HDA6_CAEEL
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 03-AUG-2022, entry version 149.
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}.
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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; 6.
DR STRING; 6239.F41H10.6c; -.
DR EPD; Q20296; -.
DR PaxDb; Q20296; -.
DR PeptideAtlas; Q20296; -.
DR PRIDE; 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 CTD; 177316; -.
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 Reactome; R-CEL-3214815; HDACs deacetylate histones.
DR PRO; PR:Q20296; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00018319; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q20296; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.800.20; -; 2.
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 Pfam; PF00850; Hist_deacetyl; 2.
DR Pfam; PF02148; zf-UBP; 1.
DR PRINTS; PR01270; HDASUPER.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF52768; SSF52768; 2.
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
