HST1_YEAST
ID HST1_YEAST Reviewed; 503 AA.
AC P53685; D6W1Z9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=NAD-dependent protein deacetylase HST1;
DE EC=2.3.1.286;
DE AltName: Full=Homologous to SIR2 protein 1;
DE AltName: Full=Regulatory protein SIR2 homolog 1;
GN Name=HST1; OrderedLocusNames=YOL068C;
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 [GENOMIC DNA].
RC STRAIN=GRY 668;
RX PubMed=8810037;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<631::aid-yea960>3.0.co;2-8;
RA Derbyshire M.K., Weinstock K.G., Strathern J.N.;
RT "HST1, a new member of the SIR2 family of genes.";
RL Yeast 12:631-640(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9178509;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<583::aid-yea111>3.0.co;2-y;
RA Tzermia M., Katsoulou C., Alexandraki D.;
RT "Sequence analysis of a 33.2 kb segment from the left arm of yeast
RT chromosome XV reveals eight known genes and ten new open reading frames
RT including homologues of ABC transporters, inositol phosphatases and human
RT expressed sequence tags.";
RL Yeast 13:583-589(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=10562556; DOI=10.1093/emboj/18.22.6448;
RA Xie J., Pierce M., Gailus-Durner V., Wagner M., Winter E., Vershon A.K.;
RT "Sum1 and Hst1 repress middle sporulation-specific gene expression during
RT mitosis in Saccharomyces cerevisiae.";
RL EMBO J. 18:6448-6454(1999).
RN [7]
RP ENZYME ACTIVITY.
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 [8]
RP IDENTIFICATION IN A COMPLEX WITH HOS2; SIF2; SNT1; CPR1; YIL112W AND SET3.
RX PubMed=11711434; DOI=10.1101/gad.207401;
RA Pijnappel W.W.M.P., Schaft D., Roguev A., Shevchenko A., Tekotte H.,
RA Wilm M., Rigaut G., Seraphin B., Aasland R., Stewart A.F.;
RT "The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and
RT Hst1, and is a meiotic-specific repressor of the sporulation gene
RT program.";
RL Genes Dev. 15:2991-3004(2001).
RN [9]
RP INTERACTION WITH RFM1.
RX PubMed=12612074; DOI=10.1128/mcb.23.6.2009-2016.2003;
RA McCord R., Pierce M., Xie J., Wonkatal S., Mickel C., Vershon A.K.;
RT "Rfm1, a novel tethering factor required to recruit the hst1 histone
RT deacetylase for repression of middle sporulation genes.";
RL Mol. Cell. Biol. 23:2009-2016(2003).
RN [10]
RP FUNCTION, ENZYME ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12972620; DOI=10.1128/mcb.23.19.7044-7054.2003;
RA Bedalov A., Hirao M., Posakony J., Nelson M., Simon J.A.;
RT "NAD+-dependent deacetylase Hst1p controls biosynthesis and cellular NAD+
RT levels in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 23:7044-7054(2003).
RN [11]
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 [12]
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).
CC -!- FUNCTION: NAD-dependent histone deacetylase involved in telomeric
CC silencing. Histone deacetylase proteins act via the formation of large
CC multiprotein complexes that are responsible for the deacetylation of
CC lysine residues on the N-terminal part of the core histones (H2A, H2B,
CC H3 and H4). Histone deacetylation gives a tag for epigenetic repression
CC and plays an important role in transcriptional regulation, cell cycle
CC progression and developmental events. Restores silencing at HMR in SIR2
CC mutants when overexpressed. Required to repress middle sporulation
CC genes during vegetative growth. Acts as a sensor of NAD(+) levels and
CC regulator of NAD(+) biosynthesis. Regulates the gene expression of de
CC novo NAD(+) biosynthesis genes. {ECO:0000269|PubMed:10562556,
CC ECO:0000269|PubMed:12972620}.
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 ECO:0000269|PubMed:10841563, ECO:0000269|PubMed:12972620};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=94.2 uM for NAD(+) {ECO:0000269|PubMed:12972620};
CC -!- SUBUNIT: Identified in the Set3C complex with HOS2, SIF2, SNT1, CPR1,
CC HOS4/YIL112W and SET3. Its presence is however not essential for
CC meiotic repression by the Set3C complex. Interacts with SUM1 and RFM1.
CC The interaction with SUM1 is mediated by RFM1.
