ID   HDA3_YEAST              Reviewed;         655 AA.
AC   Q06623;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=HDA1 complex subunit 3;
DE   AltName: Full=Histone deacetylase complex 1 subunit 3;
GN   Name=HDA3; Synonyms=PLO1; OrderedLocusNames=YPR179C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313271; PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
RP   FUNCTION, AND IDENTIFICATION IN THE HDA1 HISTONE DEACETYLASE COMPLEX.
RX   MEDLINE=96279114; PubMed=8663039; DOI=10.1074/jbc.271.26.15837;
RA   Carmen A.A., Rundlett S.E., Grunstein M.;
RT   "HDA1 and HDA3 are components of a yeast histone deacetylase (HDA)
RT   complex.";
RL   J. Biol. Chem. 271:15837-15844(1996).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH HDA1 AND HDA3.
RX   PubMed=11287668; DOI=10.1073/pnas.081560698;
RA   Wu J., Carmen A.A., Kobayashi R., Suka N., Grunstein M.;
RT   "HDA2 and HDA3 are related proteins that interact with and are
RT   essential for the activity of the yeast histone deacetylase HDA1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4391-4396(2001).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; 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   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Required for activity of HDA1 histone deacetylase
CC       complex. The HDA1 histone deacetylase complex is responsible for
CC       the deacetylation of lysine residues on the N-terminal part of the
CC       core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a
CC       tag for epigenetic repression and plays an important role in
CC       transcriptional regulation, cell cycle progression and
CC       developmental events.
CC   -!- SUBUNIT: Heterodimer with HDA2. Component of the HDA1 histone
CC       deacetylase complex composed of at least one HDA1 homodimer and
CC       one HDA2/HDA3 heterodimer. Interacts with HDA1 and HDA3.
CC   -!- INTERACTION:
CC       P16649:TUP1; NbExp=1; IntAct=EBI-38663, EBI-19654;
CC       Q96VH3:YCL021W-A; NbExp=1; IntAct=EBI-38663, EBI-2044941;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 1100 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the HDA2/3 family. HDA3 subfamily.
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DR   EMBL; U25842; AAB68112.1; -; Genomic_DNA.
DR   PIR; S59836; S59836.
DR   RefSeq; NP_015505.1; -.
DR   DIP; DIP:4636N; -.
DR   IntAct; Q06623; 13.
DR   PeptideAtlas; Q06623; -.
DR   Ensembl; YPR179C; Saccharomyces cerevisiae.
DR   GeneID; 856309; -.
DR   GenomeReviews; U00094_GR; YPR179C.
DR   KEGG; sce:YPR179C; -.
DR   NMPDR; fig|4932.3.peg.6654; -.
DR   CYGD; YPR179c; -.
DR   SGD; S000006383; HDA3.
DR   HOGENOM; Q06623; -.
DR   OMA; Q06623; YQKELTD.
DR   NextBio; 981679; -.
DR   ArrayExpress; Q06623; -.
DR   GermOnline; YPR179C; Saccharomyces cerevisiae.
DR   GO; GO:0000118; C:histone deacetylase complex; IDA:SGD.
DR   GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR   GO; GO:0004407; F:histone deacetylase activity; IMP:SGD.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR   GO; GO:0031047; P:gene silencing by RNA; IMP:SGD.
DR   GO; GO:0016575; P:histone deacetylation; IDA:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription from R...; IMP:SGD.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Coiled coil; Complete proteome; Nucleus;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    655       HDA1 complex subunit 3.
FT                                /FTId=PRO_0000083932.
FT   COILED      482    632       Potential.
SQ   SEQUENCE   655 AA;  75463 MW;  CC8F8F73D6B78E45 CRC64;
     MDLLRILDTK PIPTIVDATT LGISGNTSGD YWLPTTMSLY QKELTDQIVS LHYSDILRYF
     ETSHYKEDVI LESMKTMCLN GSLVATHPYL LIDHYMPKSL ITRDVPAHLA ENSGKFSVLR
     DLINLVQEYE TETAIVCRPG RTMDLLEALL LGNKVHIKRY DGHSIKSKQK ANDFSCTVHL
     FSSEGINFTK YPIKSKARFD MLICLDTTVD TSQKDIQYLL QYKRERKGLE RYAPIVRLVA
     INSIDHCRLF FGKKFDKNSR EYLENVTAAM VILRDRLGTL PPDLRPIYSQ KLHYLVEWLE
     NPTVPWPLPD IYPLKQYTSM DVERSLLTEV HFKKSDDQLE DAFSNCSKKR GRHGANKAAS
     STVAGIEDNI TPSFYSTKRL KNDYYTNPLK QDMTQLTGIT TADNSSNVNY HLSSGIITHK
     LIQSMGEVYM DICVQKQELD DYSCLDDLQN DHLKFFSNED EKIIKEYETV LRTNNENLNR
     SHELEVENNL KFSQIETLEK DIETLKGSLM AQGETLSKLK DAFVKTDNVQ DEIEKEERVS
     VSRDTEKKYM EQEIKRAVDA IRENEEETHK LNEKQNGLES ELKLKFEKSE ISTKELNEKI
     GFLKKELKLE NDLNEELVGQ LSKTMDNLEN LTIPRVRTQN GNTKKKSRAK KPGNV
//