HDAC4_CHICK
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 03-AUG-2022, entry version 127.
DE RecName: Full=Histone deacetylase 4;
DE Short=HD4;
DE EC=3.5.1.98;
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 (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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; AB052839; BAB60957.1; -; mRNA.
DR RefSeq; NP_989644.1; NM_204313.1.
DR RefSeq; XP_015144580.1; XM_015289094.1.
DR AlphaFoldDB; P83038; -.
DR SMR; P83038; -.
DR BioGRID; 675230; 1.
DR STRING; 9031.ENSGALP00000033098; -.
DR PaxDb; P83038; -.
DR Ensembl; ENSGALT00000033739; ENSGALP00000033098; ENSGALG00000004288.
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 OMA; AEESTPX; -.
DR OrthoDB; 1484694at2759; -.
DR PhylomeDB; P83038; -.
DR PRO; PR:P83038; -.
DR Proteomes; UP000000539; Chromosome 7.
DR Bgee; ENSGALG00000004288; Expressed in cerebellum and 12 other tissues.
DR ExpressionAtlas; P83038; 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:0140297; F:DNA-binding transcription factor binding; TAS:UniProtKB.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0070933; P:histone H4 deacetylation; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; 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; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR033660; HDAC4/7.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR017320; Histone_deAcase_II_euk.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364; PTHR45364; 1.
DR PANTHER; PTHR45364:SF3; PTHR45364:SF3; 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; SSF52768; 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 205..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1080
FT /note="Basic and acidic 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
