ID   HDT1_SOLCH              Reviewed;         269 AA.
AC   Q6V9I6;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Histone deacetylase HDT1;
DE   AltName: Full=Histone deacetylase 2a;
DE            Short=HD2a;
DE   AltName: Full=ScHD2a;
GN   Name=HDT1; Synonyms=HD2A;
OS   Solanum chacoense (Chaco potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RX   PubMed=15082924; DOI=10.1023/b:plan.0000023665.36676.89;
RA   Lagace M., Chantha S.-C., Major G., Matton D.P.;
RT   "Fertilization induces strong accumulation of a histone deacetylase (HD2)
RT   and of other chromatin-remodeling proteins in restricted areas of the
RT   ovules.";
RL   Plant Mol. Biol. 53:759-769(2003).
CC   -!- FUNCTION: Mediates the deacetylation of lysine residues on the N-
CC       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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in ovaries. Accumulates
CC       predominantly in the micropylar region of the ovule's integument.
CC       {ECO:0000269|PubMed:15082924}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during fertilization, while it is
CC       repressed during seed development. {ECO:0000269|PubMed:15082924}.
CC   -!- INDUCTION: By fertilization. {ECO:0000269|PubMed:15082924}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase HD2 family.
CC       {ECO:0000305}.
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DR   EMBL; AY346455; AAQ24532.1; -; mRNA.
DR   AlphaFoldDB; Q6V9I6; -.
DR   SMR; Q6V9I6; -.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   InterPro; IPR041232; NPL.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF17800; NPL; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Hydrolase; Metal-binding; Nucleus; Phosphoprotein;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..269
FT                   /note="Histone deacetylase HDT1"
FT                   /id="PRO_0000195211"
FT   ZN_FING         242..265
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          97..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..114
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..179
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   269 AA;  29114 MW;  58CB0A4817E46422 CRC64;
     MEFWGAEVKS GEPLTVQPGD GMVLHLSQAS LGELKKDKSE SVCLSVNIDG KKLVLGTLNS
     EKVPQQQFDL VFDRDFELSH NLKSGSVYFF GYKATNPFEE EEDDEDDYDE SDEDIPLTLA
     NSGKPEPKEA GKSNAGKDSA SGKQKVRIVE PTKDDEDESS DDDDSDMGED EDDSDDSEEE
     TPKKAEPAKR RKADSATKTP VTDKKAKLTT PQKTDGKKGG GHVATPHPSK QASKTPKSAG
     SHHCKPCNRS FGSEGALDSH SKAKHSAGK