RUVB1_DROME
ID RUVB1_DROME Reviewed; 456 AA.
AC Q9VH07; Q9NH53; Q9VH06;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=RuvB-like helicase 1;
DE EC=3.6.4.12;
DE AltName: Full=Dpontin;
DE Short=Dpon;
DE AltName: Full=Pontin;
GN Name=pont {ECO:0000312|EMBL:AAF54514.1, ECO:0000312|FlyBase:FBgn0040078};
GN ORFNames=CG4003;
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:AAF43411.1}
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:AAF54514.1}
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:AAF54514.1}
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:AAL28643.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28643.1};
RC TISSUE=Embryo {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 REPT.
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 rept.
CC {ECO:0000250, ECO:0000269|PubMed:16087886,
CC ECO:0000269|PubMed:16618800}.
CC -!- INTERACTION:
CC Q9VH07; Q9W4S7: Myc; NbExp=4; IntAct=EBI-234957, EBI-120162;
CC Q9VH07; Q9V3K3: rept; NbExp=5; IntAct=EBI-234957, EBI-192924;
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; AF233278; AAF43411.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54514.1; -; Genomic_DNA.
DR EMBL; AY061095; AAL28643.1; -; mRNA.
DR RefSeq; NP_652608.1; NM_144351.4.
DR AlphaFoldDB; Q9VH07; -.
DR SMR; Q9VH07; -.
DR BioGRID; 72727; 44.
DR IntAct; Q9VH07; 14.
DR MINT; Q9VH07; -.
DR STRING; 7227.FBpp0081704; -.
DR PaxDb; Q9VH07; -.
DR PRIDE; Q9VH07; -.
DR EnsemblMetazoa; FBtr0082226; FBpp0081704; FBgn0040078.
DR GeneID; 53439; -.
DR KEGG; dme:Dmel_CG4003; -.
DR UCSC; CG4003-RA; d. melanogaster.
DR CTD; 53439; -.
DR FlyBase; FBgn0040078; pont.
DR VEuPathDB; VectorBase:FBgn0040078; -.
DR eggNOG; KOG1942; Eukaryota.
DR GeneTree; ENSGT00940000153556; -.
DR HOGENOM; CLU_028311_1_1_1; -.
DR InParanoid; Q9VH07; -.
DR OMA; VIYVEAN; -.
DR OrthoDB; 752343at2759; -.
DR PhylomeDB; Q9VH07; -.
DR Reactome; R-DME-5689603; UCH proteinases.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; Q9VH07; -.
DR BioGRID-ORCS; 53439; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 53439; -.
DR PRO; PR:Q9VH07; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0040078; Expressed in gastrula and 53 other tissues.
DR Genevisible; Q9VH07; DM.
DR GO; GO:0035060; C:brahma complex; IDA: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:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IDA:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:FlyBase.
DR GO; GO:0060548; P:negative regulation of cell death; IGI:FlyBase.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IMP:FlyBase.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IGI:FlyBase.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; 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; IPR037938; RUVBL1.
DR InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR InterPro; IPR010339; TIP49_P-loop.
DR PANTHER; PTHR11093; PTHR11093; 1.
DR PANTHER; PTHR11093:SF6; PTHR11093:SF6; 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 Activator; ATP-binding; Cell cycle; Cell division; Chromatin regulator;
KW DNA damage; DNA recombination; DNA repair; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..456
FT /note="RuvB-like helicase 1"
FT /id="PRO_0000306320"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y230"
FT CONFLICT 71
FT /note="P -> A (in Ref. 1; AAF43411)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="E -> K (in Ref. 1; AAF43411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 50242 MW; 91683B868B18E777 CRC64;
MKIEEVKSTV RTQRIAAHSH VKGLGLDEVG AAVHSAAGLV GQKAAREAAG IVVDLIKSKK
MAGRALLLAG PPGTGKTAIA LAIAQELGNK VPFCPMVGSE VFSNEIKKTE VLMENFRRSI
GLRIRETKEV YEGEVTELTP VETENPMGGY GKTISNVVIG LKTAKGTKQL KLDPSIFDAL
QKEKVEVGDV IYIEANSGAV KRQGRSDTFA TEFDLETEEY VPLPKGDVHK KKEVIQDVTL
HDLDVANARP QGGQDVLSMM GQLMKPKKTE ITDKLRMEIN KVVNKYIDQG IAELVPGVLF
IDEIHMLDLE TFTYLHKSLE SPIAPIVIFA TNRGRCVIRG TTDIVSPHGI PLDLLDRLLI
IRTLLYSTAD MEQIIKLRAQ TEGLQLEENA FTRLSEIGTS STLRYAVQLL TPAHQMCKVN
GRNQISKDDI EDVHSLFLDA KRSSKHLSEK NNKFML
