ID G3UV76_MELGA Unreviewed; 1128 AA.
AC G3UV76;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 69.
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|Ensembl:ENSMGAP00000019750.2};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000019750.2, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000019750.2, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000019750.2}
RP IDENTIFICATION.
RG Ensembl;
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|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}.
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 AlphaFoldDB; G3UV76; -.
DR Ensembl; ENSMGAT00000019085.2; ENSMGAP00000019750.2; ENSMGAG00000010234.3.
DR GeneTree; ENSGT00940000160307; -.
DR HOGENOM; CLU_006530_2_0_1; -.
DR TreeFam; TF106174; -.
DR Proteomes; UP000001645; Chromosome 6.
DR Bgee; ENSMGAG00000010234; Expressed in heart and 15 other cell types or tissues.
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; cd10009; HDAC9; 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:SF11; HISTONE DEACETYLASE; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037911}.
FT DOMAIN 93..183
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 714..1032
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 169..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 124920 MW; 21EC38F54695241E CRC64;
MWELLKPAKN RLASFQTEPQ NLYNICQFDF IPSTAMSSTT QPDGVSGREQ LLAQQRMHSM
ISSVDVKSEV PVGLEPISPL DLRTDLRMMV PMVDPIMREK QLQQELLLIQ QQQQIQKQLL
IAEFQKQHEN LTRQHQAQLQ EHIKLQQELL AIKQQQELLE KEQKLEQQRQ EQELERHRRE
QQLPPLRGKE RVRERAVAST EVKQKLQEFL LSKSATKDSP ANGKNHSVSR HPKLWYTAAH
HTSLDQSSPP LSGASPPYKY TLPGSQDAKD DFPLRKTASE PNLKVRSRLK QKVTERRSSP
LLRRKDGNVI SSFKKRLFEV TESSVSSSSP GSGPSSPSNG PTSSITESEN SVLPSSIQAE
HLVSQQRLLI QDESVNLLSL YTSPSLPNIT LGLPAVQSQI SASSSFKEKQ KGETQTLRPG
VTLAGQYGGN IPPSSTHPHV ALEGKPNSSH QALLQHLLLK EQMRQQKLLV TGAVPLHPQS
PLAAKERVSP GIRAAHKLPR HRPLNRTQSA PLPQSTLAQL VIQQQHQQFL EKQKQYQQQI
HMNKMLSKSI EQLKQPGSHL EEAEEELNGD HSMQEERAPA SGASIRAESS SAGEDDRIGQ
QAGAVKVKEE PPDSDEDTQT QQMESGEQAA FVQQEFLVHQ RVHQLQIYQA QMATVGMAGL
DKHRLVSRTP SSPTDSTLPH PAMDQPSQHV YTTGVVYDSL MLKHQCMCGN YANHPEHAGR
IQSIWSRLQE TGLLNKCERI RGRKASLEEI QLVHSEHHSL LYGTSPLNRQ KLDPRKLLGN
VSQKLFSLLP CGGLGVDSDT VWNELHSAGA ARMAVGCVIE LAARVASREL KNGFAVVRPP
GHHAEESTAM GFCFFNSIAI TAKYLRDKLN IGKILIVDLD VHHGNGTQQA FYADPSILYV
SLHRYDEGNF FPGSGAPNEV GSGPGEGFNI NIAWTGGLDP PMGDVEYLTA FRTVIMPAAN
EFDPEIVLVS AGFDAVEGHD PPLGGYKVTA KCFGHLTKQL LKLADGRVVL ALEGGHDLTA
ICDASEACIN ALLGNELEPL PEDIVHQIPN MNAIASLKKT TEIQSKYWKS VEPYSVPVDC
ALAESQKRER EETETVSAMA SLSVDVEQCF PQESSRAAGE PMEEEPAL
//
