HDAC9_XENLA
ID HDAC9_XENLA Reviewed; 596 AA.
AC Q9YGY4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Histone deacetylase 9;
DE EC=3.5.1.98;
DE AltName: Full=Histone deacetylase-related protein;
DE AltName: Full=MEF2-interacting transcription repressor MITR;
GN Name=hdac9; Synonyms=hdrp, mitr;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MEF2, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=10487760; DOI=10.1093/emboj/18.18.5085;
RA Sparrow D.B., Miska E.A., Langley E., Reynaud-Deonauth S., Kotecha S.,
RA Towers N., Spohr G., Kouzarides T., Mohun T.J.;
RT "MEF-2 function is modified by a novel co-repressor, MITR.";
RL EMBO J. 18:5085-5098(1999).
RN [2]
RP IDENTIFICATION.
RX PubMed=10655483; DOI=10.1073/pnas.97.3.1056;
RA Zhou X., Richon V.M., Rifkind R.A., Marks P.A.;
RT "Identification of a transcriptional repressor related to the noncatalytic
RT domain of histone deacetylases 4 and 5.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000).
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. {ECO:0000269|PubMed:10487760}.
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 (By similarity). Interacts with mef2. {ECO:0000250,
CC ECO:0000269|PubMed:10487760}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:10487760}.
CC -!- DEVELOPMENTAL STAGE: Broadly expressed at low levels at all stages.
CC {ECO:0000269|PubMed:10487760}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10167.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z97214; CAB10167.1; ALT_INIT; mRNA.
DR RefSeq; NP_001079307.1; NM_001085838.1.
DR AlphaFoldDB; Q9YGY4; -.
DR SMR; Q9YGY4; -.
DR BioGRID; 97196; 1.
DR GeneID; 378615; -.
DR KEGG; xla:378615; -.
DR CTD; 378615; -.
DR Xenbase; XB-GENE-865808; hdac9.S.
DR OMA; NGFTHSA; -.
DR OrthoDB; 585259at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 378615; Expressed in brain and 12 other tissues.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:InterPro.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
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 1: Evidence at protein level;
KW Chromatin regulator; Hydrolase; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..596
FT /note="Histone deacetylase 9"
FT /id="PRO_0000280538"
FT REGION 132..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..222
FT /note="Interaction with mef2"
FT REGION 214..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 67307 MW; 4E4BD92BAC605E84 CRC64;
MLQTIYESES YFSSDGVAGR EQLLAEQRMH AMIGKDIKSE FPIGLESISP LDLRTDLRTA
VPVGDPGLRE KQLQQELLII KQQQQIQKQL LIAEFQKQHE NLTRQHQVQL QEHLKLQQEL
LAMKQQQELL EREKEQKMEQ QRKEQEAERH RQEQQLCHPR SKDRVKERAV ASTEVKQKLQ
EFILSKSATK EPLTNGTSHS MGRHPKLWYT AAHHTSLDQS SPPPSGTSPT YKCPPPGNQD
DFPLRKTASE PNLKVRSRLK QKVVERRSSP LLRRKDSIVS SSYKKRIFEV AESSVSSSSP
VSGPSSPNNG PVAMEAEHET PVLSVNSRIE NLVSHHHLVH HERSLSLLNL YTSPSLPNIT
LGLHATATQL NTSSSLKEQQ KYDPQAPRQG VSMAGQYAGG IPTSSNHVSL EGKANSHQAI
LQHLLLKEQM RQQKILASGG TPVLHQSPLA AKDRVSPAGR VAHKLPRHRP LHRTQSAPLP
QSTLAQLVIQ QQHQQFLEKQ KQYQQQIHMN KILSKSIEQL RQPEGHLEEA EEDLHGDNLM
QEKSSSIDNT RSYSSTDLRT GPFGSVKVKE EPPDSENEIK THLQSEQKSV FAQQVT
