GenomeNet

Database: UniProt
Entry: Q8RXS6
LinkDB: Q8RXS6
Original site: Q8RXS6 
ID   INO80_ARATH             Reviewed;        1507 AA.
AC   Q8RXS6; Q9M2L7;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   16-OCT-2019, entry version 112.
DE   RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000305};
DE            Short=AtINO80;
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:Q9ULG1};
DE   AltName: Full=DNA helicase-related INO80 complex homolog 1 {ECO:0000305};
GN   Name=INO80; OrderedLocusNames=At3g57300; ORFNames=F28O9.150;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15525519; DOI=10.1016/j.molcel.2004.09.034;
RA   Fritsch O., Benvenuto G., Bowler C., Molinier J., Hohn B.;
RT   "The INO80 protein controls homologous recombination in Arabidopsis
RT   thaliana.";
RL   Mol. Cell 16:479-485(2004).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA   Xu R., Zhang S., Huang J., Zheng C.;
RT   "Genome-wide comparative in silico analysis of the RNA helicase gene
RT   family in Zea mays and Glycine max: a comparison with Arabidopsis and
RT   Oryza sativa.";
RL   PLoS ONE 8:E78982-E78982(2013).
CC   -!- FUNCTION: ATPase component of the chromatin remodeling INO80
CC       complex which is involved in transcriptional regulation, DNA
CC       replication and DNA repair (By similarity). Binds DNA (By
CC       similarity). As part of the INO80 complex, remodels chromatin by
CC       shifting nucleosomes (By similarity). Positive regulator of
CC       homologous recombination, but not an essential component of
CC       homologous recombination (PubMed:15525519). Not involved in the
CC       illegitimate repair pathway (PubMed:15525519).
CC       {ECO:0000250|UniProtKB:Q9ULG1, ECO:0000269|PubMed:15525519}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q9ULG1};
CC   -!- SUBUNIT: Component of the INO80 chromatin-remodeling complex.
CC       {ECO:0000255|PROSITE-ProRule:PRU00746}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00746}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q8RXS6-1; Sequence=Displayed;
CC   -!- INDUCTION: Not induced by methyl methanesulfonate (MMS) treatment.
CC       {ECO:0000269|PubMed:15525519}.
CC   -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC       {ECO:0000250|UniProtKB:Q9ULG1}.
CC   -!- DISRUPTION PHENOTYPE: Decreased homologous recombination
CC       frequency, but unchanged sensitivity to genotoxic agents and
CC       efficiency of T-DNA integration. {ECO:0000269|PubMed:15525519}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB68136.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL137080; CAB68136.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE79637.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM65731.1; -; Genomic_DNA.
DR   EMBL; AY080695; AAL86315.1; -; mRNA.
DR   PIR; T45808; T45808.
DR   RefSeq; NP_001319776.1; NM_001339850.1. [Q8RXS6-1]
DR   RefSeq; NP_191289.2; NM_115590.4. [Q8RXS6-1]
DR   BioGrid; 10213; 2.
DR   STRING; 3702.AT3G57300.2; -.
DR   iPTMnet; Q8RXS6; -.
DR   PaxDb; Q8RXS6; -.
DR   PRIDE; Q8RXS6; -.
DR   EnsemblPlants; AT3G57300.1; AT3G57300.1; AT3G57300. [Q8RXS6-1]
DR   EnsemblPlants; AT3G57300.4; AT3G57300.4; AT3G57300. [Q8RXS6-1]
DR   GeneID; 824897; -.
DR   Gramene; AT3G57300.1; AT3G57300.1; AT3G57300. [Q8RXS6-1]
DR   Gramene; AT3G57300.4; AT3G57300.4; AT3G57300. [Q8RXS6-1]
DR   KEGG; ath:AT3G57300; -.
DR   Araport; AT3G57300; -.
DR   eggNOG; KOG0388; Eukaryota.
DR   eggNOG; ENOG410XP0A; LUCA.
DR   HOGENOM; HOG000240053; -.
DR   InParanoid; Q8RXS6; -.
DR   KO; K11665; -.
DR   OrthoDB; 188211at2759; -.
DR   PhylomeDB; Q8RXS6; -.
DR   PRO; PR:Q8RXS6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8RXS6; baseline and differential.
DR   Genevisible; Q8RXS6; AT.
DR   GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0042766; P:nucleosome mobilization; IBA:GO_Central.
DR   GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR020838; DBINO.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR031047; Ino80.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45685:SF2; PTHR45685:SF2; 1.
