ID   RCO1_YEAST              Reviewed;         684 AA.
AC   Q04779; D6VZP9;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 181.
DE   RecName: Full=Transcriptional regulatory protein RCO1;
GN   Name=RCO1; OrderedLocusNames=YMR075W; ORFNames=YM9916.14;
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=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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(S) COMPLEX, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND FUNCTION OF THE RPD3C(S) COMPLEX.
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-683, AND
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).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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: Catalytic component of the RPD3C(S) histone deacetylase
CC       complex responsible for the deacetylation of lysine residues on the N-
CC       terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC       deacetylation gives a tag for epigenetic repression and plays an
CC       important role in transcriptional regulation, cell cycle progression,
CC       DNA damage response, osmotic stress response and developmental events.
CC       {ECO:0000269|PubMed:16286008}.
CC   -!- SUBUNIT: Component of the RPD3C(S) complex composed of at least EAF3,
CC       RCO1, RPD3, SIN3, and UME1. {ECO:0000269|PubMed:16286008}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z48952; CAA88800.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09973.1; -; Genomic_DNA.
DR   PIR; S52835; S52835.
DR   RefSeq; NP_013791.1; NM_001182574.1.
DR   AlphaFoldDB; Q04779; -.
DR   SMR; Q04779; -.
DR   BioGRID; 35250; 423.
DR   ComplexPortal; CPX-1851; RPD3S histone deacetylase complex.
DR   DIP; DIP-1959N; -.
DR   IntAct; Q04779; 50.
DR   MINT; Q04779; -.
DR   STRING; 4932.YMR075W; -.
DR   iPTMnet; Q04779; -.
DR   MaxQB; Q04779; -.
DR   PaxDb; Q04779; -.
DR   PRIDE; Q04779; -.
DR   EnsemblFungi; YMR075W_mRNA; YMR075W; YMR075W.
DR   GeneID; 855097; -.
DR   KEGG; sce:YMR075W; -.
DR   SGD; S000004680; RCO1.
DR   VEuPathDB; FungiDB:YMR075W; -.
DR   eggNOG; KOG4299; Eukaryota.
DR   GeneTree; ENSGT00990000209321; -.
DR   HOGENOM; CLU_016350_0_0_1; -.
DR   InParanoid; Q04779; -.
DR   OMA; YGQSITK; -.
DR   BioCyc; YEAST:G3O-32777-MON; -.
DR   PRO; PR:Q04779; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04779; protein.
DR   GO; GO:0000118; C:histone deacetylase complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0032221; C:Rpd3S/Clr6-CII complex; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016575; P:histone deacetylation; IMP:SGD.
DR   GO; GO:0060195; P:negative regulation of antisense RNA transcription; IMP:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR   GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IMP:SGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR   GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
DR   Gene3D; 3.30.40.10; -; 2.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF57903; SSF57903; 2.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromatin regulator; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..684
FT                   /note="Transcriptional regulatory protein RCO1"
FT                   /id="PRO_0000203282"
FT   ZN_FING         260..309
FT                   /note="PHD-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         414..472
FT                   /note="PHD-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         683
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   684 AA;  78836 MW;  CFC282DC9A782E5C CRC64;
     MDTSKKDTTR SPSHSNSSSP SSSSLSSSSS KEKKRPKRLS SQNVNYDLKR RKIITSEGIE
     RSFKNEHSNL AVEDNIPEEE PKELLEKDSK GNIIKLNEPS TISEDSKVSV TGLPLNKGPS
     EKIKRESLWN YRKNLGGQSN NSEMTLVPSK RFTQVPKNFQ DLNRNDLKTF LTENMTEESN
     IRSTIGWNGD IINRTRDREP ESDRDNKKLS NIRTKIILST NATYDSKSKL FGQNSIKSTS
     NASEKIFRDK NNSTIDFENE DFCSACNQSG SFLCCDTCPK SFHFLCLDPP IDPNNLPKGD
     WHCNECKFKI FINNSMATLK KIESNFIKQN NNVKIFAKLL FNIDSHNPKQ FQLPNYIKET
     FPAVKTGSRG QYSDENDKIP LTDRQLFNTS YGQSITKLDS YNPDTHIDSN SGKFLICYKC
     NQTRLGSWSH PENSRLIMTC DYCQTPWHLD CVPRASFKNL GSKWKCPLHS PTKVYKKIHH
     CQEDNSVNYK VWKKQRLINK KNQLYYEPLQ KIGYQNNGNI QIIPTTSHTD YDFNQDFKIT
     QIDENSIKYD FFDKIYKSKM VQKRKLFQFQ ESLIDKLVSN GSQNGNSEDN MVKDIASLIY
     FQVSNNDKSS NNKSASKSNN LRKLWDLKEL TNVVVPNELD SIQFNDFSSD EIKHLLYLKK
     IIESKPKEEL LKFLNIENPE NQSE