ID HDA6_CAEEL Reviewed; 955 AA. AC Q20296; Q9BI90; Q9BI91; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2003, sequence version 2. DT 16-JUN-2009, entry version 58. DE RecName: Full=Histone deacetylase 6; DE EC=3.5.1.98; GN Name=hda-6; ORFNames=F41H10.6; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Probable histone deacetylase. Histone deacetylases are CC responsible for the deacetylation of lysine residues on the N- CC 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 CC progression and developmental events. Histone deacetylases act via CC the formation of large multiprotein complexes (By similarity). CC -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of CC a histone to yield a deacetylated histone. CC -!- SUBCELLULAR LOCATION: Nucleus (Probable). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=b; CC IsoId=Q20296-1; Sequence=Displayed; CC Note=Derived from EST data. No experimental confirmation CC available; CC Name=a; CC IsoId=Q20296-2; Sequence=VSP_007436, VSP_007437; CC Note=Derived from EST data. No experimental confirmation CC available; CC -!- SIMILARITY: Belongs to the histone deacetylase family. Type 2 CC subfamily. CC -!- SIMILARITY: Contains 1 UBP-type zinc finger. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U61954; AAK29809.1; -; Genomic_DNA. DR EMBL; U61954; AAK29810.1; -; Genomic_DNA. DR RefSeq; NP_500787.1; -. DR UniGene; Cel.12964; -. DR PRIDE; Q20296; -. DR Ensembl; F41H10.6; Caenorhabditis elegans. DR GeneID; 177316; -. DR WormBase; WBGene00018319; F41H10.6. DR WormPep; F41H10.6a; CE20772. DR WormPep; F41H10.6b; CE25887. DR OMA; Q20296; QGQGYTI. DR NextBio; 896234; -. DR ArrayExpress; Q20296; -. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR000286; His_deacetylse. DR InterPro; IPR001607; Znf_UBP. DR Gene3D; G3DSA:3.40.800.20; His_deacetylse; 2. DR PANTHER; PTHR10625; His_deacetylse; 1. DR Pfam; PF00850; Hist_deacetyl; 2. DR Pfam; PF02148; zf-UBP; 1. DR PRINTS; PR01270; HDASUPER. DR PROSITE; PS50271; ZF_UBP; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Chromatin regulator; Complete proteome; KW Hydrolase; Metal-binding; Nucleus; Repeat; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 955 Histone deacetylase 6. FT /FTId=PRO_0000114743. FT ZN_FING 873 934 UBP-type. FT REGION 15 337 Histone deacetylase 1. FT REGION 425 749 Histone deacetylase 2. FT ACT_SITE 146 146 1 (By similarity). FT ACT_SITE 561 561 2 (By similarity). FT VAR_SEQ 797 863 VTPSNYGLDIDDEAYDDDSIDMADQSSSSGSSSSSTRPSHN FT LEIMDSGPAHAVVPLATCPHLKEVKP -> IIIGSVLNSKL FT INKNGKSSAATLKVKGKAATDPVKQADDSRRYNTRRRRSAN FT DEVEDVMEKLENMKL (in isoform a). FT /FTId=VSP_007436. FT VAR_SEQ 864 955 Missing (in isoform a). FT /FTId=VSP_007437. SQ SEQUENCE 955 AA; 106749 MW; 315C314B5ACC9E0E CRC64; MLFEDRQKNR STGPTLIGFN QTQNEHENTV CPTHPESSDR ILKIKEALTK TKILEKCTVL TNFLEIDDAD LEVTHDKSMV KDLMESEKKT QEDINSQCEK YDSVFMTENS MKVAKDGVAC VRDLTNRIMA NEASNGFAVV RPPGHHADSV SPCGFCLFNN VAQAAEEAFF SGAERILIVD LDVHHGHGTQ RIFYDDKRVL YFSIHRHEHG LFWPHLPESD FDHIGSGKGL GYNANLALNE TGCTDSDYLS IIFHVLLPLA TQFDPHFVII SAGFDALLGD PLGGMCLTPD GYSHILYHLK SLAQGRMLVV LEGGYNHQIS AVAVQRCVRV LLGYAPFSIE LNEAPKESTV DSCVSLVSVL RHHWNCFDYF PSRTSLRLAQ WPIVNTKVIY NYDPTTRRAD TGEIIQDELA STEFTASDVI PTENMETLIY FNEGDDAHFD LEEDNHPEKP ARTRRILKTL RESGVLEKCV DRNCERIATN EEIRLVHTKK MLEHLRTTET MKDEELMEEA EKEFNSIYLT RDTLKVARKA VGAVLQSVDE IFEKDAGQRN ALVIVRPPGH HASASKSSGF CIFNNVAVAA KYAQRRHKAK RVLILDWDVH HGNGTQEIFY EDSNVMYMSI HRHDKGNFYP IGEPKDYSDV GEGAGEGMSV NVPFSGVQMG DNEYQMAFQR VIMPIAYQFN PDLVLISAGF DAAVDDPLGE YKVTPETFAL MTYQLSSLAG GRIITVLEGG YNLTSISNSA QAVCEVLQNR SMLRRLREEK EQFATKPQKI ESSCIKTIRE VCAVQQKYWS ILKGFQVTPS NYGLDIDDEA YDDDSIDMAD QSSSSGSSSS STRPSHNLEI MDSGPAHAVV PLATCPHLKE VKPLPPAKIN ARTACSECQI GAEVWTCLTC YKYNCGRFVN EHAMMHHLSS SHPMALSMAD LSVWCYPCDS YVHNPALIGA KSAAHESKFG ETMPS //