ID   HOS2_YEAST              Reviewed;         452 AA.
AC   P53096; D6VTW0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=Probable histone deacetylase HOS2;
DE            EC=3.5.1.98;
GN   Name=HOS2; OrderedLocusNames=YGL194C; ORFNames=G1330;
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 96604 / S288c / FY1679;
RX   PubMed=9046087;
RX   DOI=10.1002/(sici)1097-0061(199701)13:1<55::aid-yea48>3.0.co;2-9;
RA   Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.;
RT   "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII
RT   from Saccharomyces cerevisiae.";
RL   Yeast 13:55-64(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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   GENE NAME.
RX   PubMed=8962081; DOI=10.1073/pnas.93.25.14503;
RA   Rundlett S.E., Carmen A.A., Kobayashi R., Bavykin S., Turner B.M.,
RA   Grunstein M.;
RT   "HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes
RT   that regulate silencing and transcription.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:14503-14508(1996).
RN   [5]
RP   IDENTIFICATION IN A COMPLEX WITH SET3; HST1; SNT1; SIF2; CPR1 AND YIL112W.
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   [6]
RP   FUNCTION, AND MUTAGENESIS OF 195-HIS-HIS-196.
RX   PubMed=12434058; DOI=10.1126/science.1077790;
RA   Wang A., Kurdistani S.K., Grunstein M.;
RT   "Requirement of Hos2 histone deacetylase for gene activity in yeast.";
RL   Science 298:1412-1414(2002).
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).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC       N-terminal part of the core histones (H2A, H2B, H3 and H4). It is
CC       apparently involved in transcriptional activation.
CC       {ECO:0000269|PubMed:12434058}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC         [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC   -!- SUBUNIT: Identified in a Set3C complex with SET3, HST1, SNT1, SIF2,
CC       CPR1 and HOS4/YIL112W. {ECO:0000269|PubMed:11711434}.
CC   -!- INTERACTION:
CC       P53096; P14922: CYC8; NbExp=4; IntAct=EBI-8475, EBI-18215;
CC       P53096; P61830: HHT2; NbExp=2; IntAct=EBI-8475, EBI-8098;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 4890 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X91837; CAA62950.1; -; Genomic_DNA.
DR   EMBL; Z72716; CAA96906.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07921.1; -; Genomic_DNA.
DR   PIR; S64211; S64211.
DR   RefSeq; NP_011321.1; NM_001181059.1.
DR   AlphaFoldDB; P53096; -.
DR   SMR; P53096; -.
DR   BioGRID; 33063; 406.
DR   ComplexPortal; CPX-1342; SET3C histone deacetylase complex.
DR   DIP; DIP-6828N; -.
DR   IntAct; P53096; 37.
DR   STRING; 4932.YGL194C; -.
DR   MaxQB; P53096; -.
DR   PaxDb; 4932-YGL194C; -.
DR   PeptideAtlas; P53096; -.
DR   EnsemblFungi; YGL194C_mRNA; YGL194C; YGL194C.
DR   GeneID; 852681; -.
DR   KEGG; sce:YGL194C; -.
DR   AGR; SGD:S000003162; -.
DR   SGD; S000003162; HOS2.
DR   VEuPathDB; FungiDB:YGL194C; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   GeneTree; ENSGT00940000160487; -.
DR   HOGENOM; CLU_007727_7_4_1; -.
DR   InParanoid; P53096; -.
DR   OMA; CYETSIC; -.
DR   OrthoDB; 1327607at2759; -.
DR   BioCyc; YEAST:G3O-30675-MONOMER; -.
DR   Reactome; R-SCE-2500257; Resolution of Sister Chromatid Cohesion.
DR   BioGRID-ORCS; 852681; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53096; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53096; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR   GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR   GO; GO:0034967; C:Set3 complex; IDA:SGD.
DR   GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR   GO; GO:0045129; F:NAD-independent histone deacetylase activity; IDA:SGD.
DR   GO; GO:0009267; P:cellular response to starvation; NAS:ComplexPortal.
DR   GO; GO:0006974; P:DNA damage response; NAS:ComplexPortal.
DR   GO; GO:0045835; P:negative regulation of meiotic nuclear division; IDA:ComplexPortal.
DR   GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:SGD.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:SGD.
DR   CDD; cd11598; HDAC_Hos2; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625:SF25; HISTONE DEACETYLASE 3; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   1: Evidence at protein level;
KW   Activator; Chromatin regulator; Hydrolase; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..452
FT                   /note="Probable histone deacetylase HOS2"
FT                   /id="PRO_0000114723"
FT   REGION          26..340
FT                   /note="Histone deacetylase"
FT   REGION          428..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         196..197
FT                   /note="HH->AA: Leads to hyperacetylation."
FT   CONFLICT        352..364
FT                   /note="PFRDSFGPDYSLY -> HSGTHSGRIIHFI (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   452 AA;  51455 MW;  024E8AEA0A445A08 CRC64;
     MSGTFSYDVK TKENEPLFEF NSAYSPRVSY HFNSKVSHYH YGVKHPMKPF RLMLTDHLVS
     SYGLHKIMDL YETRSATRDE LLQFHSEDYV NFLSKVSPEN ANKLPRGTLE NFNIGDDCPI
     FQNLYDYTTL YTGASLDATR KLINNQSDIA INWSGGLHHA KKNSPSGFCY VNDIVLSILN
     LLRYHPRILY IDIDLHHGDG VQEAFYTTDR VFTLSFHKYN GEFFPGTGDL TEIGCDKGKH
     FALNVPLEDG IDDDSYINLF KSIVDPLIMT FKPTLIVQQC GADSLGHDRL GCFNLNIKAH
     GECVKFVKSF GLPMLVVGGG GYTPRNVSRL WTYETGILND VLLPEDIPED IPFRDSFGPD
     YSLYPMLDDL YENKNSKKLL EDIRIRCLEN IRYLQGAPSV RMDAECIPTQ DISALTEEED
     KIIQEMNEET EADSSNRLEE MEKENSGLIA FS
//