ID   HDA7_ARATH              Reviewed;         409 AA.
AC   Q9FH09; A0MFJ3;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Histone deacetylase 7;
DE            EC=3.5.1.98;
GN   Name=HDA7; OrderedLocusNames=At5g35600; ORFNames=K2K18.5;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=12466527; DOI=10.1093/nar/gkf660;
RA   Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA   Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT   "Analysis of histone acetyltransferase and histone deacetylase families of
RT   Arabidopsis thaliana suggests functional diversification of chromatin
RT   modification among multicellular eukaryotes.";
RL   Nucleic Acids Res. 30:5036-5055(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16699543; DOI=10.1038/sj.cr.7310059;
RA   Fong P.M., Tian L., Chen Z.J.;
RT   "Arabidopsis thaliana histone deacetylase 1 (AtHD1) is localized in
RT   euchromatic regions and demonstrates histone deacetylase activity in
RT   vitro.";
RL   Cell Res. 16:479-488(2006).
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. May be involved in flowering induction.
CC       Histone deacetylases act via the formation of large multiprotein
CC       complexes. {ECO:0000305|PubMed:16699543}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q8GXJ1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q8GXJ1};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Low expression in flowers.
CC       {ECO:0000269|PubMed:16699543}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK28721.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF510166; AAM49768.1; -; mRNA.
DR   EMBL; AB023031; BAB09994.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93985.1; -; Genomic_DNA.
DR   EMBL; DQ447001; ABE66192.1; -; mRNA.
DR   EMBL; DQ653319; ABK28721.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_198410.1; NM_122951.1.
DR   AlphaFoldDB; Q9FH09; -.
DR   SMR; Q9FH09; -.
DR   STRING; 3702.Q9FH09; -.
DR   PaxDb; 3702-AT5G35600-1; -.
DR   ProteomicsDB; 230311; -.
DR   EnsemblPlants; AT5G35600.1; AT5G35600.1; AT5G35600.
DR   GeneID; 833525; -.
DR   Gramene; AT5G35600.1; AT5G35600.1; AT5G35600.
DR   KEGG; ath:AT5G35600; -.
DR   Araport; AT5G35600; -.
DR   TAIR; AT5G35600; HDA7.
DR   eggNOG; KOG1342; Eukaryota.
DR   HOGENOM; CLU_007727_7_4_1; -.
DR   InParanoid; Q9FH09; -.
DR   OMA; YITCLAT; -.
DR   OrthoDB; 638399at2759; -.
DR   PhylomeDB; Q9FH09; -.
DR   PRO; PR:Q9FH09; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FH09; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR   GO; GO:0009845; P:seed germination; IMP:TAIR.
DR   CDD; cd09991; HDAC_classI; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625:SF24; HISTONE DEACETYLASE 7; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   Genevisible; Q9FH09; AT.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Hydrolase; Metal-binding; Nucleus; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..409
FT                   /note="Histone deacetylase 7"
FT                   /id="PRO_0000280086"
FT   REGION          11..324
FT                   /note="Histone deacetylase"
FT   REGION          383..409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        148
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT   BINDING         267
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
FT   SITE            306
FT                   /note="Polarizes the scissile carbonyl of the substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GXJ1"
SQ   SEQUENCE   409 AA;  46017 MW;  56A4FFAF9A0734AE CRC64;
     MASLADGGKR RVSYFYEPMI GDYYYGVNQP TKPQRIRVTH NLILSYNLHR HMEINHPDLA
     DASDFEKFHS LEYINFLKSV TPETVTDPHP SVSENLKRFN VDVDWDGPVF HNLFDYCRAY
     AGGSISAAAK LNRQEADIAI NWAGGMHHVK KDKASGFGYV NDVVLAILEL LKSFKRVLYI
     EIGFPHGDEV EEAFKDTDRV MTVSFHKVGD TGDISDYGEG KGQYYSLNAP LKDGLDDFSL
     RGLFIPVIHR AMEIYEPEVI VLQCGADSLA GDPFGTFNLS IKGHGDCLQY VRSFNVPLMI
     LGGGGYTLPN VARCWCYETA IAVGEQLDND LPGNDYMKYF RPDYKLHILP TNRQNLNTRL
     DIITMRETLL AQLSLVMHAP SVPFQDTPSS SQATEAAEVD MEKRNDPRI
//