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Database: UniProt
Entry: G1T7F7_RABIT
LinkDB: G1T7F7_RABIT
Original site: G1T7F7_RABIT 
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
//
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