ID HDAC4_CHICK Reviewed; 1080 AA. AC P83038; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 14-AUG-2001, sequence version 1. DT 02-SEP-2026, entry version 143. DE RecName: Full=Histone deacetylase 4 {ECO:0000250|UniProtKB:P56524}; DE Short=HD4; DE EC=3.5.1.98 {ECO:0000250|UniProtKB:P56524}; GN Name=HDAC4; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Takechi S., Azuma R., Nakayama T.; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000250|UniProtKB:P56524}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + CC acetate; 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:0000250|UniProtKB:P56524}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197; CC Evidence={ECO:0000250|UniProtKB:P56524}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6NZM9}. 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; AB052839; BAB60957.1; -; mRNA. DR RefSeq; NP_989644.1; NM_204313.2. DR AlphaFoldDB; P83038; -. DR SMR; P83038; -. DR BioGRID; 675230; 1. DR FunCoup; P83038; 1804. DR STRING; 9031.ENSGALP00000033098; -. DR PaxDb; 9031-ENSGALP00000033098; -. DR Ensembl; ENSGALT00010033011.1; ENSGALP00010019516.1; ENSGALG00010013697.1. DR GeneID; 374207; -. DR KEGG; gga:374207; -. DR CTD; 9759; -. DR VEuPathDB; HostDB:geneid_374207; -. DR eggNOG; KOG1343; Eukaryota. DR GeneTree; ENSGT00940000157440; -. DR InParanoid; P83038; -. DR OrthoDB; 424012at2759; -. DR PhylomeDB; P83038; -. DR Reactome; R-GGA-350054; Notch-HLH transcription pathway. DR Reactome; R-GGA-4090294; SUMOylation of intracellular receptors. DR Reactome; R-GGA-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-GGA-8951936; RUNX3 regulates p14-ARF. DR PRO; PR:P83038; -. DR Proteomes; UP000000539; Chromosome 7. DR Bgee; ENSGALG00000004288; Expressed in cerebellum and 12 other cell types or tissues. DR GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; TAS:UniProtKB. DR GO; GO:0004407; F:histone deacetylase activity; TAS:UniProtKB. DR GO; GO:0141221; F:histone deacetylase activity, hydrolytic mechanism; ISS:UniProtKB. DR GO; GO:0042113; P:B cell activation; TAS:UniProtKB. DR GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB. DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; TAS:UniProtKB. DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; TAS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro. DR GO; GO:0007399; P:nervous system development; TAS:UniProtKB. DR CDD; cd10162; ClassIIa_HDAC4_Gln-rich-N; 1. DR CDD; cd10006; HDAC4; 1. DR FunFam; 3.40.800.20:FF:000002; Histone deacetylase; 1. DR Gene3D; 6.10.250.1550; -; 1. DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1. DR InterPro; IPR046949; HDAC4/5/7/9. DR InterPro; IPR000286; HDACs. DR InterPro; IPR023801; His_deacetylse_dom. DR InterPro; IPR037138; His_deacetylse_dom_sf. DR InterPro; IPR024643; Hist_deacetylase_Gln_rich_N. DR InterPro; IPR023696; Ureohydrolase_dom_sf. DR PANTHER; PTHR45364:SF13; HISTONE DEACETYLASE; 1. DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1. DR Pfam; PF12203; HDAC4_Gln; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PIRSF; PIRSF037911; HDAC_II_euk; 1. DR PRINTS; PR01270; HDASUPER. DR SUPFAM; SSF52768; Arginase/deacetylase; 1. PE 2: Evidence at transcript level; KW Chromatin regulator; Hydrolase; Metal-binding; Nucleus; Reference proteome; KW Repressor; Transcription; Transcription regulation; Zinc. FT CHAIN 1..1080 FT /note="Histone deacetylase 4" FT /id="PRO_0000114700" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 132..165 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 205..312 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 506..527 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 558..579 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 622..646 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 651..1080 FT /note="Histone deacetylase" FT REGION 1055..1080 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 348..353 FT /note="PxLPxI/L" FT /evidence="ECO:0000250|UniProtKB:P56524" FT COMPBIAS 132..162 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 205..224 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 233..244 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 258..273 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 289..312 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 509..527 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 560..571 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 625..637 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 799 FT /evidence="ECO:0000250" FT BINDING 663 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 665 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 671 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 747 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" SQ SEQUENCE 1080 AA; 119468 MW; B6416E2C43F1428C CRC64; MSSQSHPDGL SGRDQPVELL NPPRVNHMPS SVDVSTALPL QVAPTSVPMD LRLDHQFPMP VTEPTLREQQ LQQELLALKQ KQQIQRQILI AEFQRQHEQL SRQHEAQLHE HIKQQEMLAM KHQQELLEHQ RKLEQHRQEQ ELEKQHREQK LQQLKNKEKG KESAVASTEV KMKLQEFVLN KKKALAHRNL NHCISSDPRF WYGKTQHSSL DQSSPPQSGV SGTYNHPVLG MYDSKDDFPL RKTASEPNLK LRSRLKQKVA ERRSSPLLRR KDGPVVTALK KRPLDVTDSA CNSAPGSGPS SPNNSSNNIS AENGITGSVT SIQAETSLAH RLVNREGSVT QLPLYTSPSL PNITLGLPAT GPSSGGSAQQ DAERLAIPAL QQRISLFPGT HLTPYLSTTT LERDGGTAHN PLLQHMVLLE QPTAQTPLVT GLPLHAQSLV GGERVSPSIH KLRQHRPLGR TQSAPLPQNA QALQQLVIQQ QHQQFLEKHK QQFQQQQLHI NKIISKPNEP ARQHESHPEE TEEELREHQA LLEEPYSDRV SSQKEVPGLA NMVQVKQEPI ESDEEEAEPQ QELESGQRQA EQELLFRQQA LLLEQQRIHQ LRNYQASLEA AGMPVSFGGH RPLSRAQSSP ASATFPMSVQ EPPTKPRFTT GLVYDTLMLK HQCTCGNTNS HPEHAGRIQS IWSRLQETGL RGKCECIRGR KATLEELQTV HSEAHTLLYG TNPLNRQKLD SKKLLGSLTS MFVRLPCGGV GVDSDTIWNE VHSSGAARLA VGCVIELVFK VATGELKNGF AVVRPPGHHA EESTPMGFCY FNSVAIAAKL LQQRLNVSKI LIVDWDVHHG NGTQQAFYND PNVLYISLHR YDDGNFFPGS GAPDEVGTGA GVGFNVNMAF TGGLDPPMGD TEYLTAFRTV VMPIANEFAP DVVLVSSGFD AVEGHPTPLG GYNLSAKCFG YLTKQLMGLA GGRVVLALEG GHDLTAICDA SEACVSALLG NELDPLPEKV LQQRANANAV HSMEKVIEIH SKYWHSLQRY ASTVGYSLVE AQKCENEEAE TVTAMASLSV GVKPAEKRPD DEPMEEEPPL //