CC {ECO:0000269|PubMed:11711434, ECO:0000269|PubMed:12612074}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Note=But
CC not nucleolar, and cytoplasmic.
CC -!- MISCELLANEOUS: Present with 1440 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; U39041; AAA81033.1; -; Genomic_DNA.
DR EMBL; L47120; AAB38430.1; -; Genomic_DNA.
DR EMBL; Z74810; CAA99078.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10715.1; -; Genomic_DNA.
DR PIR; S59698; S59698.
DR RefSeq; NP_014573.1; NM_001183323.1.
DR AlphaFoldDB; P53685; -.
DR SMR; P53685; -.
DR BioGRID; 34333; 157.
DR ComplexPortal; CPX-1342; SET3C histone deacetylase complex.
DR ComplexPortal; CPX-1384; SUM1-RFM1-HST1 histone deacetylase complex.
DR DIP; DIP-6757N; -.
DR IntAct; P53685; 5.
DR MINT; P53685; -.
DR STRING; 4932.YOL068C; -.
DR iPTMnet; P53685; -.
DR MaxQB; P53685; -.
DR PaxDb; P53685; -.
DR PRIDE; P53685; -.
DR EnsemblFungi; YOL068C_mRNA; YOL068C; YOL068C.
DR GeneID; 854086; -.
DR KEGG; sce:YOL068C; -.
DR SGD; S000005429; HST1.
DR VEuPathDB; FungiDB:YOL068C; -.
DR eggNOG; KOG2684; Eukaryota.
DR GeneTree; ENSGT00940000159406; -.
DR HOGENOM; CLU_023643_5_0_1; -.
DR InParanoid; P53685; -.
DR OMA; KRKQYFP; -.
DR BioCyc; YEAST:G3O-33473-MON; -.
DR SABIO-RK; P53685; -.
DR PRO; PR:P53685; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P53685; protein.
DR GO; GO:0000118; C:histone deacetylase complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0034967; C:Set3 complex; IDA:SGD.
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:0046970; F:NAD-dependent histone deacetylase activity (H4-K16 specific); IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0009267; P:cellular response to starvation; IC:ComplexPortal.
DR GO; GO:0016575; P:histone deacetylation; IDA:SGD.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IDA:ComplexPortal.
DR GO; GO:0045950; P:negative regulation of mitotic recombination; IMP:SGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IC:ComplexPortal.
DR GO; GO:0043937; P:regulation of sporulation; IC:ComplexPortal.
DR GO; GO:0070623; P:regulation of thiamine biosynthetic process; IMP:CACAO.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1600.10; -; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR007654; NAD-dep_histone_deAcase_SIR2_N.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF04574; DUF592; 1.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Metal-binding; NAD; Nucleus; Reference proteome;
KW Repressor; Sporulation; Transcription; Transcription regulation;
KW Transferase; Zinc.
FT CHAIN 1..503
FT /note="NAD-dependent protein deacetylase HST1"
FT /id="PRO_0000110281"
FT DOMAIN 191..470
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT ACT_SITE 310
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 208..227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 290..293
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 412..414
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 437..439
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 503 AA; 57702 MW; 4CDF2799E4135ABB CRC64;
MNILLMQRIV SFILVVSQGR YFHVGELTMT MLKRPQEEES DNNATKKLKT RLTYPCILGK
DKVTGKFIFP AITKDDVMNA RLFLKDNDLK TFLEYFLPVE VNSIYIYFMI KLLGFDVKDK
ELFMALNSNI TSNKERSSAE LSSIHAKAED EDELTDPLEK KHAVKLIKDL QKAINKVLST
RLRLPNFNTI DHFTATLRNA KKILVLTGAG VSTSLGIPDF RSSEGFYSKI RHLGLEDPQD
VFNLDIFLQD PSVFYNIAHM VLPPENMYSP LHSFIKMLQD KGKLLRNYTQ NIDNLESYAG
IDPDKLVQCH GSFATASCVT CHWQIPGEKI FENIRNLELP LCPYCYQKRK QYFPMSNGNN
TVQTNINFNS PILKSYGVLK PDMTFFGEAL PSRFHKTIRK DILECDLLIC IGTSLKVAPV
SEIVNMVPSH VPQILINRDM VTHAEFDLNL LGFCDDVASL VAKKCHWDIP HKKWQDLKKI
DYNCTEIDKG TYKIKKQPRK KQQ
