HST3_YEAST
ID HST3_YEAST Reviewed; 447 AA.
AC P53687; D6W291; Q66R16;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=NAD-dependent histone deacetylase HST3;
DE EC=2.3.1.286;
DE AltName: Full=Homologous to SIR2 protein 3;
DE AltName: Full=Regulatory protein SIR2 homolog 3;
GN Name=HST3; OrderedLocusNames=YOR025W; ORFNames=OR26.15;
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=S288c / YPH1;
RX PubMed=7498786; DOI=10.1101/gad.9.23.2888;
RA Brachmann C.B., Sherman J.M., Devine S.E., Cameron E.E., Pillus L.,
RA Boeke J.D.;
RT "The SIR2 gene family, conserved from bacteria to humans, functions in
RT silencing, cell cycle progression, and chromosome stability.";
RL Genes Dev. 9:2888-2902(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [5]
RP FUNCTION.
RX PubMed=10841563; DOI=10.1073/pnas.97.12.6658;
RA Smith J.S., Brachmann C.B., Celic I., Kenna M.A., Muhammad S., Starai V.J.,
RA Avalos J.L., Escalante-Semerena J.C., Grubmeyer C., Wolberger C.,
RA Boeke J.D.;
RT "A phylogenetically conserved NAD+-dependent protein deacetylase activity
RT in the Sir2 protein family.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6658-6663(2000).
RN [6]
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=16487579; DOI=10.1016/j.cell.2005.12.036;
RA Pan X., Ye P., Yuan D.S., Wang X., Bader J.S., Boeke J.D.;
RT "A DNA integrity network in the yeast Saccharomyces cerevisiae.";
RL Cell 124:1069-1081(2006).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17106263; DOI=10.4161/cc.5.22.3501;
RA Miller K.M., Maas N.L., Toczyski D.P.;
RT "Taking it off: regulation of H3 K56 acetylation by Hst3 and Hst4.";
RL Cell Cycle 5:2561-2565(2006).
RN [10]
RP FUNCTION.
RX PubMed=16815704; DOI=10.1016/j.cub.2006.06.023;
RA Celic I., Masumoto H., Griffith W.P., Meluh P., Cotter R.J., Boeke J.D.,
RA Verreault A.;
RT "The sirtuins Hst3 and Hst4p preserve genome integrity by controlling
RT histone H3 lysine 56 deacetylation.";
RL Curr. Biol. 16:1280-1289(2006).
CC -!- FUNCTION: NAD-dependent histone deacetylase, which contributes together
CC with HST4 to histone H3 'Lys-56' deacetylation, regulation of telomeric
CC silencing, proper cell cycle progression, DNA damage control, DNA
CC recombination, and genomic maintenance. {ECO:0000269|PubMed:10841563,
CC ECO:0000269|PubMed:16487579, ECO:0000269|PubMed:16815704,
CC ECO:0000269|PubMed:17106263}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000305}.
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DR EMBL; U39062; AAA81034.1; -; Genomic_DNA.
DR EMBL; X87331; CAA60741.1; -; Genomic_DNA.
DR EMBL; Z74933; CAA99215.1; -; Genomic_DNA.
DR EMBL; AY723866; AAU09783.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10807.1; -; Genomic_DNA.
DR PIR; S54631; S54631.
DR RefSeq; NP_014668.1; NM_001183444.1.
DR AlphaFoldDB; P53687; -.
DR SMR; P53687; -.
DR BioGRID; 34428; 299.
DR DIP; DIP-1378N; -.
DR IntAct; P53687; 3.
DR MINT; P53687; -.
DR STRING; 4932.YOR025W; -.
DR iPTMnet; P53687; -.
DR PaxDb; P53687; -.
DR PRIDE; P53687; -.
DR EnsemblFungi; YOR025W_mRNA; YOR025W; YOR025W.
DR GeneID; 854190; -.
DR KEGG; sce:YOR025W; -.
DR SGD; S000005551; HST3.
DR VEuPathDB; FungiDB:YOR025W; -.
DR eggNOG; KOG2684; Eukaryota.
DR HOGENOM; CLU_021544_4_0_1; -.
DR InParanoid; P53687; -.
DR OMA; THKFIAH; -.
DR BioCyc; YEAST:G3O-33572-MON; -.
DR PRO; PR:P53687; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P53687; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IDA:SGD.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IMP:SGD.
DR GO; GO:0009299; P:mRNA transcription; IDA:SGD.
DR GO; GO:0098781; P:ncRNA transcription; IDA:SGD.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:SGD.
DR GO; GO:0046459; P:short-chain fatty acid metabolic process; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IGI:SGD.
DR Gene3D; 3.30.1600.10; -; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; NAD; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Transferase; Zinc.
FT CHAIN 1..447
FT /note="NAD-dependent histone deacetylase HST3"
FT /id="PRO_0000110283"
FT DOMAIN 43..349
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 60..79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 151..154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 282..284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 312..314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 418
FT /note="E -> G (in Ref. 4; AAU09783)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 50524 MW; 59CD5FBD712B7005 CRC64;
MTSVSPSPPA SRSGSMCSDL PSSLQTEKLA HIIGLDADDE VLRRVTKQLS RSRRIACLTG
AGISCNAGIP DFRSSDGLYD LVKKDCSQYW SIKSGREMFD ISLFRDDFKI SIFAKFMERL
YSNVQLAKPT KTHKFIAHLK DRNKLLRCYT QNIDGLEESI GLTLSNRKLP LTSFSSHWKN
LDVVQLHGDL KTLSCTKCFQ TFPWSRYWSR CLRRGELPLC PDCEALINKR LNEGKRTLGS
NVGILRPNIV LYGENHPSCE IITQGLNLDI IKGNPDFLII MGTSLKVDGV KQLVKKLSKK
IHDRGGLIIL VNKTPIGESS WHGIIDYQIH SDCDNWVTFL ESQIPDFFKT QDQIKKLRQL
KREASDLRKQ MKAQKDSIGT PPTTPLRTAQ GIDIQGNNEL NTKIKSLNTV KRKILSPENS
SEEDEEENLD TRKRAKIRPT FGDNQAS
