ID   CLR3_SCHPO              Reviewed;         687 AA.
AC   P56523;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-NOV-2009, entry version 63.
DE   RecName: Full=Histone deacetylase clr3;
DE            EC=3.5.1.98;
DE   AltName: Full=Cryptic loci regulator 3;
GN   Name=clr3; ORFNames=SPBC800.03;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=98429513; PubMed=9755190;
RA   Grewal S.I.S., Bonaduce M.J., Klar A.J.S.;
RT   "Histone deacetylase homologs regulate epigenetic inheritance of
RT   transcriptional silencing and chromosome segregation in fission
RT   yeast.";
RL   Genetics 150:563-576(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [4]
RP   FUNCTION, INTERACTION WITH CCQ1; CLR1; CLR2 AND MIT1, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF ASP-232.
RX   PubMed=17289569; DOI=10.1016/j.cell.2006.12.035;
RA   Sugiyama T., Cam H.P., Sugiyama R., Noma K., Zofall M., Kobayashi R.,
RA   Grewal S.I.S.;
RT   "SHREC, an effector complex for heterochromatic transcriptional
RT   silencing.";
RL   Cell 128:491-504(2007).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes. Required for proper
CC       positioning of nucleosomes at heterochromatic loci and for
CC       transcriptional gene silencing (TGS) function of the Snf2/Hdac-
CC       containing repressor complex (SHREC).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Interacts with ccq1, clr1, clr2 and mit1.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Associates with major
CC       heterochromatin, centromeres, sub-telomeres, rDNA and the mat
CC       locus.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. Type 2
CC       subfamily.
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DR   EMBL; AF064207; AAD05212.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAC01518.1; -; Genomic_DNA.
DR   PIR; T43797; T43797.
DR   RefSeq; NP_595104.1; -.
DR   STRING; P56523; -.
DR   GeneID; 2540821; -.
DR   GenomeReviews; CU329671_GR; clr3.
DR   KEGG; spo:SPBC800.03; -.
DR   NMPDR; fig|4896.1.peg.970; -.
DR   GeneDB_Spombe; SPBC800.03; -.
DR   OMA; DPHPEDP; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-003203-MON; -.
DR   ArrayExpress; P56523; -.
DR   GO; GO:0005721; C:centromeric heterochromatin; IDA:GeneDB_SPombe.
DR   GO; GO:0031934; C:mating-type region heterochromatin; IDA:GeneDB_SPombe.
DR   GO; GO:0030874; C:nucleolar chromatin; IDA:GeneDB_SPombe.
DR   GO; GO:0016581; C:NuRD complex; IDA:GeneDB_SPombe.
DR   GO; GO:0033553; C:rDNA heterochromatin; IDA:GeneDB_SPombe.
DR   GO; GO:0031933; C:telomeric heterochromatin; IDA:GeneDB_SPombe.
DR   GO; GO:0031078; F:histone deacetylase activity (H3-K14 specific); IMP:GeneDB_SPombe.
DR   GO; GO:0030702; P:chromatin silencing at centromere; IMP:GeneDB_SPombe.
DR   GO; GO:0000183; P:chromatin silencing at rDNA; IMP:GeneDB_SPombe.
DR   GO; GO:0030466; P:chromatin silencing at silent mating-type c...; IMP:GeneDB_SPombe.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IMP:GeneDB_SPombe.
DR   GO; GO:0016575; P:histone deacetylation; IMP:GeneDB_SPombe.
DR   GO; GO:0000122; P:negative regulation of transcription from R...; IMP:GeneDB_SPombe.
DR   GO; GO:0016584; P:nucleosome positioning; IMP:GeneDB_SPombe.
DR   GO; GO:0031060; P:regulation of histone methylation; IMP:GeneDB_SPombe.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR019154; Arb2_domain.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR017321; Hist_deAcase_II_yeast.
DR   Gene3D; G3DSA:3.40.800.20; His_deacetylse; 1.
DR   PANTHER; PTHR10625; His_deacetylse; 1.
DR   Pfam; PF09757; Arb2; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037919; HDAC_II_yeast; 1.
DR   PRINTS; PR01270; HDASUPER.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Complete proteome; Hydrolase; Nucleus; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    687       Histone deacetylase clr3.
FT                                /FTId=PRO_0000114739.
FT   REGION       55    385       Histone deacetylase.
FT   ACT_SITE    195    195       By similarity.
FT   MUTAGEN     232    232       D->N: No activity; weak silencing defect.
SQ   SEQUENCE   687 AA;  76792 MW;  6B0E4184A056D899 CRC64;
     MLASNSDGAS TSVKPSDDAV NTVTPWSILL TNNKPMSGSE NTLNNESHEM SQILKKSGLC
     YDPRMRFHAT LSEVDDHPED PRRVLRVFEA IKKAGYVSNV PSPSDVFLRI PAREATLEEL
     LQVHSQEMYD RVTNTEKMSH EDLANLEKIS DSLYYNNESA FCARLACGSA IETCTAVVTG
     QVKNAFAVVR PPGHHAEPHK PGGFCLFNNV SVTARSMLQR FPDKIKRVLI VDWDIHHGNG
     TQMAFYDDPN VLYVSLHRYE NGRFYPGTNY GCAENCGEGP GLGRTVNIPW SCAGMGDGDY
     IYAFQRVVMP VAYEFDPDLV IVSCGFDAAA GDHIGQFLLT PAAYAHMTQM LMGLADGKVF
     ISLEGGYNLD SISTSALAVA QSLLGIPPGR LHTTYACPQA VATINHVTKI QSQYWRCMRP
     KHFDANPKDA HVDRLHDVIR TYQAKKLFED WKITNMPILR DSVSNVFNNQ VLCSSNFFQK
     DNLLVIVHES PRVLGNGTSE TNVLNLNDSL LVDPVSLYVE WAMQQDWGLI DINIPEVVTD
     GENAPVDILS EVKELCLYVW DNYVELSISK NIFFIGGGKA VHGLVNLASS RNVSDRVKCM
     VNFLGTEPLV GLKTASEEDL PTWYYRHSLV FVSSSNECWK KAKRAKRRYG RLMQSEHTET
     SDMMEQHYRA VTQYLLHLLQ KARPTSQ
//