RUVB2_DROME
ID RUVB2_DROME Reviewed; 481 AA.
AC Q9V3K3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=RuvB-like helicase 2;
DE EC=3.6.4.12;
DE AltName: Full=Dreptin;
DE Short=Drep;
DE AltName: Full=Reptin;
GN Name=rept {ECO:0000312|EMBL:AAF49182.1, ECO:0000312|FlyBase:FBgn0040075};
GN ORFNames=CG9750;
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] {ECO:0000305, ECO:0000312|EMBL:AAF43412.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11080158; DOI=10.1093/emboj/19.22.6121;
RA Bauer A., Chauvet S., Huber O., Usseglio F., Rothbaecher U., Aragnol D.,
RA Kemler R., Pradel J.;
RT "Pontin52 and reptin52 function as antagonistic regulators of beta-catenin
RT signalling activity.";
RL EMBO J. 19:6121-6130(2000).
RN [2] {ECO:0000312|EMBL:AAF49182.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF49182.1}
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] {ECO:0000312|EMBL:AAL28500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28500.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569}, and
RC Ovary {ECO:0000269|PubMed:12537569};
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] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH MYC AND PONT.
RX PubMed=16087886; DOI=10.1073/pnas.0408945102;
RA Bellosta P., Hulf T., Balla Diop S., Usseglio F., Pradel J., Aragnol D.,
RA Gallant P.;
RT "Myc interacts genetically with Tip48/Reptin and Tip49/Pontin to control
RT growth and proliferation during Drosophila development.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11799-11804(2005).
RN [6] {ECO:0000305}
RP IDENTIFICATION IN THE INO80 COMPLEX.
RC TISSUE=Embryo {ECO:0000269|PubMed:16618800};
RX PubMed=16618800; DOI=10.1101/gad.377406;
RA Klymenko T., Papp B., Fischle W., Koecher T., Schelder M., Fritsch C.,
RA Wild B., Wilm M., Mueller J.;
RT "A Polycomb group protein complex with sequence-specific DNA-binding and
RT selective methyl-lysine-binding activities.";
RL Genes Dev. 20:1110-1122(2006).
CC -!- FUNCTION: Acts as a transcriptional coactivator in Wg signaling caused
CC by altered arm signaling. Pont and rept interfere antagonistically with
CC nuclear arm signaling function, and are required to enhance or reduce
CC arm activity, respectively. Also an essential cofactor for the normal
CC function of Myc; required for cellular proliferation and growth.
CC {ECO:0000269|PubMed:11080158, ECO:0000269|PubMed:16087886}.
CC -!- FUNCTION: Proposed core component of the chromatin remodeling Ino80
CC complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Forms homohexameric rings. May form a dodecamer with rept made
CC of two stacked hexameric rings (By similarity). Component of the
CC chromatin remodeling Ino80 complex. Interacts with Myc and pont.
CC {ECO:0000250, ECO:0000269|PubMed:16087886,
CC ECO:0000269|PubMed:16618800}.
CC -!- INTERACTION:
CC Q9V3K3; Q9W4S7: Myc; NbExp=4; IntAct=EBI-192924, EBI-120162;
CC Q9V3K3; Q9VH07: pont; NbExp=5; IntAct=EBI-192924, EBI-234957;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11080158}.
CC -!- TISSUE SPECIFICITY: Higher expression occurs in primordia of mesoderm,
CC anterior and posterior midgut and cephalic furrow early in
CC gastrulation, as well as in endoderm and mesoderm lineages during germ
CC band extension. Later in development expression is only maintained in
CC endoderm cells. Expressed in thoracic and abdominal segment neural
CC precursors of all embryonic chordotonal organs.
CC {ECO:0000269|PubMed:11080158}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:11080158}.
CC -!- DISRUPTION PHENOTYPE: Death at first larval instar.
CC {ECO:0000269|PubMed:11080158}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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DR EMBL; AF233279; AAF43412.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49182.1; -; Genomic_DNA.
DR EMBL; AY060952; AAL28500.1; -; mRNA.
DR EMBL; AY061155; AAL28703.1; -; mRNA.
