INO80_YEAST
ID INO80_YEAST Reviewed; 1489 AA.
AC P53115; D6VU00;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000305};
DE EC=3.6.4.- {ECO:0000269|PubMed:10952318};
DE AltName: Full=Inositol-requiring protein 80;
GN Name=INO80; OrderedLocusNames=YGL150C; ORFNames=G1880;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8585324; DOI=10.1002/yea.320111409;
RA James C.M., Indge K.J., Oliver S.G.;
RT "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae
RT chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2,
RT PMR1, RCK1, AMS1 and CAL1/CDC43.";
RL Yeast 11:1413-1419(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046099;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<177::aid-yea62>3.0.co;2-2;
RA Voet M., Defoor E., Verhasselt P., Riles L., Robben J., Volckaert G.;
RT "The sequence of a nearly unclonable 22.8 kb segment on the left arm
RT chromosome VII from Saccharomyces cerevisiae reveals ARO2, RPL9A, TIP1,
RT MRF1 genes and six new open reading frames.";
RL Yeast 13:177-182(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN
RP THE INO80 COMPLEX, AND MUTAGENESIS OF LYS-737.
RX PubMed=10952318; DOI=10.1038/35020123;
RA Shen X., Mizuguchi G., Hamiche A., Wu C.;
RT "A chromatin remodelling complex involved in transcription and DNA
RT processing.";
RL Nature 406:541-544(2000).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN A HIGH MOLECULAR WEIGHT COMPLEX.
RX PubMed=10361278; DOI=10.1046/j.1365-2958.1999.01390.x;
RA Ebbert R., Birkmann A., Schueller H.-J.;
RT "The product of the SNF2/SWI2 paralogue INO80 of Saccharomyces cerevisiae
RT required for efficient expression of various yeast structural genes is part
RT of a high-molecular-weight protein complex.";
RL Mol. Microbiol. 32:741-751(1999).
RN [7]
RP IDENTIFICATION AS A PUTATIVE HELICASE.
RX PubMed=10077188;
RX DOI=10.1002/(sici)1097-0061(199902)15:3<219::aid-yea349>3.0.co;2-3;
RA Shiratori A., Shibata T., Arisawa M., Hanaoka F., Murakami Y., Eki T.;
RT "Systematic identification, classification, and characterization of the
RT open reading frames which encode novel helicase-related proteins in
RT Saccharomyces cerevisiae by gene disruption and Northern analysis.";
RL Yeast 15:219-253(1999).
RN [8]
RP FUNCTION OF THE INO80 COMPLEX.
RX PubMed=12887900; DOI=10.1016/s1097-2765(03)00264-8;
RA Shen X., Ranallo R., Choi E., Wu C.;
RT "Involvement of actin-related proteins in ATP-dependent chromatin
RT remodeling.";
RL Mol. Cell 12:147-155(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP REGULATION OF THE INO80 COMPLEX BY INOSITOL POLYPHOSPHATES.
RX PubMed=12434012; DOI=10.1126/science.1078062;
RA Steger D.J., Haswell E.S., Miller A.L., Wente S.R., O'Shea E.K.;
RT "Regulation of chromatin remodeling by inositol polyphosphates.";
RL Science 299:114-116(2003).
RN [12]
RP FUNCTION OF THE INO80 COMPLEX.
RX PubMed=15607974; DOI=10.1016/j.cell.2004.11.037;
RA Morrison A.J., Highland J., Krogan N.J., Arbel-Eden A., Greenblatt J.F.,
RA Haber J.E., Shen X.;
RT "INO80 and gamma-H2AX interaction links ATP-dependent chromatin remodeling
RT to DNA damage repair.";
RL Cell 119:767-775(2004).
RN [13]
RP FUNCTION OF THE INO80 COMPLEX.
