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 27-MAR-2024, entry version 158. DE RecName: Full=Histone deacetylase clr3; DE EC=3.5.1.98 {ECO:0000269|PubMed:17289569}; DE AltName: Full=Cryptic loci regulator 3; GN Name=clr3; ORFNames=SPBC800.03; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=9755190; DOI=10.1093/genetics/150.2.563; 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 yeast."; RL Genetics 150:563-576(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX 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., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA 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 fission RT yeast Schizosaccharomyces pombe."; RL Nat. Biotechnol. 24:841-847(2006). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CCQ1; CLR1; CLR2 AND MIT1, RP SUBCELLULAR 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 the CC N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone CC deacetylation gives a tag for epigenetic repression and plays an CC important role in transcriptional regulation, cell cycle progression CC and developmental events. Histone deacetylases act via the formation of CC large multiprotein complexes. Required for proper positioning of CC nucleosomes at heterochromatic loci and for transcriptional gene CC silencing (TGS) function of the Snf2/Hdac-containing repressor complex CC (SHREC). {ECO:0000269|PubMed:17289569}. 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 Evidence={ECO:0000269|PubMed:17289569}; CC -!- SUBUNIT: Interacts with ccq1, clr1, clr2 and mit1. CC {ECO:0000269|PubMed:17289569}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17289569}. CC Chromosome, centromere {ECO:0000269|PubMed:17289569}. Chromosome, CC telomere {ECO:0000269|PubMed:17289569}. Note=Associates with major CC heterochromatin, centromeres, sub-telomeres, rDNA and the mat locus. CC {ECO:0000269|PubMed:17289569}. CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF064207; AAD05212.1; -; Genomic_DNA. DR EMBL; CU329671; CAC01518.1; -; Genomic_DNA. DR PIR; T43797; T43797. DR RefSeq; NP_595104.1; NM_001021011.2. DR PDB; 5IKK; X-ray; 2.40 A; A=31-687. DR PDBsum; 5IKK; -. DR AlphaFoldDB; P56523; -. DR SMR; P56523; -. DR BioGRID; 277339; 161. DR DIP; DIP-59446N; -. DR IntAct; P56523; 1. DR STRING; 284812.P56523; -. DR ESTHER; schpo-clr3; Arb2_domain. DR iPTMnet; P56523; -. DR MaxQB; P56523; -. DR PaxDb; 4896-SPBC800-03-1; -. DR EnsemblFungi; SPBC800.03.1; SPBC800.03.1:pep; SPBC800.03. DR GeneID; 2540821; -. DR KEGG; spo:SPBC800.03; -. DR PomBase; SPBC800.03; clr3. DR VEuPathDB; FungiDB:SPBC800.03; -. DR eggNOG; KOG1343; Eukaryota. DR HOGENOM; CLU_007727_4_0_1; -. DR InParanoid; P56523; -. DR OMA; FVSPACY; -. DR PhylomeDB; P56523; -. DR Reactome; R-SPO-3371511; HSF1 activation. DR Reactome; R-SPO-5617833; Cilium Assembly. DR PRO; PR:P56523; -. DR Proteomes; UP000002485; Chromosome II. DR GO; GO:0000785; C:chromatin; IDA:PomBase. DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase. DR GO; GO:1990342; C:heterochromatin island; IDA:PomBase. DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central. DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase. DR GO; GO:0005730; C:nucleolus; IDA:PomBase. DR GO; GO:0005634; C:nucleus; HDA:PomBase. DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase. DR GO; GO:0033553; C:rDNA heterochromatin; IDA:PomBase. DR GO; GO:0070824; C:SHREC complex; IDA:PomBase. DR GO; GO:0140720; C:subtelomeric heterochromatin; EXP:PomBase. DR GO; GO:0004407; F:histone deacetylase activity; IDA:PomBase. DR GO; GO:0031078; F:histone H3K14 deacetylase activity; IMP:PomBase. DR GO; GO:0006325; P:chromatin organization; IMP:PomBase. DR GO; GO:0040029; P:epigenetic regulation of gene expression; IMP:PomBase. DR GO; GO:0031507; P:heterochromatin formation; IMP:PomBase. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0090053; P:positive regulation of pericentric heterochromatin formation; IMP:CACAO. DR GO; GO:0000183; P:rDNA heterochromatin formation; IMP:PomBase. DR GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IMP:PomBase. DR CDD; cd11600; HDAC_Clr3; 1. DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1. DR InterPro; IPR019154; Arb2-like_domain. DR InterPro; IPR000286; His_deacetylse. DR InterPro; IPR023801; His_deacetylse_dom. DR InterPro; IPR037138; His_deacetylse_dom_sf. DR InterPro; IPR017321; Hist_deAcase_II_yeast. DR InterPro; IPR023696; Ureohydrolase_dom_sf. DR PANTHER; PTHR10625:SF4; HISTONE DEACETYLASE 6, ISOFORM G; 1. DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1. DR Pfam; PF09757; Arb2; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PIRSF; PIRSF037919; HDAC_II_yeast; 1. DR PRINTS; PR01270; HDASUPER. DR SUPFAM; SSF52768; Arginase/deacetylase; 1. PE 1: Evidence at protein level; KW 3D-structure; Centromere; Chromatin regulator; Chromosome; Hydrolase; KW Nucleus; Reference proteome; Repressor; Telomere; Transcription; KW Transcription regulation. FT CHAIN 1..687 FT /note="Histone deacetylase clr3" FT /id="PRO_0000114739" FT REGION 55..385 FT /note="Histone deacetylase" FT ACT_SITE 195 FT /evidence="ECO:0000250" FT MUTAGEN 232 FT /note="D->N: No histone deacetylase activity; weak FT silencing defect." FT /evidence="ECO:0000269|PubMed:17289569" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 65..68 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 82..93 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 117..129 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 146..151 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 160..178 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 181..188 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 209..220 FT /evidence="ECO:0007829|PDB:5IKK" FT TURN 222..224 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 228..232 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 239..245 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 249..258 FT /evidence="ECO:0007829|PDB:5IKK" FT TURN 260..263 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 269..271 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 279..281 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 285..293 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 297..306 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 308..315 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 318..324 FT /evidence="ECO:0007829|PDB:5IKK" FT TURN 333..335 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 341..351 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 355..357 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 359..363 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 369..383 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 398..411 FT /evidence="ECO:0007829|PDB:5IKK" FT TURN 412..414 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 435..451 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 470..473 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 477..479 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 481..488 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 492..494 FT /evidence="ECO:0007829|PDB:5IKK" FT TURN 506..508 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 510..512 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 515..524 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 528..533 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 548..562 FT /evidence="ECO:0007829|PDB:5IKK" FT TURN 563..566 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 570..577 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 580..590 FT /evidence="ECO:0007829|PDB:5IKK" FT TURN 594..596 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 597..603 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 619..626 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 628..632 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 637..639 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 647..649 FT /evidence="ECO:0007829|PDB:5IKK" FT STRAND 652..654 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 660..666 FT /evidence="ECO:0007829|PDB:5IKK" FT HELIX 668..678 FT /evidence="ECO:0007829|PDB:5IKK" 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 //