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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
 
 
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