RX PubMed=15607975; DOI=10.1016/j.cell.2004.11.033;
RA van Attikum H., Fritsch O., Hohn B., Gasser S.M.;
RT "Recruitment of the INO80 complex by H2A phosphorylation links ATP-
RT dependent chromatin remodeling with DNA double-strand break repair.";
RL Cell 119:777-788(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-115 AND SER-133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-133 AND SER-610, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: ATPase component of the INO80 complex which remodels
CC chromatin by shifting nucleosomes and is involved in DNA repair
CC (PubMed:10952318, PubMed:12887900). Its ability to induce transcription
CC of some phosphate-responsive genes is modulated by inositol
CC polyphosphates (PubMed:10952318, PubMed:10361278). The INO80 complex is
CC involved in DNA repair by associating with 'Ser-129' phosphorylated H2A
CC histones as a response to DNA damage (PubMed:15607974,
CC PubMed:15607975). {ECO:0000269|PubMed:10361278,
CC ECO:0000269|PubMed:10952318, ECO:0000269|PubMed:12887900,
CC ECO:0000269|PubMed:15607974, ECO:0000269|PubMed:15607975}.
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:0000269|PubMed:10952318};
CC -!- SUBUNIT: Component of the chromatin-remodeling INO80 complex, at least
CC composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3,
CC IES4, IES6, ACT1, IES2, IES5 and INO80. {ECO:0000269|PubMed:10361278,
CC ECO:0000269|PubMed:10952318}.
CC -!- INTERACTION:
CC P53115; Q03435: NHP10; NbExp=10; IntAct=EBI-24019, EBI-12010;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00746,
CC ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC {ECO:0000250|UniProtKB:Q9ULG1}.
CC -!- MISCELLANEOUS: Present with 1110 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; Z48618; CAA88537.1; -; Genomic_DNA.
DR EMBL; X99960; CAA68224.1; -; Genomic_DNA.
DR EMBL; Z72672; CAA96861.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07961.1; -; Genomic_DNA.
DR PIR; S60416; S60416.
DR RefSeq; NP_011365.1; NM_001181015.1.
DR PDB; 5NBN; X-ray; 4.00 A; G/H=462-598.
DR PDBsum; 5NBN; -.
DR AlphaFoldDB; P53115; -.
DR SMR; P53115; -.
DR BioGRID; 33103; 280.
DR ComplexPortal; CPX-863; INO80 chromatin remodeling complex.
DR DIP; DIP-1386N; -.
DR IntAct; P53115; 47.
DR MINT; P53115; -.
DR STRING; 4932.YGL150C; -.
DR iPTMnet; P53115; -.
DR MaxQB; P53115; -.
DR PaxDb; P53115; -.
DR PRIDE; P53115; -.
DR EnsemblFungi; YGL150C_mRNA; YGL150C; YGL150C.
DR GeneID; 852728; -.
DR KEGG; sce:YGL150C; -.
DR SGD; S000003118; INO80.
DR VEuPathDB; FungiDB:YGL150C; -.
DR eggNOG; KOG0388; Eukaryota.
DR GeneTree; ENSGT00900000141110; -.
DR HOGENOM; CLU_000315_26_2_1; -.
DR InParanoid; P53115; -.
DR OMA; FWKKNER; -.
DR BioCyc; YEAST:G3O-30642-MON; -.
DR PRO; PR:P53115; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53115; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0031011; C:Ino80 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:GOC.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0043486; P:histone exchange; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0035065; P:regulation of histone acetylation; IDA:SGD.
DR GO; GO:0019222; P:regulation of metabolic process; IDA:SGD.
DR GO; GO:0032006; P:regulation of TOR signaling; IMP:SGD.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
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 3D-structure; Activator; ATP-binding; Direct protein sequencing;
KW DNA damage; DNA repair; DNA-binding; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1489
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000074329"
FT DOMAIN 476..601
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 718..890
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1303..1467
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 137..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 841..844
FT /note="DEAQ box"
FT COMPBIAS 138..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..289
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 731..738
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 737
FT /note="K->A: Reduced ATPase activity of the INO80 complex."
