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RXT3_YEAST
ID   RXT3_YEAST              Reviewed;         294 AA.
AC   Q07458; D6VRS3;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Transcriptional regulatory protein RXT3;
GN   Name=RXT3; OrderedLocusNames=YDL076C;
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=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
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   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   [4]
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   [5]
RP   IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16314178; DOI=10.1016/j.bbaexp.2005.09.005;
RA   Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S., Yates J.,
RA   Washburn M.P., Workman J.L.;
RT   "Stable incorporation of sequence specific repressors Ash1 and Ume6 into
RT   the Rpd3L complex.";
RL   Biochim. Biophys. Acta 1731:77-87(2005).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Component of the RPD3C(L) histone deacetylase complex (HDAC)
CC       responsible for the deacetylation of lysine residues on the N-terminal
CC       part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation
CC       gives a tag for epigenetic repression and plays an important role in
CC       transcriptional regulation, cell cycle progression and developmental
CC       events.
CC   -!- SUBUNIT: Component of the RPD3C(L) complex composed of at least ASH1,
CC       CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6.
CC       {ECO:0000269|PubMed:16314178}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the RXT3 family. {ECO:0000305}.
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DR   EMBL; Z74124; CAA98642.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11783.1; -; Genomic_DNA.
DR   PIR; S67612; S67612.
DR   RefSeq; NP_010207.1; NM_001180135.1.
DR   AlphaFoldDB; Q07458; -.
DR   BioGRID; 31985; 237.
DR   ComplexPortal; CPX-1852; RPD3L histone deacetylase complex.
DR   DIP; DIP-1797N; -.
DR   IntAct; Q07458; 21.
DR   MINT; Q07458; -.
DR   STRING; 4932.YDL076C; -.
DR   iPTMnet; Q07458; -.
DR   MaxQB; Q07458; -.
DR   PaxDb; Q07458; -.
DR   PRIDE; Q07458; -.
DR   EnsemblFungi; YDL076C_mRNA; YDL076C; YDL076C.
DR   GeneID; 851483; -.
DR   KEGG; sce:YDL076C; -.
DR   SGD; S000002234; RXT3.
DR   VEuPathDB; FungiDB:YDL076C; -.
DR   eggNOG; KOG4843; Eukaryota.
DR   HOGENOM; CLU_947333_0_0_1; -.
DR   InParanoid; Q07458; -.
DR   OMA; NNELWGC; -.
DR   BioCyc; YEAST:G3O-29487-MON; -.
DR   PRO; PR:Q07458; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q07458; protein.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0033698; C:Rpd3L complex; IDA:SGD.
DR   GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR   GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR   GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IMP:SGD.
DR   GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR   InterPro; IPR013951; Rxt3.
DR   Pfam; PF08642; Rxt3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromatin regulator; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..294
FT                   /note="Transcriptional regulatory protein RXT3"
FT                   /id="PRO_0000234080"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   294 AA;  33812 MW;  810F0970897878AD CRC64;
     MSVSEQDPNR AYRETQSQIY KLQETLLNSA RTKNKQEEGQ ESNTHSFPEQ YMHYQNGRNS
     AYDLPNVSSQ SVLAFTEKHY PNKLKNLGTL YYNRFKEGSF DEDSTSYSDR HSFPYNLYDN
     TLPPPFLPAI GIQNINNIAT LKITYEDIQA SFNNIESPRK RNNEIWGCDI YSDDSDPILV
     LRHCGFKIGA PSGGSFHKLR RTPVNVTNQD NVTGNLPLLE GTPFDLEVEL LFLPTLQKYP
     SVKRFDITSR EWGSEATVIH DGLSYGIYSI VIKQRLDRDK PHEPNGYIKN LKWT
 
 
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