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Database: UniProt
Entry: F6VAD3_MACMU
LinkDB: F6VAD3_MACMU
Original site: F6VAD3_MACMU 
ID   F6VAD3_MACMU            Unreviewed;       594 AA.
AC   F6VAD3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
GN   Name=HDAC9 {ECO:0000313|Ensembl:ENSMMUP00000014628.4,
GN   ECO:0000313|VGNC:VGNC:73165};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000014628.4, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000014628.4}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000014628.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000256|ARBA:ARBA00007738}.
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DR   AlphaFoldDB; F6VAD3; -.
DR   SMR; F6VAD3; -.
DR   Ensembl; ENSMMUT00000015619.4; ENSMMUP00000014628.4; ENSMMUG00000011170.4.
DR   VEuPathDB; HostDB:ENSMMUG00000011170; -.
DR   VGNC; VGNC:73165; HDAC9.
DR   GeneTree; ENSGT00940000160307; -.
DR   HOGENOM; CLU_006530_2_1_1; -.
DR   Proteomes; UP000006718; Chromosome 3.
DR   Bgee; ENSMMUG00000011170; Expressed in dorsolateral prefrontal cortex and 20 other cell types or tissues.
DR   ExpressionAtlas; F6VAD3; baseline.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR   CDD; cd10163; ClassIIa_HDAC9_Gln-rich-N; 1.
DR   Gene3D; 6.10.250.1550; -; 1.
DR   InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR   PANTHER; PTHR45364:SF12; HISTONE DEACETYLASE 9; 1.
DR   PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR   Pfam; PF12203; HDAC4_Gln; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718}.
FT   DOMAIN          38..128
FT                   /note="Histone deacetylase glutamine rich N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12203"
FT   REGION          114..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   594 AA;  66389 MW;  BDB3BB7613115B52 CRC64;
     FHSLMFGSVD VKSEVPVGLE PISPLDLRTD LRMMMPVVDP VVREKQLQQE LLLIQQQQQI
     QKQLLIAEFQ KQHENLTRQH QAQLQEHIKL QQELLAIKQQ QELLEKEQKL EQQRQEQEVE
     RHRREQQLPP LRGKDRGRER AVASTEVKQK LQEFLLSKSA TKDTPTNGKN HSVSRHPKLW
     YTAAHHTSLD QSSPPLSGTS PSYKYTLPGA QDAKDDFPLR KTASEPNLKV RSRLKQKVAE
     RRSSPLLRRK DGNVVTSFKK RMFEVTESSV SSSSPGSGPS SPNNGPTGSV TENETSVLPP
     TPHAEQMVSQ QRILIHEDSM NLLSLYTSPS LPNITLGLPA VPSQLNASNS LKEKQKCETQ
     TLRQGVPLPG QYGGSIPASS SHPHVTLEGK PPNSSHQALL QHLLLKEQMR QQKLLVAGGV
     PLHPQSPLAT KERISPGIRG THKLPRHRPL NRTQSAPLPQ STLAQLVIQQ QHQQFLEKQK
     QYQQQIHMNK LLSKSIEQLK QPGSHLEEAE EELQGDQAMQ EDRAPSSGNS TRSDSSACVD
     DTLGQVGAVK VKEEPVDSDE DAQIQEMESG EQAAFMQQVI GKDLAPGFVI KVII
//
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