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 27-MAR-2024, entry version 158. 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; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX 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 investigating RT 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-terminal CC part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation CC gives a tag for epigenetic repression and plays an important role in CC transcriptional regulation, cell cycle progression and developmental CC events. Histone deacetylases act via the formation of large CC multiprotein complexes (By similarity). {ECO:0000250}. 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 -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=b; CC IsoId=Q20296-1; Sequence=Displayed; CC Name=a; CC IsoId=Q20296-2; Sequence=VSP_007436, VSP_007437; 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; FO081367; CCD71098.1; -; Genomic_DNA. DR EMBL; FO081367; CCD71099.1; -; Genomic_DNA. DR RefSeq; NP_500787.1; NM_068386.3. [Q20296-1] DR RefSeq; NP_500788.1; NM_068387.3. [Q20296-2] DR AlphaFoldDB; Q20296; -. DR SMR; Q20296; -. DR BioGRID; 42439; 7. DR STRING; 6239.F41H10.6c.1; -. DR EPD; Q20296; -. DR PaxDb; 6239-F41H10-6c; -. DR PeptideAtlas; Q20296; -. DR EnsemblMetazoa; F41H10.6a.1; F41H10.6a.1; WBGene00018319. [Q20296-2] DR EnsemblMetazoa; F41H10.6b.1; F41H10.6b.1; WBGene00018319. [Q20296-1] DR GeneID; 177316; -. DR KEGG; cel:CELE_F41H10.6; -. DR UCSC; Y51H1A.5.1; c. elegans. [Q20296-1] DR AGR; WB:WBGene00018319; -. DR WormBase; F41H10.6a; CE20772; WBGene00018319; hda-6. [Q20296-2] DR WormBase; F41H10.6b; CE25887; WBGene00018319; hda-6. [Q20296-1] DR eggNOG; KOG1343; Eukaryota. DR GeneTree; ENSGT00940000159563; -. DR InParanoid; Q20296; -. DR PRO; PR:Q20296; -. DR Proteomes; UP000001940; Chromosome IV. DR Bgee; WBGene00018319; Expressed in germ line (C elegans) and 4 other cell types or tissues. DR ExpressionAtlas; Q20296; baseline and differential. DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central. DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central. DR GO; GO:0033558; F:protein lysine deacetylase activity; ISS:WormBase. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 3.40.800.20; Histone deacetylase domain; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR000286; His_deacetylse. DR InterPro; IPR023801; His_deacetylse_dom. DR InterPro; IPR037138; His_deacetylse_dom_sf. DR InterPro; IPR023696; Ureohydrolase_dom_sf. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR001607; Znf_UBP. DR PANTHER; PTHR10625:SF31; HISTONE DEACETYLASE 6; 1. DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1. DR Pfam; PF00850; Hist_deacetyl; 2. DR Pfam; PF02148; zf-UBP; 1. DR PRINTS; PR01270; HDASUPER. DR SMART; SM00290; ZnF_UBP; 1. DR SUPFAM; SSF52768; Arginase/deacetylase; 2. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50271; ZF_UBP; 1. PE 3: Inferred from homology; KW Alternative splicing; Chromatin regulator; Hydrolase; Metal-binding; KW Nucleus; Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..955 FT /note="Histone deacetylase 6" FT /id="PRO_0000114743" FT ZN_FING 853..951 FT /note="UBP-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT REGION 15..337 FT /note="Histone deacetylase 1" FT REGION 425..749 FT /note="Histone deacetylase 2" FT REGION 815..840 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 896..898 FT /note="Ubiquitin binding" FT /evidence="ECO:0000250" FT REGION 924..931 FT /note="Ubiquitin binding" FT /evidence="ECO:0000250" FT COMPBIAS 817..838 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 146 FT /note="1" FT /evidence="ECO:0000250" FT ACT_SITE 561 FT /note="2" FT /evidence="ECO:0000250" FT BINDING 855 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 857 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 875 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 878 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 887 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 890 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 895 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 902 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 906 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 912 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 925 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 928 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT VAR_SEQ 797..863 FT /note="VTPSNYGLDIDDEAYDDDSIDMADQSSSSGSSSSSTRPSHNLEIMDSGPAHA FT VVPLATCPHLKEVKP -> IIIGSVLNSKLINKNGKSSAATLKVKGKAATDPVKQADDS FT RRYNTRRRRSANDEVEDVMEKLENMKL (in isoform a)" FT /evidence="ECO:0000305" FT /id="VSP_007436" FT VAR_SEQ 864..955 FT /note="Missing (in isoform a)" FT /evidence="ECO:0000305" FT /id="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 //