RUVB2_DANRE
ID RUVB2_DANRE Reviewed; 463 AA.
AC P83571;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=RuvB-like 2;
DE EC=3.6.4.12 {ECO:0000269|PubMed:12464178};
DE AltName: Full=Reptin;
DE AltName: Full=zReptin;
GN Name=ruvbl2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:AAL18005.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION
RP PHENOTYPE, MUTAGENESIS OF GLY-190, AND CATALYTIC ACTIVITY.
RX PubMed=12464178; DOI=10.1016/s0092-8674(02)01112-1;
RA Rottbauer W., Saurin A.J., Lickert H., Shen X., Burns C.G., Wo Z.G.,
RA Kemler R., Kingston R., Wu C., Fishman M.;
RT "Reptin and pontin antagonistically regulate heart growth in zebrafish
RT embryos.";
RL Cell 111:661-672(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has double-stranded DNA-stimulated ATPase activity
CC (PubMed:12464178). Has ATP-dependent DNA helicase (5' to 3') activity
CC suggesting a role in nuclear processes such as recombination and
CC transcription (By similarity). Represses gene activation mediated by
CC beta-catenin (PubMed:12464178). Proposed core component of the
CC chromatin remodeling Ino80 complex which exhibits DNA- and nucleosome-
CC activated ATPase activity and catalyzes ATP-dependent nucleosome
CC sliding (By similarity). Involved in the endoplasmic reticulum (ER)-
CC associated degradation (ERAD) pathway where it negatively regulates
CC expression of ER stress response genes (By similarity). May act as a
CC regulator of embryonic heart growth (PubMed:12464178).
CC {ECO:0000250|UniProtKB:Q9Y230, ECO:0000269|PubMed:12464178}.
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:0000269|PubMed:12464178};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000305|PubMed:12464178};
CC -!- SUBUNIT: Forms homohexameric rings (Probable). Can form a dodecamer
CC with ruvbl1 made of two stacked hexameric rings (By similarity).
CC Component of the chromatin-remodeling Ino80 complex (By similarity).
CC Component of some MLL1/MLL complex (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y230, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:Q9DE27}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in the embryo. After 60 hours
CC post-fertilization there is increased expression in heart, liver,
CC branchial arches, exocrine pancreas and intestine.
CC {ECO:0000269|PubMed:12464178}.
CC -!- DISRUPTION PHENOTYPE: Fishes display embryonic cardiac hyperplasia with
CC increased cell number and size by 72 hours post-fertilization. Gut and
CC gut-derived organs are incapable of growth and differentiation after
CC this time. The mutation enhances ATPase activity, rendering it DNA-
CC independent and causes aggregation of the protein into large complexes.
CC {ECO:0000269|PubMed:12464178}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000250|UniProtKB:Q9Y230}.
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DR EMBL; AY057075; AAL18005.1; -; mRNA.
DR EMBL; BC058871; AAH58871.1; -; mRNA.
DR RefSeq; NP_777285.1; NM_174860.2.
DR AlphaFoldDB; P83571; -.
DR SMR; P83571; -.
DR STRING; 7955.ENSDARP00000072482; -.
DR PaxDb; P83571; -.
DR PRIDE; P83571; -.
DR Ensembl; ENSDART00000078018; ENSDARP00000072482; ENSDARG00000055639.
DR GeneID; 317678; -.
DR KEGG; dre:317678; -.
DR CTD; 10856; -.
DR ZFIN; ZDB-GENE-030109-1; ruvbl2.
DR eggNOG; KOG2680; Eukaryota.
DR GeneTree; ENSGT00940000153556; -.
DR HOGENOM; CLU_028311_4_0_1; -.
DR InParanoid; P83571; -.
DR OMA; YDMGAKM; -.
DR OrthoDB; 752343at2759; -.
DR PhylomeDB; P83571; -.
DR TreeFam; TF300469; -.
DR PRO; PR:P83571; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000055639; Expressed in testis and 23 other tissues.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0097255; C:R2TP complex; IBA:GO_Central.
DR GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0070286; P:axonemal dynein complex assembly; IMP:ZFIN.
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:0048565; P:digestive tract development; IMP:ZFIN.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0044458; P:motile cilium assembly; IMP:ZFIN.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0060420; P:regulation of heart growth; IMP:ZFIN.
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; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..463
FT /note="RuvB-like 2"
FT /id="PRO_0000165646"
FT BINDING 77..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 190
FT /note="G->GFCR: In LIK mutant; causes embryonic cardiac
FT hyperplasia."
FT /evidence="ECO:0000269|PubMed:12464178"
SQ SEQUENCE 463 AA; 51251 MW; 517DE09F228AB61D CRC64;
MAAQVATTKV PEVRDITRIE RIGAHSHIRG LGLDDALEPR QVSQGMVGQL ASRRAAGLIL
EMIKDGQIAG RAVLIAGQPG TGKTAIAMGI AQSLGPDTPF TALAGSEIFS LEMSKTEALS
QAFRKAIGVR IKEETEIIEG EVVEIQIDRP ATGTGAKVGK LTLKTTEMET IYDLGTKMIE
SLSKERVQAG DVITIDKATG KISKLGRSFT RARDYDAMGA QTQFVQCPEG ELQKRKEVVH
TVSLHEIDVI NSRTQGFLAL FSGDTGEIKS EVREQINAKV SEWREEGKAE IIPGVLFIDE
VHMLDIECFS FLNRALESDL SPVLIMATNR GITRIRGTNY QSPHGIPIDM LDRLLIIATT
PYTEKETRQI LKIRCEEEDV ELSEEAHTVL TRIGQETSLR YAIQLISTAG LVCRKRRGTE
VQVEDIKRVY SLFLDEARSS QYMKEYQDSF LFNETQTSQM DTS