FT /evidence="ECO:0000269|PubMed:10952318"
SQ SEQUENCE 1489 AA; 171455 MW; 017053C5A245337E CRC64;
MSLAVLLNKE DKDISDFSKT TAGKSAKKNS RERVADVAPT RVLDKKQAYL SQLNSEFNRI
KRRDSIEQLY QDWKFINLQE FELISEWNQQ SKDWQFDNTN DSQDLHFKKL YRDMSMINKE
WAEYQSFKNA NLSDIINEKD ADEDEEDDED ELEDGEEDME EDEASTGRHT NGKSMRGNGI
QKSRKKDAAA AAAIGKAIKD DQTHADTVVT VNGDENEDGN NGEDEDNDND NENNNDNDND
NENENDNDSD NDDEEENGEE DEEEEEIEDL DEEDFAAFEE QDDNDDEDFN PDVEKRRKRS
SSSSSSTKLS MNSLSLITSK KINKNITINS DRPKIVRELI KMCNKNKHQK IKKRRFTNCI
VTDYNPIDSK LNIKITLKQY HVKRLKKLIN DAKREREREE ALKNNVGLDG NDLDNDEDGS
ESHKRRKLNN NTANGADDAN KRKFNTRHGL PTYGMKMNAK EARAIQRHYD NTYTTIWKDM
ARKDSTKMSR LVQQIQSIRS TNFRKTSSLC AREAKKWQSK NFKQIKDFQT RARRGIREMS
NFWKKNEREE RDLKKKIEKE AMEQAKKEEE EKESKRQAKK LNFLLTQTEL YSHFIGRKIK
TNELEGNNVS SNDSESQKNI DISALAPNKN DFHAIDFDNE NDEQLRLRAA ENASNALAET
RAKAKQFDDH ANAHEEEEEE DELNFQNPTS LGEITIEQPK ILACTLKEYQ LKGLNWLANL
YDQGINGILA DEMGLGKTVQ SISVLAHLAE NHNIWGPFLV VTPASTLHNW VNEISKFLPQ
FKILPYWGNA NDRKVLRKFW DRKNLRYNKN APFHVMVTSY QMVVTDANYL QKMKWQYMIL
DEAQAIKSSQ SSRWKNLLSF HCRNRLLLTG TPIQNSMQEL WALLHFIMPS LFDSHDEFNE
WFSKDIESHA EANTKLNQQQ LRRLHMILKP FMLRRVKKNV QSELGDKIEI DVLCDLTQRQ
AKLYQVLKSQ ISTNYDAIEN AATNDSTSNS ASNSGSDQNL INAVMQFRKV CNHPDLFERA
DVDSPFSFTT FGKTTSMLTA SVANNNSSVI SNSNMNLSSM SSNNISNGKF TDLIYSSRNP
IKYSLPRLIY EDLILPNYNN DVDIANKLKN VKFNIFNPST NYELCLFLSK LTGEPSLNEF
FRVSTTPLLK RVIERTNGPK NTDSLSFKTI TQELLEVTRN APSEGVMASL LNVEKHAYER
EYLNCIQRGY HPNVSAPPVT IEVLGSSHVT NSINNELFDP LISQALSDIP AITQYNMHVK
KGIPVEDFPK TGLFPEPLNK NFSSNISMPS MDRFITESAK LRKLDELLVK LKSEGHRVLI
YFQMTKMMDL MEEYLTYRQY NHIRLDGSSK LEDRRDLVHD WQTNPEIFVF LLSTRAGGLG
INLTAADTVI FYDSDWNPTI DSQAMDRAHR LGQTRQVTVY RLLVRGTIEE RMRDRAKQKE
QVQQVVMEGK TQEKNIKTIE VGENDSEVTR EGSKSISQDG IKEAASALA
