ID   IOC3_YEAST              Reviewed;         787 AA.
AC   P43596; D6VTP4;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=ISWI one complex protein 3;
GN   Name=IOC3; OrderedLocusNames=YFR013W;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA   Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA   Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT   cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
RN   [2]
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   [3]
RP   FUNCTION OF THE ISW1A COMPLEX.
RX   PubMed=14622597; DOI=10.1016/s0092-8674(03)00880-8;
RA   Morillon A., Karabetsou N., O'Sullivan J., Kent N., Proudfoot N.,
RA   Mellor J.;
RT   "Isw1 chromatin remodeling ATPase coordinates transcription elongation and
RT   termination by RNA polymerase II.";
RL   Cell 115:425-435(2003).
RN   [4]
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   [5]
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   [6]
RP   IDENTIFICATION IN THE ISW1A COMPLEX, AND FUNCTION OF THE ISW1A COMPLEX.
RX   PubMed=12482963; DOI=10.1128/mcb.23.1.80-91.2003;
RA   Vary J.C. Jr., Gangaraju V.K., Qin J., Landel C.C., Kooperberg C.,
RA   Bartholomew B., Tsukiyama T.;
RT   "Yeast Isw1p forms two separable complexes in vivo.";
RL   Mol. Cell. Biol. 23:80-91(2003).
CC   -!- FUNCTION: Functions as a component of the ISW1A complex, which acts in
CC       remodeling the chromatin by catalyzing an ATP-dependent alteration in
CC       the structure of nucleosomal DNA. The ISW1A complex represses gene
CC       expression at initiation through specific positioning of a promoter
CC       proximal dinucleosome. {ECO:0000269|PubMed:12482963,
CC       ECO:0000269|PubMed:14622597}.
CC   -!- SUBUNIT: Component of the ISW1A complex, which at least consists of
CC       ISW1 and IOC3. {ECO:0000269|PubMed:12482963}.
CC   -!- INTERACTION:
CC       P43596; P38144: ISW1; NbExp=11; IntAct=EBI-22944, EBI-21087;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1770 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; D50617; BAA09252.1; -; Genomic_DNA.
DR   EMBL; BK006940; DAA12454.1; -; Genomic_DNA.
DR   PIR; S56268; S56268.
DR   RefSeq; NP_116668.1; NM_001179978.1.
DR   PDB; 2Y9Y; X-ray; 3.25 A; B=127-749.
DR   PDB; 2Y9Z; X-ray; 3.60 A; B=127-749.
DR   PDB; 7X3T; EM; 5.40 A; U=127-749.
DR   PDB; 7X3V; EM; 3.09 A; U=127-749.
DR   PDBsum; 2Y9Y; -.
DR   PDBsum; 2Y9Z; -.
DR   PDBsum; 7X3T; -.
DR   PDBsum; 7X3V; -.
DR   AlphaFoldDB; P43596; -.
DR   EMDB; EMD-32992; -.
DR   EMDB; EMD-32994; -.
DR   SMR; P43596; -.
DR   BioGRID; 31165; 148.
DR   ComplexPortal; CPX-637; ISW1a chromatin remodeling complex.
DR   DIP; DIP-5446N; -.
DR   IntAct; P43596; 29.
DR   MINT; P43596; -.
DR   STRING; 4932.YFR013W; -.
DR   MaxQB; P43596; -.
DR   PaxDb; 4932-YFR013W; -.
DR   PeptideAtlas; P43596; -.
DR   EnsemblFungi; YFR013W_mRNA; YFR013W; YFR013W.
DR   GeneID; 850567; -.
DR   KEGG; sce:YFR013W; -.
DR   AGR; SGD:S000001909; -.
DR   SGD; S000001909; IOC3.
DR   VEuPathDB; FungiDB:YFR013W; -.
DR   eggNOG; ENOG502QVSC; Eukaryota.
DR   GeneTree; ENSGT00940000176416; -.
DR   HOGENOM; CLU_014696_0_0_1; -.
DR   InParanoid; P43596; -.
