RUVB1_CAEEL
ID RUVB1_CAEEL Reviewed; 476 AA.
AC O17607;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=RuvB-like 1 {ECO:0000250|UniProtKB:Q9Y265};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P0A812};
DE AltName: Full=Pontin {ECO:0000303|PubMed:25437307};
GN Name=ruvb-1 {ECO:0000312|WormBase:C27H6.2};
GN ORFNames=C27H6.2 {ECO:0000312|WormBase:C27H6.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLU-371.
RX PubMed=17720918; DOI=10.1534/genetics.107.076653;
RA Updike D.L., Mango S.E.;
RT "Genetic suppressors of Caenorhabditis elegans pha-4/FoxA identify the
RT predicted AAA helicase ruvb-1/RuvB.";
RL Genetics 177:819-833(2007).
RN [3] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-371.
RX PubMed=18804378; DOI=10.1016/j.cub.2008.07.097;
RA Sheaffer K.L., Updike D.L., Mango S.E.;
RT "The Target of Rapamycin pathway antagonizes pha-4/FoxA to control
RT development and aging.";
RL Curr. Biol. 18:1355-1364(2008).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25437307; DOI=10.7554/elife.04449;
RA Kato M., Chou T.F., Yu C.Z., DeModena J., Sternberg P.W.;
RT "LINKIN, a new transmembrane protein necessary for cell adhesion.";
RL Elife 3:E04449-E04449(2014).
CC -!- FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP
CC dependent DNA helicase (3' to 5') activity suggesting a role in nuclear
CC processes such as recombination and transcription (By similarity). May
CC participate in several chromatin remodeling complexes that mediate the
CC ATP-dependent exchange of histones and remodel chromatin by shifting
CC nucleosomes (By similarity). Involvement in these complexes is likely
CC required for transcriptional activation of selected genes and DNA
CC repair in response to DNA damage (By similarity). Involved in the Ce-
CC Tor signaling pathway whereby it is required for the accumulation and
CC localization of box C/D snoRNP to nucleoli to regulate ribosomal
CC maturation and thus protein synthesis (PubMed:18804378). Antagonizes
CC the transcriptional activity of transcription factor pha-4, to control
CC postembryonic development and adult longevity (PubMed:17720918,
CC PubMed:18804378). Has a role in pharyngeal development
CC (PubMed:17720918). Has a role in gonadal development (PubMed:25437307).
CC {ECO:0000250|UniProtKB:Q03940, ECO:0000250|UniProtKB:Q9Y265,
CC ECO:0000269|PubMed:17720918, ECO:0000269|PubMed:18804378,
CC ECO:0000269|PubMed:25437307}.
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 Evidence={ECO:0000250|UniProtKB:P0A812};
CC -!- SUBUNIT: Forms homohexameric rings. May form a dodecamer with ruvb-2
CC made of two stacked hexameric rings. {ECO:0000250|UniProtKB:Q9Y265}.
CC -!- INTERACTION:
CC O17607; Q9GZH2: ruvb-2; NbExp=7; IntAct=EBI-316213, EBI-316221;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25437307}. Nucleus
CC {ECO:0000269|PubMed:25437307}.
CC -!- TISSUE SPECIFICITY: Expressed in gonadal cells.
CC {ECO:0000269|PubMed:25437307}.
CC -!- DEVELOPMENTAL STAGE: Expressed in most cells of the early embryo. From
CC the two-cell stage until late embryogenesis, expression is restricted
CC to pharyngeal cells. Detected in two intestinal cells during the larval
CC stage. {ECO:0000269|PubMed:17720918}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in arrest at
CC larval stage L3, with less than 40% forming a mature vulva, lipid
CC accumulation, epidermal granule formation and reduced protein synthesis
CC (PubMed:17720918, PubMed:18804378). There is also gonadal detachment
CC during gonad migration (PubMed:25437307). {ECO:0000269|PubMed:17720918,
CC ECO:0000269|PubMed:18804378, ECO:0000269|PubMed:25437307}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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DR EMBL; BX284605; CAB02793.2; -; Genomic_DNA.
DR RefSeq; NP_505567.2; NM_073166.4.
DR AlphaFoldDB; O17607; -.
DR SMR; O17607; -.
DR DIP; DIP-25966N; -.
DR IntAct; O17607; 4.
DR STRING; 6239.C27H6.2; -.
DR EPD; O17607; -.
DR PaxDb; O17607; -.
DR PeptideAtlas; O17607; -.
DR EnsemblMetazoa; C27H6.2.1; C27H6.2.1; WBGene00007784.
DR GeneID; 179388; -.
DR KEGG; cel:CELE_C27H6.2; -.
DR UCSC; C27H6.2; c. elegans.
DR CTD; 179388; -.
DR WormBase; C27H6.2; CE43279; WBGene00007784; ruvb-1.
DR eggNOG; KOG1942; Eukaryota.
DR GeneTree; ENSGT00940000153556; -.
DR HOGENOM; CLU_028311_1_1_1; -.
DR InParanoid; O17607; -.
DR OMA; VIYVEAN; -.
DR OrthoDB; 752343at2759; -.
DR PhylomeDB; O17607; -.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR PRO; PR:O17607; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00007784; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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:0000492; P:box C/D snoRNP assembly; IMP:WormBase.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0045727; P:positive regulation of translation; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0031929; P:TOR signaling; IMP:WormBase.
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 ATP-binding; Chromatin regulator; Cytoplasm; DNA damage; DNA repair;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..476
FT /note="RuvB-like 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434944"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 371
FT /note="E->K: In px34; results in arrest at larval stage L3,
FT but with continued pharyngeal pumping regardless of arrest,
FT perturbed vulval development, blocked gonadogenesis,
FT increased intestinal lipids, abundant epidermal granules
FT and smaller nucleoli."
FT /evidence="ECO:0000269|PubMed:17720918,
FT ECO:0000269|PubMed:18804378"
SQ SEQUENCE 476 AA; 52512 MW; 7726D025810D2753 CRC64;
MDMEVDEAIS GTSSSRLAPI EEVKPTPKQI KRIAAHSHVK GLGIDTETQE AHYEAAGFVG
QAPARTAASI VVDMIRLKCM AGRAVLIAGP PATGKTAIAL AMSQELGDGV PFVPLVASEV
FSNEVKKTEV LMRSFRRAIG LRVKETKDVY EGEVTELSPV EASDNSGMGK TISHLVLSLK
TAKGSKQLKL DPSIYDSILK QRVEVGDVIY IEANSGIVKR VGRCDVYASE FDLEADEFVP
MPKGDVRKSK DIVQNVSLHD LDIANARPQG RQGDVSNIVS QLMTPKKTEV TDRLRSEINK
VVNEYIESGV AELMPGVLFI DEVHMLDVEC FTYLYRALES PMAPVVVFAT NRGTTTVRGL
GDKAPHGIPP EMLDRLMIIP TMKYNEEDIR KILVHRTEAE NVQFEEKAFD LLSKVGAEKS
LRYALQLIAP ARLCAQTCGR EVIEVEDVDR CTKLFMDRGE SLKKAEEEMR QPKNKK
