HDT3_MAIZE
ID HDT3_MAIZE Reviewed; 300 AA.
AC Q9M4U4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Histone deacetylase HDT3;
DE AltName: Full=Histone deacetylase 2c;
DE Short=HD2c;
DE AltName: Full=Zm-HD2c;
GN Name=HDT3; Synonyms=HD2C;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11469594; DOI=10.1007/s004250000506;
RA Dangl M., Brosch G., Haas H., Loidl P., Lusser A.;
RT "Comparative analysis of HD2 type histone deacetylases in higher plants.";
RL Planta 213:280-285(2001).
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 -!- SUBUNIT: Multimer. Possibly forms a homotrimer with HDT1 and/or HDT2
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone deacetylase HD2 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF254073; AAF68625.1; -; mRNA.
DR AlphaFoldDB; Q9M4U4; -.
DR SMR; Q9M4U4; -.
DR STRING; 4577.GRMZM2G159032_P01; -.
DR PaxDb; Q9M4U4; -.
DR PRIDE; Q9M4U4; -.
DR eggNOG; ENOG502QVH6; Eukaryota.
DR SABIO-RK; Q9M4U4; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9M4U4; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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 Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..300
FT /note="Histone deacetylase HDT3"
FT /id="PRO_0000195210"
FT ZN_FING 274..297
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 98..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..113
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 32457 MW; 62F6C4148EB1E1FE CRC64;
MEFWGLEVKP GSTVKCEPGY GFVLHLSQAA LGESKKSDNA LMYVKIDDQK LAIGTLSVDK
NPHIQFDLIF DKEFELSHTS KTTSVFFTGY KVEQPFEEDE MDLDSEDEDE ELNVPAVKEN
GKADEKKQKS QEKAVAAPSK SSPDSKKSKD DDDSDEDETD DSDEDETDDS DEGLSPEEGD
DDSSDEDDTS DDEEEDTPTP KKPEVGKKRA AESSVLKTPL SDKKAKVATP SSQKTGGKKG
AAVHVATPHP AKGKTIVNND KSVKSPKSAP KSGVPCKSCS KSFISETAPQ AHSKAKHGGK
