ID   HDAC9_CHICK             Reviewed;         594 AA.
AC   Q5ZKH6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Histone deacetylase 9;
DE            EC=3.5.1.98;
GN   Name=hdac9; ORFNames=RCJMB04_10m2;
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 [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Devoided of intrinsic deacetylase activity, promotes the
CC       deacetylation of lysine residues on the N-terminal part of the core
CC       histones (H2A, H2B, H3 and H4) by recruiting other histone
CC       deacetylases. Histone deacetylation gives a tag for epigenetic
CC       repression and plays an important role in transcriptional regulation,
CC       cell cycle progression and developmental events. Represses MEF2-
CC       dependent transcription (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   -!- SUBUNIT: Homodimer. Interacts with mef2 (By similarity). {ECO:0000250}.
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; AJ720108; CAG31767.1; -; mRNA.
DR   AlphaFoldDB; Q5ZKH6; -.
DR   SMR; Q5ZKH6; -.
DR   STRING; 9031.ENSGALP00000017619; -.
DR   PaxDb; Q5ZKH6; -.
DR   VEuPathDB; HostDB:geneid_420599; -.
DR   eggNOG; KOG1343; Eukaryota.
DR   InParanoid; Q5ZKH6; -.
DR   PhylomeDB; Q5ZKH6; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0000118; C:histone deacetylase complex; IEA:InterPro.
DR   GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003714; F:transcription corepressor activity; ISS:AgBase.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0007507; P:heart development; ISS:AgBase.
DR   GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:AgBase.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:AgBase.
DR   GO; GO:0048742; P:regulation of skeletal muscle fiber development; ISS:UniProtKB.
DR   GO; GO:0051153; P:regulation of striated muscle cell differentiation; ISS:UniProtKB.
DR   InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR   InterPro; IPR017320; Histone_deAcase_II_euk.
DR   PANTHER; PTHR45364; PTHR45364; 1.
DR   Pfam; PF12203; HDAC4_Gln; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Hydrolase; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..594
FT                   /note="Histone deacetylase 9"
FT                   /id="PRO_0000280536"
FT   REGION          113..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..193
FT                   /note="Interaction with mef2"
FT                   /evidence="ECO:0000250"
FT   REGION          187..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          265..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   594 AA;  66214 MW;  C3BA308AA746BA5E CRC64;
     MHSMISSVDV KSEVPVGLEP ISPLDLRTDL RMMVPMVDPI MREKQLQQEL LLIQQQQQIQ
     KQLLIAEFQK QHENLTRQHQ AQLQEHIKLQ QELLAIKQQQ ELLEKEQKLE QQRQEQELER
     HRREQQLPPL RGKERGRERA VASTEVKQKL QEFLLSKSAT KDSPANGKNH SVSRHPKLWY
     TAAHHTSLDQ SSPPLSGASP PYKYTLPGSQ DAKDDFPLRK TASEPNLKVR SRLKQKVTER
     RSSPLLRRKD GNVVSSFKKR LFEVTESSVS SSSPGSGPSS PSNGPTSSIT ESETSVLPSS
     IQAEHLVSQQ RLLIQDESVN LLSLYTSPSL PNITLGLPAV QSQISASSSF KEKQKGETQT
     LRPGVALAGQ YGGNLPPSST HPHVALEGKP NSSHQALLQH LLLKEQMRQQ KLLVTGAVPL
     HPQSPLAAKE RGSPGVRAAH KLPRHRPLNR TQSAPLPQST LAQLVIQQQH QQFLEKQKQY
     QQQIHMNKML SKSIEQLKQP GSHLEEAEEE LNGDHSMQEE RAPASSASIR AESSSAGEDD
     RIGQQVGAVK VKEEPPDSDE DTQTQQMESG EQAAFVQQVI GKDLAPGFVI KVII