ID A0A2Y9P8M9_DELLE Unreviewed; 1043 AA.
AC A0A2Y9P8M9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
GN Name=HDAC9 {ECO:0000313|RefSeq:XP_022443384.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022443384.1};
RN [1] {ECO:0000313|RefSeq:XP_022443384.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022443384.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|PIRNR:PIRNR037911}.
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 Evidence={ECO:0000256|ARBA:ARBA00001028,
CC ECO:0000256|PIRNR:PIRNR037911};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037911}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00007738,
CC ECO:0000256|PIRNR:PIRNR037911}.
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DR RefSeq; XP_022443384.1; XM_022587676.2.
DR AlphaFoldDB; A0A2Y9P8M9; -.
DR STRING; 9749.A0A2Y9P8M9; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd10163; ClassIIa_HDAC9_Gln-rich-N; 1.
DR CDD; cd11681; HDAC_classIIa; 1.
DR Gene3D; 6.10.250.1550; -; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR046949; HDAC4/5/7/9.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364:SF12; HISTONE DEACETYLASE 9; 1.
DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR Pfam; PF12203; HDAC4_Gln; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037911};
KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 6..96
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 631..949
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 82..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 760
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 623
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 625
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 631
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 708
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 933
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1043 AA; 114716 MW; 41A727F7BC2E944C CRC64;
MMMPVVDPVV REKQLQQELL LIQQQQQIQK QLLIAEFQKQ HENLTRQHQA QLQEHIKLQQ
ELLAIKQQQE LLEKEQKLEQ QRQEQEVERH RREQQLPPLR GKDRGRESKR HQGAVASTEV
KQKLQEFLLS KSATKDTPTN GKNHSVSRHP KLWYTAAHHT SLDQSSPPLS GTSPSYKYTL
PGAQDAKDDF PLRKTASEPN LKVRSRLKQK VAERRSSPLL RRKDGNVVTS FKKRMFEVTE
SSVSSSSPGS GPSSPNNGPT GNVTENETSV LPPTPQAEKM VSQQRILIHE DSMNLLSLYT
SPSLPNITLG LPAVPAQLNA SNSLKEKQKC ETQTLRQGVP LPGQYGGSIP ASSSHPHVTL
EGKPNSSHQA LLQHLLLKEQ MRQQKLLVAG GVPLHPQSPL ATKERISPGI RGTHKLPRHR
PLNRTQSAPL PQSTLAQLVI QQQHQQFLEK QKQYQQQIHM NKLLSKSIEQ LKQPGSHLEE
AEEELQGDQA MQEDRAPSSG NSTRSDSSAC VDDTLGQVGA VKVKEEPVDS DEDAQIQEME
SGEQAAFMQQ QPFLEPQHAR ALSVRPAQPA ADGMDGLEKH RLVSRTHSSP AACILPHPAM
DCHLLPGSAT GIAYDPLMLK HQCICGNSTT HPEHAGRIQS IWSRLQETGL LNKCERIQGR
KASLEEIQLV HSEHHSLLYG TNPLDGQKLD PRTLLGDSSQ KFFSSLPCGG LGVDSDTIWN
ELHSSGAARM AVGCVIELAS KVASGELKNG FAVVRPPGHH AEESTAMGFC FFNSVAITAK
YLRDQLNISK ILIVDLDVHH GNGTQQAFYA DPSILYISLH RYDEGNFFPG SGAPNEVGTG
LGEGYNINIA WTGGLDPPMG DTEYLEAFRT IVKPVAKEFD PDMVLVSAGF DALEGHAPPL
GGYKVTAKCF GHLTKQLMTL ADGHVVLALE GGHDLTAICD ASEACVNALL GNELEPLAED
ILQQTPNMNA VISLQKIIEI QSKYWKSVRT VSVPRGCALA GAQLQEETET VSALASLTVD
VEQPFAREDN RTAGEPMEEE PAL
//
