ID G1T7F7_RABIT Unreviewed; 1068 AA.
AC G1T7F7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 24-JAN-2024, entry version 72.
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:ENSOCUP00000012429.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000012429.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000012429.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000012429.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000012429.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000012429.3};
RG Ensembl;
RL Submitted (JUL-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 EMBL; AAGW02036139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02036140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02036141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02036142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02036143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02036144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02036145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02036146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02036147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02036148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1T7F7; -.
DR SMR; G1T7F7; -.
DR STRING; 9986.ENSOCUP00000012429; -.
DR PaxDb; 9986-ENSOCUP00000012429; -.
DR Ensembl; ENSOCUT00000014455.4; ENSOCUP00000012429.3; ENSOCUG00000014444.4.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000160307; -.
DR HOGENOM; CLU_006530_2_0_1; -.
DR InParanoid; G1T7F7; -.
DR OMA; EYLEAFX; -.
DR TreeFam; TF106174; -.
DR Proteomes; UP000001811; Chromosome 10.
DR Bgee; ENSOCUG00000014444; Expressed in adult mammalian kidney and 16 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0034739; F:histone H4K16 deacetylase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0001818; P:negative regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
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; IPR017320; Histone_deAcase_II_euk.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364:SF1; 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|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037911-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
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 37..127
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 656..974
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 113..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 785
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 656
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 733
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 958
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1068 AA; 117332 MW; 64DB0E791A344BF7 CRC64;
MHSMISSVDV KSEVPVGLEP ISPLDLRTDL RMMMPAVDPV VREKQLQQEL LLIQQQQQIQ
KQLLIAEFQK QHENLTRQHQ AQLQEHIKLQ QELLAIKQQQ ELLEKEQKLE QQRQEQEVER
HRRELQLPPL RGKDRGRERA VASTEVKQKL QEFLLSKSAT KDTPANGKNH SVSRHPKLWY
TAAHHTSLDQ SSPPLSGTSP SYKYTLPGAQ DTKDDFPLRK TASEPNLKVR SRLKQKVAER
RSSPLLRRKD GNVVTSFKKR MFEVTESSVS SSSPGSGPSS PNNGPTGNVT ENETSVLPPT
PHAEQMVSQQ RILIHEDSMN LLSLYTSPSL PNITLGLPAV SSQLNASNSL KEKQKCETQT
LRPGVALPGQ YGASMAASSS HPHAAALEGK PNSSHQALLQ HLLLKEQMRQ QKLLVTGGVA
LHPQSPLATK ERISPGIRGS HKLPRHRPLN RTQSAPLPQS TLAQLVIQQQ HQQFLEKQKQ
YQQQIHMNKL LSKSIEQLKA PGSHLEEAEE ELQGDQAMQE DRAPSSGSST RSDSACVDDT
LGQVGAVKIK EEPVDSDEDA QIQEMESGEQ AAFMQQPFLE PQHTRARSMR QAQLAVVGTD
GLDKHRLVSR AHSSPAASVL PHPAMDRPLQ PGPATGIAYD PLMLKHQCIC GNATTHPEHA
GRIQSIWSRL QETGLLNKCE RIQGRKASLE EIQLVHSEHH SLLYGTNPLD GQKLDPRILL
GDDSQKFFSS LPCGGLGVDT DTVWNELHSS GAARMAVGCV IELASKVASG ELKNGFAVVR
PPGHHAEEST AMGFCFFNSV AITAKYLRDQ LNISKILIVD LDVHHGNGTQ QAFYADPSIL
YISLHRYDEG NFFPGSGAPN EVGTGLGEGF TINIAWTGGL DPPMGDIEYL EAFRTVVMPV
AKEFDPDLVL VSAGFDALEG HTPPLGGYKV TAKCFGHLTK QLMTLADGRV VLALEGGHDL
TAICDASEAC VNALLGNELE PLSEDVLHQT PNVNAVISLQ KIIEIQSKYW KSVRMTAMPR
GCALAGAQLQ EETETVSALA SLTVDVEQPF AQEESRTAGE PMEEEPAL
//