INO80_DROME
ID INO80_DROME Reviewed; 1638 AA.
AC Q9VDY1; Q8T9F9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000305};
DE Short=dINO80;
DE EC=3.6.4.- {ECO:0000250|UniProtKB:Q9ULG1};
GN Name=Ino80 {ECO:0000303|PubMed:16618800, ECO:0000312|FlyBase:FBgn0086613};
GN ORFNames=CG31212 {ECO:0000312|FlyBase:FBgn0086613};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF55658.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF55658.2}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL39931.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP IDENTIFICATION IN THE INO80 COMPLEX, AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo {ECO:0000269|PubMed:16618800};
RX PubMed=16618800; DOI=10.1101/gad.377406;
RA Klymenko T., Papp B., Fischle W., Koecher T., Schelder M., Fritsch C.,
RA Wild B., Wilm M., Mueller J.;
RT "A Polycomb group protein complex with sequence-specific DNA-binding and
RT selective methyl-lysine-binding activities.";
RL Genes Dev. 20:1110-1122(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-48; THR-52; SER-67;
RP SER-70; SER-227 AND SER-230, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: ATPase component of the chromatin remodeling INO80 complex
CC which is involved in transcriptional regulation, DNA replication and
CC DNA repair. Binds DNA. As part of the INO80 complex, remodels chromatin
CC by shifting nucleosomes. {ECO:0000250|UniProtKB:Q9ULG1}.
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 chromatin remodeling Ino80 complex.
CC {ECO:0000269|PubMed:16618800}.
CC -!- INTERACTION:
CC Q9VDY1; Q8ST83: pho; NbExp=4; IntAct=EBI-3414232, EBI-125201;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00746,
CC ECO:0000269|PubMed:16618800}.
CC -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC {ECO:0000250|UniProtKB:Q9ULG1}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014297; AAF55658.2; -; Genomic_DNA.
DR EMBL; AY069786; AAL39931.1; -; mRNA.
DR RefSeq; NP_732413.1; NM_169854.2.
DR AlphaFoldDB; Q9VDY1; -.
DR SMR; Q9VDY1; -.
DR BioGRID; 67311; 5.
DR IntAct; Q9VDY1; 388.
DR STRING; 7227.FBpp0083185; -.
DR iPTMnet; Q9VDY1; -.
DR PaxDb; Q9VDY1; -.
DR EnsemblMetazoa; FBtr0083771; FBpp0083185; FBgn0086613.
DR GeneID; 42314; -.
DR KEGG; dme:Dmel_CG31212; -.
DR UCSC; CG31212-RA; d. melanogaster.
DR CTD; 54617; -.
DR FlyBase; FBgn0086613; Ino80.
DR VEuPathDB; VectorBase:FBgn0086613; -.
DR eggNOG; KOG0388; Eukaryota.
DR GeneTree; ENSGT00900000141110; -.
DR HOGENOM; CLU_000315_19_0_1; -.
DR InParanoid; Q9VDY1; -.
DR OMA; AQYAYYS; -.
DR OrthoDB; 188211at2759; -.
DR PhylomeDB; Q9VDY1; -.
DR Reactome; R-DME-5689603; UCH proteinases.
DR Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; Q9VDY1; -.
DR BioGRID-ORCS; 42314; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Ino80; fly.
DR GenomeRNAi; 42314; -.
DR PRO; PR:Q9VDY1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0086613; Expressed in spermathecum and 21 other tissues.
DR ExpressionAtlas; Q9VDY1; baseline and differential.
DR Genevisible; Q9VDY1; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0031011; C:Ino80 complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:UniProtKB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0040034; P:regulation of development, heterochronic; IMP:FlyBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:FlyBase.
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 Gene3D; 3.40.50.300; -; 2.
