HDA7_ARATH
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 03-AUG-2022, entry version 124.
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.AT5G35600.1; -.
DR PaxDb; Q9FH09; -.
DR PRIDE; Q9FH09; -.
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; locus:2157111; AT5G35600.
DR eggNOG; KOG1342; Eukaryota.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; Q9FH09; -.
DR OMA; YITCLAT; -.
DR OrthoDB; 732770at2759; -.
DR PhylomeDB; Q9FH09; -.
DR PRO; PR:Q9FH09; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH09; baseline and differential.
DR Genevisible; Q9FH09; AT.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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:0016575; P:histone deacetylation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR Gene3D; 3.40.800.20; -; 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 Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
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..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