RUVB2_CAEEL
ID RUVB2_CAEEL Reviewed; 448 AA.
AC Q9GZH2;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=RuvB-like 2 {ECO:0000250|UniProtKB:Q9Y230};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P0A812};
DE AltName: Full=Reptin {ECO:0000303|PubMed:25437307};
GN Name=ruvb-2 {ECO:0000312|WormBase:T22D1.10};
GN ORFNames=T22D1.10 {ECO:0000312|WormBase:T22D1.10};
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, 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).
RN [3] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25652260; DOI=10.15252/embr.201439123;
RA Marza E., Taouji S., Barroso K., Raymond A.A., Guignard L., Bonneu M.,
RA Pallares-Lupon N., Dupuy J.W., Fernandez-Zapico M.E., Rosenbaum J.,
RA Palladino F., Dupuy D., Chevet E.;
RT "Genome-wide screen identifies a novel p97/CDC-48-dependent pathway
RT regulating ER-stress-induced gene transcription.";
RL EMBO Rep. 16:332-340(2015).
CC -!- FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-
CC dependent DNA helicase (5' to 3') 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). Has a role in gonadal
CC development (PubMed:25437307). Involved in the endoplasmic reticulum
CC (ER)-associated degradation (ERAD) pathway where it negatively
CC regulates expression of ER stress response genes (PubMed:25652260).
CC Specifically, negatively controls the expression of ER homeostasis
CC regulator ckb-2 in a cdc-48.1/2-dependent manner (PubMed:25652260).
CC {ECO:0000250|UniProtKB:Q12464, ECO:0000250|UniProtKB:Q9Y230,
CC ECO:0000269|PubMed:25437307, ECO:0000269|PubMed:25652260}.
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-1
CC made of two stacked hexameric rings. {ECO:0000250|UniProtKB:Q9Y230}.
CC -!- INTERACTION:
CC Q9GZH2; O17607: ruvb-1; NbExp=7; IntAct=EBI-316221, EBI-316213;
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 -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in gonadal
CC detachment during gonad migration (PubMed:25437307). RNAi-mediated
CC knockdown upon tunicamycin-induced ER stress in a cdc-48.1 and/or cdc-
CC 48.2 mutant background (insensitive to tunicamycin-induced ER stress)
CC restores the expression of ER homeostasis regulator, ckb-2
CC (PubMed:25652260). {ECO:0000269|PubMed:25437307,
CC ECO:0000269|PubMed:25652260}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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DR EMBL; BX284604; CCD62026.1; -; Genomic_DNA.
DR PIR; T32710; T32710.
DR RefSeq; NP_501067.1; NM_068666.3.
DR AlphaFoldDB; Q9GZH2; -.
DR SMR; Q9GZH2; -.
DR IntAct; Q9GZH2; 2.
DR STRING; 6239.T22D1.10; -.
DR EPD; Q9GZH2; -.
DR PaxDb; Q9GZH2; -.
DR PeptideAtlas; Q9GZH2; -.
DR EnsemblMetazoa; T22D1.10.1; T22D1.10.1; WBGene00020687.
DR GeneID; 177458; -.
DR KEGG; cel:CELE_T22D1.10; -.
DR UCSC; T22D1.10; c. elegans.
DR CTD; 177458; -.
DR WormBase; T22D1.10; CE17254; WBGene00020687; ruvb-2.
DR eggNOG; KOG2680; Eukaryota.
DR GeneTree; ENSGT00940000153556; -.
DR HOGENOM; CLU_028311_4_0_1; -.
DR InParanoid; Q9GZH2; -.
DR OMA; YDMGAKM; -.
DR OrthoDB; 752343at2759; -.
DR PhylomeDB; Q9GZH2; -.
DR PRO; PR:Q9GZH2; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00020687; 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; 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:0016573; P:histone acetylation; IBA:GO_Central.
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; IPR012340; NA-bd_OB-fold.
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; SSF50249; SSF50249; 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..448
FT /note="RuvB-like 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434945"
FT BINDING 73..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
SQ SEQUENCE 448 AA; 49299 MW; C3EA01148E4DA0BA CRC64;
MATLDGINVK DIVKVERTSV HSHITGLGLN DRLEAEYVSG GMVGQVAARQ AAGLIVKMIQ
EGKIAGRALL VTGEPGAGKT AIAIAISKEL GEDTPFVSIV ASEIYSNEIN KTEALTQAFR
RALGIQIKEE TEVLEGEVIS LEVDRSANGM GPKVGKLTMR TTDMETIYDL GSKMVDACLK
EKVMPGDVIQ VDKASGRVTR LGRSFNRSHD YDAMGPKVKL VQCPDGEIQK RRETVHTVCL
HDIDVINSRT QGYVALFSGD TGEIKAEVRD QINKKVLEWR EEGKAKFVPG VLFIDEAHML
DIECFSFLNR AIEGELSPLI IMATNRLIEK VRGTDVESAH GIPSDFLDRM LIINAIPYTK
EDTAKILSIR CDEEGVKLQP TALDLLVKLQ EATSLRYCIH LIAASEVIRI RSKAEIVTTD
HIGSAYRLFF DTKRSEKILT EESAGFLQ