DR RefSeq; NP_001262040.1; NM_001275111.1.
DR RefSeq; NP_001287113.1; NM_001300184.1.
DR RefSeq; NP_524156.1; NM_079432.3.
DR AlphaFoldDB; Q9V3K3; -.
DR SMR; Q9V3K3; -.
DR BioGRID; 65368; 34.
DR IntAct; Q9V3K3; 9.
DR STRING; 7227.FBpp0074756; -.
DR PaxDb; Q9V3K3; -.
DR PRIDE; Q9V3K3; -.
DR EnsemblMetazoa; FBtr0074988; FBpp0074756; FBgn0040075.
DR EnsemblMetazoa; FBtr0331852; FBpp0304236; FBgn0040075.
DR EnsemblMetazoa; FBtr0344993; FBpp0311247; FBgn0040075.
DR GeneID; 40092; -.
DR KEGG; dme:Dmel_CG9750; -.
DR UCSC; CG9750-RA; d. melanogaster.
DR CTD; 40092; -.
DR FlyBase; FBgn0040075; rept.
DR VEuPathDB; VectorBase:FBgn0040075; -.
DR eggNOG; KOG2680; Eukaryota.
DR GeneTree; ENSGT00940000153556; -.
DR HOGENOM; CLU_028311_4_0_1; -.
DR InParanoid; Q9V3K3; -.
DR OMA; YDMGAKM; -.
DR OrthoDB; 752343at2759; -.
DR PhylomeDB; Q9V3K3; -.
DR SignaLink; Q9V3K3; -.
DR BioGRID-ORCS; 40092; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 40092; -.
DR PRO; PR:Q9V3K3; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0040075; Expressed in wing disc and 60 other tissues.
DR ExpressionAtlas; Q9V3K3; baseline and differential.
DR Genevisible; Q9V3K3; DM.
DR GO; GO:0000123; C:histone acetyltransferase complex; IPI:FlyBase.
DR GO; GO:0031011; C:Ino80 complex; IDA:FlyBase.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0097255; C:R2TP complex; IBA:GO_Central.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0035072; P:ecdysone-mediated induction of salivary gland cell autophagic cell death; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IDA:UniProtKB.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; IMP:FlyBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.40.50.360; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR027238; RuvB-like.
DR InterPro; IPR041048; RuvB-like_C.
DR InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR InterPro; IPR037942; RUVBL2.
DR InterPro; IPR010339; TIP49_P-loop.
DR PANTHER; PTHR11093; PTHR11093; 1.
DR PANTHER; PTHR11093:SF2; PTHR11093:SF2; 1.
DR Pfam; PF06068; TIP49; 1.
DR Pfam; PF17856; TIP49_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; DNA damage; DNA repair; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..481
FT /note="RuvB-like helicase 2"
FT /id="PRO_0000306323"
FT REGION 453..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y230"
SQ SEQUENCE 481 AA; 53541 MW; AF41DFCBE19C09C3 CRC64;
MAETEKIEVR DVTRIERIGA HSHIRGLGLD DVLEARLVSQ GMVGQKDARR AAGVVVQMVR
EGKIAGRCIL LAGEPSTGKT AIAVGMAQAL GTETPFTSMS GSEIYSLEMS KTEALSQALR
KSIGVRIKEE TEIIEGEVVE IQIERPASGT GQKVGKVTLK TTEMETNYDL GNKIIECFMK
EKIQAGDVIT IDKASGKVNK LGRSFTRARD YDATGAQTRF VQCPEGELQK RKEVVHTVTL
HEIDVINSRT HGFLALFSGD TGEIKQEVRD QINNKVLEWR EEGKAEINPG VLFIDEVHML
DIECFSFLNR ALESDMAPVV VMATNRGITR IRGTNYRSPH GIPIDLLDRM IIIRTVPYSE
KEVKEILKIR CEEEDCIMHP DALTILTRIA TDTSLRYAIQ LITTANLVCR RRKATEVNTE
DVKKVYSLFL DENRSSKILK EYQDDYMFSE ITEEVERDPA AGGGAKRRVE GGGGDAQPME
H
