IOC3_YEAST
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 03-AUG-2022, entry version 151.
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 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 PDBsum; 2Y9Y; -.
DR PDBsum; 2Y9Z; -.
DR AlphaFoldDB; P43596; -.
DR SMR; P43596; -.
DR BioGRID; 31165; 136.
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; P43596; -.
DR PRIDE; P43596; -.
DR EnsemblFungi; YFR013W_mRNA; YFR013W; YFR013W.
DR GeneID; 850567; -.
DR KEGG; sce:YFR013W; -.
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 BioCyc; YEAST:G3O-30466-MON; -.
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 transcription, DNA-templated; IC: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