DR   OMA; YWYEMCH; -.
DR   OrthoDB; 2037049at2759; -.
DR   BioCyc; YEAST:G3O-30466-MONOMER; -.
DR   BioGRID-ORCS; 850567; 3 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P43596; -.
DR   PRO; PR:P43596; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P43596; Protein.
DR   GO; GO:0016587; C:Isw1 complex; IPI:ComplexPortal.
DR   GO; GO:0036436; C:Isw1a complex; IDA:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:ComplexPortal.
DR   GO; GO:0007062; P:sister chromatid cohesion; IMP:SGD.
DR   InterPro; IPR028942; WHIM1_dom.
DR   Pfam; PF15612; WHIM1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..787
FT                   /note="ISWI one complex protein 3"
FT                   /id="PRO_0000202685"
FT   REGION          1..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          749..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..773
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           144..147
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           179..191
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   TURN            192..195
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   TURN            198..202
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           205..212
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   STRAND          219..222
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   STRAND          224..227
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           238..241
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           245..265
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   TURN            266..268
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           284..287
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           293..305
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   TURN            306..309
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   TURN            313..315
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   STRAND          326..328
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   TURN            365..367
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           369..371
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           373..377
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           380..382
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           385..402
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           404..414
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           432..435
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           437..453
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   TURN            454..457
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           462..465
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   TURN            470..472
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           473..481
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           483..490
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   TURN            491..493
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           500..503
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           506..513
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   STRAND          514..516
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           525..527
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   TURN            529..534
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   STRAND          539..543
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   TURN            544..546
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   STRAND          547..550
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   STRAND          557..559
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           569..580
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           586..591
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           594..596
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   STRAND          604..606
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           608..617
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   STRAND          627..629
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           634..643
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           645..648
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           694..696
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           697..726
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   STRAND          727..729
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   HELIX           735..739
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
FT   TURN            740..743
FT                   /evidence="ECO:0007829|PDB:2Y9Y"
SQ   SEQUENCE   787 AA;  90897 MW;  1919A8A1F58B5340 CRC64;
     MDSPSNSIQN LQQEAQGSSS AQLADHDHDR VSMAMPLQTD QSVSVSQSSD NLRRSRRVPK
     PRTSIYDEYE EELKERANKP KRKRPAPPKK KAPSTQNSKS NDKVEKKKTT SIAKDGKPTL
     KTNDKKVAPK PKPAHEQVEP ALIPSNWTSV IPLLTSDFKN QYSVISRLKN PNMKPVPYAG
     DIIKLMAFIN KFSSFFHSDL QNLSFQDFEV GLDLYPGDPN GSAAGIVKGP EDTSLLLYPD
     FMAIKDIVYC QDKMNLLFLS LLDLTFTENF DGKSAKKKGP LTTWENLKSS SKKVFSNPLY
     RLRLVAREWG YPREWRQQLP SDQDISKPKT ALFEQDEQTP VVDPSHPEIL TPNIYTWNAN
     EPLPLESNPL YNREMDKNGI LALKPMDRVV LLRALTDWCA SHSSAIHDEI YKLTHGKKDP
     VFGIQTQQVP RYTIEGVDNT INQFKKLCSL IQSRYEIRSK KKHFVKQLKE GKKPDLSRKL
     EILKEIKAEL KNAVKSEKDE LLFSLYDKWV PLFEGELPDQ PLANPFSERL YKLRLQEFFL
     GRVPHIGDFY MPRLHSYGDS LEMSTFTDLR NLQALLSKFK NNEYNAFTLF ENDGQSMSAQ
     FKLFYHDTPS LAHDVARGRN TSGKVYWYEL CHDSATLLEF LEFLDYKIVK PQDEKKEGNE
     KEKEALNNEA HILEQKSTTD NNPSINTNPL PKDAKYNTAR KKLQILKEFL SDYYFILRQF
     EQMKVQFADM KPGKRQLRRI QRQTVNYNTE YDSEEYVDDE EDDEADIYDD NDNDSSFDDG
     RVKRQRT
//