DR   Pfam; PF13892; DBINO; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51413; DBINO; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   Activator; Alternative splicing; ATP-binding; Complete proteome;
KW   DNA damage; DNA repair; DNA-binding; Hydrolase; Nucleotide-binding;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN         1   1507       Chromatin-remodeling ATPase INO80.
FT                                /FTId=PRO_0000375865.
FT   DOMAIN      350    475       DBINO. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00746}.
FT   DOMAIN      598    769       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1210   1360       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     611    618       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COMPBIAS     82     85       Poly-Asp.
SQ   SEQUENCE   1507 AA;  172172 MW;  B64F7CCF96452E6B CRC64;
     MDPSRRPPKD SPYANLFDLE PLMKFRIPKP EDEVDYYGSS SQDESRSTQG GVVANYSNGS
     KSRMNASSKK RKRWTEAEDA EDDDDLYNQH VTEEHYRSML GEHVQKFKNR SKETQGNPPH
     LMGFPVLKSN VGSYRGRKPG NDYHGRFYDM DNSPNFAADV TPHRRGSYHD RDITPKIAYE
     PSYLDIGDGV IYKIPPSYDK LVASLNLPSF SDIHVEEFYL KGTLDLRSLA ELMASDKRSG
     VRSRNGMGEP RPQYESLQAR MKALSPSNST PNFSLKVSEA AMNSAIPEGS AGSTARTILS
     EGGVLQVHYV KILEKGDTYE IVKRSLPKKL KAKNDPAVIE KTERDKIRKA WINIVRRDIA
     KHHRIFTTFH RKLSIDAKRF ADGCQREVRM KVGRSYKIPR TAPIRTRKIS RDMLLFWKRY
     DKQMAEERKK QEKEAAEAFK REQEQRESKR QQQRLNFLIK QTELYSHFMQ NKTDSNPSEA
     LPIGDENPID EVLPETSAAE PSEVEDPEEA ELKEKVLRAA QDAVSKQKQI TDAFDTEYMK
     LRQTSEMEGP LNDISVSGSS NIDLHNPSTM PVTSTVQTPE LFKGTLKEYQ MKGLQWLVNC
     YEQGLNGILA DEMGLGKTIQ AMAFLAHLAE EKNIWGPFLV VAPASVLNNW ADEISRFCPD
     LKTLPYWGGL QERTILRKNI NPKRMYRRDA GFHILITSYQ LLVTDEKYFR RVKWQYMVLD
     EAQAIKSSSS IRWKTLLSFN CRNRLLLTGT PIQNNMAELW ALLHFIMPML FDNHDQFNEW
     FSKGIENHAE HGGTLNEHQL NRLHAILKPF MLRRVKKDVV SELTTKTEVT VHCKLSSRQQ
     AFYQAIKNKI SLAELFDSNR GQFTDKKVLN LMNIVIQLRK VCNHPELFER NEGSSYLYFG
     VTSNSLLPHP FGELEDVHYS GGQNPIIYKI PKLLHQEVLQ NSETFCSSVG RGISRESFLK
     HFNIYSPEYI LKSIFPSDSG VDQVVSGSGA FGFSRLMDLS PSEVGYLALC SVAERLLFSI
     LRWERQFLDE LVNSLMESKD GDLSDNNIER VKTKAVTRML LMPSKVETNF QKRRLSTGPT
     RPSFEALVIS HQDRFLSSIK LLHSAYTYIP KARAPPVSIH CSDRNSAYRV TEELHQPWLK
     RLLIGFARTS EANGPRKPNS FPHPLIQEID SELPVVQPAL QLTHRIFGSC PPMQSFDPAK
     LLTDSGKLQT LDILLKRLRA GNHRVLLFAQ MTKMLNILED YMNYRKYKYL RLDGSSTIMD
     RRDMVRDFQH RSDIFVFLLS TRAGGLGINL TAADTVIFYE SDWNPTLDLQ AMDRAHRLGQ
     TKDVTVYRLI CKETVEEKIL HRASQKNTVQ QLVMTGGHVQ GDDFLGAADV VSLLMDDAEA
     AQLEQKFREL PLQVKDRQKK KTKRIRIDAE GDATLEELED VDRQDNGQEP LEEPEKPKSS
     NKKRRAASNP KARAPQKAKE EANGEDTPQR TKRVKRQTKS INESLEPVFS ASVTESNKGF
     DPSSSAN
//
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