ITC1_YEAST
ID ITC1_YEAST Reviewed; 1264 AA.
AC P53125; D6VU16;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Imitation switch two complex protein 1;
GN Name=ITC1; OrderedLocusNames=YGL133W; ORFNames=G2842;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8840506;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<887::aid-yea971>3.0.co;2-d;
RA Escribano V., Eraso P., Portillo F., Mazon M.J.;
RT "Sequence analysis of a 14.6 kb DNA fragment of Saccharomyces cerevisiae
RT chromosome VII reveals SEC27, SSM1b, a putative S-adenosylmethionine-
RT dependent enzyme and six new open reading frames.";
RL Yeast 12:887-892(1996).
RN [2]
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 [3]
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 [4]
RP FUNCTION OF THE ISW2 COMPLEX.
RX PubMed=11081629; DOI=10.1016/s0092-8674(00)00134-3;
RA Goldmark J.P., Fazzio T.G., Estep P.W., Church G.M., Tsukiyama T.;
RT "The Isw2 chromatin remodeling complex represses early meiotic genes upon
RT recruitment by Ume6p.";
RL Cell 103:423-433(2000).
RN [5]
RP FUNCTION.
RX PubMed=11489850; DOI=10.1128/jb.183.17.4985-4993.2001;
RA Sugiyama M., Nikawa J.;
RT "The Saccharomyces cerevisiae Isw2p-Itc1p complex represses INO1 expression
RT and maintains cell morphology.";
RL J. Bacteriol. 183:4985-4993(2001).
RN [6]
RP FUNCTION OF THE ISW2 COMPLEX, INTERACTION WITH ISW2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11238944; DOI=10.1128/mcb.21.6.2098-2106.2001;
RA Gelbart M.E., Rechsteiner T., Richmond T.J., Tsukiyama T.;
RT "Interactions of Isw2 chromatin remodeling complex with nucleosomal arrays:
RT analyses using recombinant yeast histones and immobilized templates.";
RL Mol. Cell. Biol. 21:2098-2106(2001).
RN [7]
RP FUNCTION OF THE ISW2 COMPLEX.
RX PubMed=11533234; DOI=10.1128/mcb.21.19.6450-6460.2001;
RA Fazzio T.G., Kooperberg C., Goldmark J.P., Neal C., Basom R., Delrow J.,
RA Tsukiyama T.;
RT "Widespread collaboration of Isw2 and Sin3-Rpd3 chromatin remodeling
RT complexes in transcriptional repression.";
RL Mol. Cell. Biol. 21:6450-6460(2001).
RN [8]
RP FUNCTION.
RX PubMed=12624196; DOI=10.1099/mic.0.25920-0;
RA Ruiz C., Escribano V., Morgado E., Molina M., Mazon M.J.;
RT "Cell-type-dependent repression of yeast a-specific genes requires Itc1p, a
RT subunit of the Isw2p-Itc1p chromatin remodelling complex.";
RL Microbiology 149:341-351(2003).
RN [9]
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 [10]
RP IDENTIFICATION IN THE ISW2 COMPLEX, AND FUNCTION OF THE ISW2 COMPLEX.
RX PubMed=14673157; DOI=10.1128/mcb.24.1.217-227.2004;
RA Iida T., Araki H.;
RT "Noncompetitive counteractions of DNA polymerase epsilon and ISW2/yCHRAC
RT for epigenetic inheritance of telomere position effect in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 24:217-227(2004).
RN [11]
RP IDENTIFICATION IN THE ISW2 COMPLEX.
RX PubMed=15024052; DOI=10.1128/mcb.24.7.2605-2613.2004;
RA McConnell A.D., Gelbart M.E., Tsukiyama T.;
RT "Histone fold protein Dls1p is required for Isw2-dependent chromatin
RT remodeling in vivo.";
RL Mol. Cell. Biol. 24:2605-2613(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [13]
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).
CC -!- FUNCTION: Functions as component of the ISW2 complex, which acts in
CC remodeling the chromatin by catalyzing an ATP-dependent alteration in
CC the structure of nucleosomal DNA. The ISW2 complex is involved in
CC coordinating transcriptional repression and in inheritance of telomeric
CC silencing. It is involved in repression of MAT a-specific genes, INO1,
CC and early meiotic genes during mitotic growth dependent upon
CC transcription factor UME6 and in a parallel pathway to the RPD3-SIN3
CC histone deacetylase complex. ITC1 is required for nucleosome-stimulated
CC ATPase activity and chromatin-remodeling activity of the complex.
CC Required for the repression of MATa a-specific genes.
CC {ECO:0000269|PubMed:11081629, ECO:0000269|PubMed:11238944,
CC ECO:0000269|PubMed:11489850, ECO:0000269|PubMed:11533234,
CC ECO:0000269|PubMed:12624196, ECO:0000269|PubMed:14673157}.
CC -!- SUBUNIT: Component of the ISW2 complex, which at least consists of
CC ISW2, ITC1, DLS1 and DPB4. May form a stable subcomplex with ISW2.
CC {ECO:0000269|PubMed:14673157, ECO:0000269|PubMed:15024052}.
