RXT2_YEAST
ID RXT2_YEAST Reviewed; 430 AA.
AC P38255; D6VQ96;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Transcriptional regulatory protein RXT2;
GN Name=RXT2; Synonyms=RAF60; OrderedLocusNames=YBR095C; ORFNames=YBR0822;
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 26109 / X2180;
RA Dekker P.J.T., Hoekert W., van Oosterum K., Grivell L.A.;
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
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 [8]
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 [9]
RP IDENTIFICATION IN THE RPD3 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 [10]
RP FUNCTION, IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=16275642; DOI=10.1074/jbc.m511561200;
RA Colina A.R., Young D.;
RT "Raf60, a novel component of the Rpd3 histone deacetylase complex required
RT for Rpd3 activity in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:42552-42556(2005).
RN [11]
RP IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16286008; DOI=10.1016/j.cell.2005.10.025;
RA Keogh M.-C., Kurdistani S.K., Morris S.A., Ahn S.H., Podolny V.,
RA Collins S.R., Schuldiner M., Chin K., Punna T., Thompson N.J., Boone C.,
RA Emili A., Weissman J.S., Hughes T.R., Strahl B.D., Grunstein M.,
RA Greenblatt J.F., Buratowski S., Krogan N.J.;
RT "Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a
RT repressive Rpd3 complex.";
RL Cell 123:593-605(2005).
RN [12]
RP IDENTIFICATION BY 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).
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. {ECO:0000269|PubMed:16275642}.
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:16275642, ECO:0000269|PubMed:16286008,
CC ECO:0000269|PubMed:16314178}.
CC -!- INTERACTION:
CC P38255; P32561: RPD3; NbExp=6; IntAct=EBI-21537, EBI-15864;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RXT2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT92704.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA49507.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA55600.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA85048.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X69881; CAA49507.1; ALT_INIT; Genomic_DNA.
DR EMBL; X78993; CAA55600.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z35964; CAA85048.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY692685; AAT92704.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006936; DAA07216.1; -; Genomic_DNA.
DR PIR; S31313; S31313.
DR RefSeq; NP_009653.2; NM_001178443.1.
DR AlphaFoldDB; P38255; -.
DR BioGRID; 32801; 582.
DR ComplexPortal; CPX-1852; RPD3L histone deacetylase complex.
DR DIP; DIP-6755N; -.
DR IntAct; P38255; 14.
DR MINT; P38255; -.
DR STRING; 4932.YBR095C; -.
DR iPTMnet; P38255; -.
DR MaxQB; P38255; -.
DR PaxDb; P38255; -.
DR PRIDE; P38255; -.
DR EnsemblFungi; YBR095C_mRNA; YBR095C; YBR095C.
DR GeneID; 852392; -.
DR KEGG; sce:YBR095C; -.
DR SGD; S000000299; RXT2.
DR VEuPathDB; FungiDB:YBR095C; -.
DR eggNOG; ENOG502QU3T; Eukaryota.
DR HOGENOM; CLU_756436_0_0_1; -.
DR InParanoid; P38255; -.
DR OMA; YNGSEHN; -.
DR BioCyc; YEAST:G3O-29059-MON; -.
DR PRO; PR:P38255; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38255; protein.
DR GO; GO:1990483; C:Clr6 histone deacetylase complex I''; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0033698; C:Rpd3L complex; IDA:SGD.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0061188; P:negative regulation of ribosomal DNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0061186; P:negative regulation of silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:2000219; P:positive regulation of invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
DR InterPro; IPR039602; Rxt2.
DR InterPro; IPR013904; RXT2_N.
DR PANTHER; PTHR28232; PTHR28232; 1.
DR Pfam; PF08595; RXT2_N; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..430
FT /note="Transcriptional regulatory protein RXT2"
FT /id="PRO_0000202482"
FT REGION 408..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 48629 MW; A78CCBC603E2316C CRC64;
MTIRSSMKNN AELESKSVLA NESNIISTFT RRIIKEKSGN YQVLKRSLDG KLIYPEATGI
SSNRGNKLLQ RSEVVTRRDL NNSKPMIEQT VFYNGSEHRL LQTNIVTDSR RKRIKFTPDI
NVEPVLVGDE NDIDGSEKED ENITDEYYGE EDDDDLSKLV NVKEILTPIL SLGDIINHKT
ISRTFSSPIL KNLALQIILM IEKEQMSVVR YSQFLEVFLG DHPEPIYESN LNLPSYNHNL
TLPEDRGASD EDDINNKNNI NEVNSNSLST EAGHINNGME EFGEEDPFFA LPRLEQSNAL
LSLLPSSSGS ASISTLTAAE QQQLNEEIES ARQLSQIALQ RNKEFIRNLQ KIRKSVIKAN
RIRGRILNWS REYLGISDDD ITIPVALRVV KRGLISATTN KTTNFEEEIE NTMEDGVVDD
NEPDEEANRA
