RUVB2_XENLA
ID RUVB2_XENLA Reviewed; 462 AA.
AC Q9DE27;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=RuvB-like 2;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P83571};
DE AltName: Full=Reptin;
GN Name=ruvbl2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10842076; DOI=10.1016/s0925-4773(00)00305-1;
RA Etard C., Wedlich D., Bauer A., Huber O., Kuehl M.;
RT "Expression of Xenopus homologs of the beta-catenin binding protein
RT pontin52.";
RL Mech. Dev. 94:219-222(2000).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=30561330; DOI=10.7554/elife.38497;
RA Huizar R.L., Lee C., Boulgakov A.A., Horani A., Tu F., Marcotte E.M.,
RA Brody S.L., Wallingford J.B.;
RT "A liquid-like organelle at the root of motile ciliopathy.";
RL Elife 7:0-0(2018).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=33263282; DOI=10.7554/elife.58662;
RA Lee C., Cox R.M., Papoulas O., Horani A., Drew K., Devitt C.C., Brody S.L.,
RA Marcotte E.M., Wallingford J.B.;
RT "Functional partitioning of a liquid-like organelle during assembly of
RT axonemal dyneins.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Has single-stranded DNA-stimulated ATPase and ATP-dependent
CC DNA helicase (5' to 3') activity suggesting a role in nuclear processes
CC such as recombination and transcription (By similarity). Proposed core
CC component of the chromatin remodeling INO80 complex which exhibits
CC DNA- and nucleosome-activated ATPase activity and catalyzes ATP-
CC dependent nucleosome sliding (By similarity). Involved in the
CC endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where
CC it negatively regulates expression of ER stress response genes (By
CC similarity). {ECO:0000250|UniProtKB:P83571,
CC ECO:0000250|UniProtKB:Q9Y230}.
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:P83571};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P83571};
CC -!- SUBUNIT: Forms homohexameric rings (Probable). Can form a dodecamer
CC with ruvbl2 made of two stacked hexameric rings (By similarity). Is a
CC component of the RNA polymerase II holoenzyme complex (By similarity).
CC Component of the chromatin-remodeling Ino80 complex. Component of some
CC MLL1/MLL complex (By similarity). {ECO:0000250|UniProtKB:Q9Y230,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Dynein axonemal particle
CC {ECO:0000269|PubMed:30561330, ECO:0000269|PubMed:33263282}.
CC -!- DEVELOPMENTAL STAGE: Expression decreases until onset of zygotic
CC transcription before increasing again at later stages. Is expressed in
CC neural crest cells, in particular in a subpopulation that give raise to
CC the adrenal medulla.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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DR EMBL; AF218071; AAG44126.1; -; mRNA.
DR AlphaFoldDB; Q9DE27; -.
DR SMR; Q9DE27; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0120293; C:dynein axonemal particle; IDA:UniProtKB.
DR GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0097255; C:R2TP complex; IEA:InterPro.
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; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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..462
FT /note="RuvB-like 2"
FT /id="PRO_0000165647"
FT BINDING 76..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 462 AA; 51188 MW; C837947F8D80D7C9 CRC64;
MATMAATKVP EVRDVTRIER IGAHSHIRGL GLDDALEPRQ VSQGMVGQLA SRRAAGVILE
MIKEGKIAGR AVLIAGQPGT GKTAIAMGMA QALGSDTPFT AIAGSEIFSL EMSKTEALTQ
AFRRSIGVRI KEETEIIEGE VVEVQIDRPA TGTGAKVGKL TLKTTEMETI YDLGTKMIES
LTKEKVQAGD VITIDKATGK ITKLGRAFTR ARDYDAMGSQ TKFVQCPDGE LQKRKEVVHT
VSLHEIDVIN SRTQGFLALF SGDTGEIKSE VREQINAKVA EWREEGKAEI IPGVLFIDEV
HMLDIECFSF LNRALESDMA PVLIMATNRG ITRIRGTNYQ SPHGIPIDLL DRLLIISTSP
YNEKETKQIL KIRCEEEDVD MSEDAYTVLT RIGLETSLRY SMQLITAASL VCRKRKGTEV
QVDDIKRVYS LFLDESRSTQ YMKEYQDAFM FNEMKTDTMD TS