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-rel_dom; 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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1638
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000306380"
FT DOMAIN 313..438
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 547..718
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1160..1315
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 41..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1463..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 136..161
FT /evidence="ECO:0000255"
FT COMPBIAS 43..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1491
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 560..567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 1628..1629
FT /note="LS -> SA (in Ref. 3; AAL39931)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1638 AA; 187086 MW; B9D8BB664644512B CRC64;
MEAKPVPAPQ PRPRAMAEPL HIQRLEAALN MRPFMNMAKR SLRKPLSSDE ETDDEHVVKR
EHDVQDSDDS STVGVVRMKQ SSKRKSRLLA SKEERQSVKA QLYNFNDLTS DREWLYDLLL
SDTESDDPTI TEDEYVQQLL REHVREQRQR KNYYKKAANA QYAYYGSGLL SNHDIFAERQ
LATAGVRKRR RRTKQEILMA RLAEAQAGPK PPKQRRRGRK KRDNMGSPES GEVPPSELGK
YTFGDTLPNN EDDDEDGGEV DYKRELASLA LDYPEEEEIE EEVDVEGGTE GQVTKVRRKR
KNPAALAARR RRIWQIMSKK ESGRLQRIKS NNHKEMLANC KRVAGMCAKV VRQRAINSQR
IMKETVWRAK RLTREMLAYW KRYERVERDQ RRKQEREAEE QRKQDVELIE VKRQQRKLNF
LITQTELYAH FMSKKLGQGS EEDQLRILSQ LDEETNARLA AQDDYDAGEM KLLAQENAEA
AMQRDLDKTR AFDVFAKKKE KEEEEQAQES VEDIKPEPRP EMKDLPQPKM FKGTLKGYQI
KGMTWLANIY DQGISGILAD EMGLGKTVQS IAFLCHIAEH YGVWGPFLVI SPASTLHNWQ
QEMSRFVPDF KVVPYWGSPA ERKILRQFWD QKHLHTRDAS FHVVITSYQL VVSDYKYFNR
IKWQYMVLDE AQAIKSAASQ RWKLLLGFSC RNRLLLSGTP IQNSMAELWA LLHFIMPTLF
DSHDEFNEWF SKDIESHAEN KTGIDEKQIS RLHMILKPFM LRRIKKDVEN ELSDKIEIMV
YCPLTIRQKL LYRALKQKIR IEDLLHLTSG STTTSSSSSA SNLMNLVMQF RKVCNHPELF
ERRDARSPFF MRCAEYTIPR LIHEEGLIHR MLPSRKHLLY NRFNIFKSEY IQRSLFEDVN
VNSCFGFTRL CDLSVGDMVE VTLNGLIDFL LHYRRVLEKY PLLAYRRFWW KKQPDSRYQL
LEPMLENKLA LDYMPPNSVL KNFIFTAMTA NESSVYAFGD YFTYNMQETI EHRVIRSKIL
KKKTSLIEEM EDVSKQKLEI ESVEVQTKSN AKSDVKVTTL LLLPEFPHRP RKPRKYVCEP
LSMPRILYDL GQKVQAVHRY LYCDSRSAAW SQIRHNQCEN SQGRELVSSG LALCKPHGGW
SSIVVPDKET LITDAGKLFV LDNLLTRLKA NGHRVLIYSQ MTKMIDLLEE YMWHRKHRYM
RLDGSSKISA RRDMVADFQT RADIFVFLLS TRAGGLGINL TAADTVIFYD SDWNPTVDQQ
AMDRAHRLGQ TKQVTVYRLI CKGTIEERIL QRAREKSEIQ RMVISGGNFK PDTLKPKEVV
SLLLDDEEIE MKYRQEAKLQ SSSPIPAATQ SERKRRHPQK DVNMGGTTIA ATSATQNPDD
DVPSCSSAAK RIKLETEEDF IDVGITSSAS SVGTDSNHPT LSQETYVPGA TCVQQTEIDS
ENEALVVDGD SPTMLGQNES MNFLDDLSGI SPMRRRHHPR GTRRGRPRGS TRRGGGHGSI
PRVLTPTQAA TPAVPATASQ AAAAGTGAAA GTSSPLPQQE VSGGGDNAGV PLHEEEYRTS
PSGQSPGVSC KRGPGRPRSK TATPISRGTR GAPRARRPMG PLLVPLGRSP DDTPPSSSPA
TSRAPSPLSG SHGAVGPE