CC -!- INTERACTION:
CC P53125; Q08773: ISW2; NbExp=2; IntAct=EBI-23967, EBI-31118;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063,
CC ECO:0000255|PROSITE-ProRule:PRU00475, ECO:0000269|PubMed:11238944}.
CC -!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z72655; CAA96844.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07977.1; -; Genomic_DNA.
DR PIR; S64146; S64146.
DR RefSeq; NP_011382.1; NM_001180998.1.
DR AlphaFoldDB; P53125; -.
DR SMR; P53125; -.
DR BioGRID; 33119; 271.
DR ComplexPortal; CPX-728; ISW2 chromatin remodeling complex.
DR ComplexPortal; CPX-734; ISW2 chromatin remodeling complex variant 2.
DR DIP; DIP-6737N; -.
DR IntAct; P53125; 36.
DR MINT; P53125; -.
DR STRING; 4932.YGL133W; -.
DR iPTMnet; P53125; -.
DR MaxQB; P53125; -.
DR PaxDb; P53125; -.
DR PRIDE; P53125; -.
DR EnsemblFungi; YGL133W_mRNA; YGL133W; YGL133W.
DR GeneID; 852744; -.
DR KEGG; sce:YGL133W; -.
DR SGD; S000003101; ITC1.
DR VEuPathDB; FungiDB:YGL133W; -.
DR eggNOG; KOG1245; Eukaryota.
DR GeneTree; ENSGT00940000176599; -.
DR HOGENOM; CLU_265647_0_0_1; -.
DR InParanoid; P53125; -.
DR OMA; GAPWCVK; -.
DR BioCyc; YEAST:G3O-30628-MON; -.
DR PRO; PR:P53125; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53125; protein.
DR GO; GO:0008623; C:CHRAC; IPI:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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 InterPro; IPR018501; DDT_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR013136; WSTF_Acf1_Cbp146.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
DR Pfam; PF15613; WSD; 1.
DR SMART; SM00571; DDT; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS51136; WAC; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1264
FT /note="Imitation switch two complex protein 1"
FT /id="PRO_0000084270"
FT DOMAIN 23..130
FT /note="WAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00475"
FT DOMAIN 423..483
FT /note="DDT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT REGION 130..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1264 AA; 145643 MW; 45E4CF8835C7C746 CRC64;
MVLYKRKPIL LPDPKPLPLD LNVQVWHIEE TGEWFSSYEE FLERFDFYTR HHFTCEITGT
SCLTFFQALD SEETQFKYVE DRFPLKLREP VARFLHFNGI RRLDALVEKV YARFKNDFFP
GEVVYLRKQK DSSTTSSNSQ QSTPQPDDMV EINSVGNPGL PQYQYQRRYV IKEKVQFNAT
INPESREIVM PAHTKYMLIE EAASSNKSFI VDQGQIYRDR STFTKHLIKC FFKITLQRAS
SKMGAPWCVK PEYLAMYGLT MEWPKDMLKY KEDEPVVARR SNSANVSSPE SEKNKRQSKS
SGKSNTSNDA SNKKETKKKR KPTEVNDSEN NSSEEDKKKG QNVTSETHSK KRKKEANEEP
NTENVESVPT PANAEPQAVT ITSIMDDLAL PYQHPPNIFP NLTYYNEKLE CISLGSTKLS
RPFDSFGKLL QAYQFLNTFG SKICLSHFSL DQFITSLKCT DPYELKGEVV LVNIRTQTSK
EQEIENNGLP MKNKAETTTE EDSENPSDWQ RNSFIRDMIM KRNSDKVEYK IVHDDPASDD
ILDNINHNGS ALLIEVFTAL LRLFINEEGD WSCIVVENWI IDDKGVLMER KDERGEGEAK
QKRNAHGYFL QDKEKIDNLK DTLKENATEV QKESDAKNET NSESDSKSDS DSEERDPKLE
KCLNYRNVNW IERLTKRQFN NSYWLIILLG VLEDCRHLPM YTEFIDSFIE KIIPKDISAT
QLPKQLWRNF CRKLSFSDKV NALWILVDLV SHFSPDIKAA VDDSMELCGQ IRSERFKVAR
ELKTEAAVLS NLQGDLQAIQ EKLNKTDENT PSADGADKKD DSESNSEPID LIIIEKKQKL
IEEQDKKVQA LQSDKNFLDN CLFENDLQRL KPLGLDRYGN RYFWLDHNGV PFPQYPAGMN
ETPKSNNSLS YHSGRLLIQG PKASSAKFFL NVSDEQLSNW QKIRNSEGIS EATREVFGIS
KTSSGSYNYV ENGIEVELLD SNDRVNPLIE LTPIQKKIMD ETPSRLLLSP DQWYCIDKLE
DLSRIMDWLD NWGRKEHDLL RQIRPIMERI KSSLSLRDHA LSLTAFTKNE EKLLKELENN
EFTENELNVD SMDVDDKNSG VKSEVDVQVD AEEKREAVID EKLEVIADEL MKLDDSSKTR
NVLNRIQELE DQRDELLEQK KSIINSQRPG ARILARSERK RTKISRGNKV NKQIEILTDL
VNYRHFKAME DVIAWKNVLA NSIWGSSLRK NASGNKRSGV IETVDDKLKD IVGQTSRTVT
PAPN
