HDA9B_DANRE
ID HDA9B_DANRE Reviewed; 582 AA.
AC Q6PBI4; Q6TEP8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Histone deacetylase 9-B;
DE EC=3.5.1.98;
GN Name=hdac9b; Synonyms=hdac9;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Devoided of intrinsic deacetylase activity, promotes the
CC deacetylation of lysine residues on the N-terminal part of the core
CC histones (H2A, H2B, H3 and H4) by recruiting other histone
CC deacetylases. Histone deacetylation gives a tag for epigenetic
CC repression and plays an important role in transcriptional regulation,
CC cell cycle progression and developmental events. Represses MEF2-
CC dependent transcription (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. Interacts with mef2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PBI4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PBI4-2; Sequence=VSP_029171, VSP_029172;
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ97977.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAQ97977.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AY423001; AAQ97977.1; ALT_SEQ; mRNA.
DR EMBL; BC059696; AAH59696.1; -; mRNA.
DR RefSeq; NP_957110.2; NM_200816.2. [Q6PBI4-1]
DR AlphaFoldDB; Q6PBI4; -.
DR SMR; Q6PBI4; -.
DR STRING; 7955.ENSDARP00000073611; -.
DR PaxDb; Q6PBI4; -.
DR GeneID; 393789; -.
DR KEGG; dre:393789; -.
DR CTD; 393789; -.
DR ZFIN; ZDB-GENE-040109-7; hdac9b.
DR eggNOG; KOG1343; Eukaryota.
DR InParanoid; Q6PBI4; -.
DR OrthoDB; 585259at2759; -.
DR PhylomeDB; Q6PBI4; -.
DR PRO; PR:Q6PBI4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:InterPro.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0001525; P:angiogenesis; IMP:ZFIN.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR GO; GO:0001945; P:lymph vessel development; IMP:ZFIN.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; IMP:ZFIN.
DR GO; GO:0060215; P:primitive hemopoiesis; IMP:ZFIN.
DR GO; GO:0001944; P:vasculature development; IMP:ZFIN.
DR InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR017320; Histone_deAcase_II_euk.
DR PANTHER; PTHR45364; PTHR45364; 1.
DR Pfam; PF12203; HDAC4_Gln; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromatin regulator; Hydrolase; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..582
FT /note="Histone deacetylase 9-B"
FT /id="PRO_0000280537"
FT REGION 146..195
FT /note="Interaction with mef2"
FT /evidence="ECO:0000250"
FT REGION 189..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 140..142
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15520368"
FT /id="VSP_029171"
FT VAR_SEQ 182..183
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15520368"
FT /id="VSP_029172"
FT CONFLICT 306
FT /note="E -> K (in Ref. 1; AAQ97977)"
FT /evidence="ECO:0000305"
FT CONFLICT 364..365
FT /note="AV -> PD (in Ref. 1; AAQ97977)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="S -> I (in Ref. 1; AAQ97977)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="P -> T (in Ref. 1; AAQ97977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 65117 MW; BD2CEF4E205C5EDD CRC64;
MHNVNNSVDI KPEVPLALDP GSPLDLRTDI RMQGSASEVT VWERQLQQEL LLIQKQQQIQ
KQLLITEFQK QHENLVRQHQ AQIQEHLKLQ QELHVMKQQQ EQLEKERKLE LQSQERELER
HRREQQVLVL RNRERTRESL TGAVASNEVK QKLQEFLLSK STKDITLNGI PQKITQSSKL
WYTASHHTSL EQSSPPLGGA SSSCKISLPS PQDYRDDFPL RKTVSEPNLK VRSRLKQKVA
ERRSSPLLRR KEGNIMTPFK KRALELLEST ASSSAPGSGP SSPNGACSAL GAENGPSSLP
VTTRTERWPS QSRLLGPESS VSMLNLYTSP SLPNISLGFS AASSPISAAL GLQEKHVDNG
AVSAVIQGLP TQLLGPVPLS VMETKVSSSH QALLQHLLQK EQLRHQKILS SGQSPVHPPS
PLAMMENSPS STRPKLPRHR PLNRTQSAPL PQSTLAQLVI QQQHQNFLEK QKQYQQQVHI
NKMLSKSIEQ LRQPNVHLQE SEEEEGEDCQ EHAMQEESSP SGGVIRKHSP QNTSRSPTIP
LDSHPGVIRV KEEPGASDDE TMANQSSYIH QVKGRMVIQA MI
