPDVSG
RASDLQLSPH PKERAAQPKK VTQSHSLFVS QMSKNEIQQS PNQMVYSFCR SPAKDLQAMN
EKVRGGKRML SFGDEPGLGT MAETKRSKIS QVKAVMDDPE LQSAEQQTAV TTEGCVGGEG
GEHET
