ID F1MQP3_BOVIN Unreviewed; 1129 AA.
AC F1MQP3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Histone deacetylase 6 {ECO:0000313|Ensembl:ENSBTAP00000017618.6};
GN Name=HDAC6 {ECO:0000313|Ensembl:ENSBTAP00000017618.6,
GN ECO:0000313|VGNC:VGNC:50613};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000017618.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000017618.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017618.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000017618.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000017618.6};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR STRING; 9913.ENSBTAP00000072990; -.
DR PaxDb; 9913-ENSBTAP00000017618; -.
DR Ensembl; ENSBTAT00000017618.6; ENSBTAP00000017618.6; ENSBTAG00000013244.6.
DR Ensembl; ENSBTAT00000069208.1; ENSBTAP00000069588.1; ENSBTAG00000013244.6.
DR Ensembl; ENSBTAT00000078707.1; ENSBTAP00000072990.1; ENSBTAG00000013244.6.
DR VEuPathDB; HostDB:ENSBTAG00000013244; -.
DR VGNC; VGNC:50613; HDAC6.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000159563; -.
DR HOGENOM; CLU_007727_2_1_1; -.
DR OMA; MCHLEEL; -.
DR TreeFam; TF106173; -.
DR Reactome; R-BTA-3371511; HSF1 activation.
DR Reactome; R-BTA-350054; Notch-HLH transcription pathway.
DR Reactome; R-BTA-5617833; Cilium Assembly.
DR Reactome; R-BTA-9646399; Aggrephagy.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000013244; Expressed in cortex of kidney and 105 other cell types or tissues.
DR GO; GO:0016235; C:aggresome; IEA:Ensembl.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005901; C:caveola; IEA:Ensembl.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0005875; C:microtubule associated complex; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
DR GO; GO:0070840; F:dynein complex binding; IEA:Ensembl.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0048156; F:tau protein binding; IEA:Ensembl.
DR GO; GO:0001222; F:transcription corepressor binding; IEA:Ensembl.
DR GO; GO:0042903; F:tubulin deacetylase activity; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0070842; P:aggresome assembly; IEA:Ensembl.
DR GO; GO:0019896; P:axonal transport of mitochondrion; IEA:Ensembl.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0071218; P:cellular response to misfolded protein; IEA:Ensembl.
DR GO; GO:0061523; P:cilium disassembly; IEA:Ensembl.
DR GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0043131; P:erythrocyte enucleation; IEA:Ensembl.
DR GO; GO:0032418; P:lysosome localization; IEA:Ensembl.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IEA:Ensembl.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0070845; P:polyubiquitinated misfolded protein transport; IEA:Ensembl.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:Ensembl.
DR GO; GO:0032984; P:protein-containing complex disassembly; IEA:Ensembl.
DR GO; GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0016241; P:regulation of macroautophagy; IEA:Ensembl.
DR GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:Ensembl.
DR CDD; cd10003; HDAC6-dom2; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR10625:SF22; HISTONE DEACETYLASE 6; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 2.
DR Pfam; PF02148; zf-UBP; 1.
DR PRINTS; PR01270; HDASUPER.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF52768; Arginase/deacetylase; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00502};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00502};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00502}.
FT DOMAIN 1025..1123
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 123927 MW; D4D038AADAB34D13 CRC64;
MTSTGQDSTT PKERRSRHNP HSPTHDSSIT SKRGVKKSAI LRSSPSLAEV KKKGRMKKLS
QTAEQDLIMG LQGLNLNLES RTLSGTGLVF DEQLNEFHCL WDDSFPERPE RLHAIKEQLI
QEGLLDRCVS FQARFAEKEE LMLVHSLEYI DLMETTQYMN EEELHVLADT YDSVYLHPNS
YTCACLASGS VLRLVDAVLE AEIRNGMAII RPPGHHAQHS LMDGYCMFNH VAVAARYAQQ
KHDIQRVLIV DWDVHHGQGI QFAFDQDPSV LYFSIHRYEQ GRFWPHLKAS NWSTTGLGQG
QGYTINVPWN QVGMQDADYI AAFLHVLLPV AFEFQPQLVL VAAGFDALQG DPKGEMAATP
AGFAQLTHLL MGLAEGKLIL SLEGGYNLHS LAEGVSATLH TLLGDPCPVL ESPGAPCPSA
QASLSCTLEA LEPFWESLVR SVESLEEKDT VEKDDVEEKE EERLPQSPEL SVPIWPVLQA
RTGLVYDQQM MDHHNLWDNY HPEMPQRIHF IMHHLDELGL AKRCHSLPAR PATDAELLTC
HSAEHLERLR ATEKMKTREL RREGANYDSI YICSSTFACA QLAAGAACRL VEAVLAGEVL
NGVAVVRPPG HHAEPDAACG FCFFNSVAVA ARHAQAISGH ALRILIVDWD IHHGNGTQHI
FEEDPSVLYI SLHRYDHGTF FPMGNEGACT RIGKATGTGF TVNVAWNGPR MGDADYLAAW
HRLVLPVAYE FNPELVLVSA GFDAARGDPL GGCQVSPEGY AHLTHQLMGL ANGHIILILE
GGYNLTSISE SMAACTRSLL GDPLPLLTRL RPPLSGAQAS ITKTIQVHRR YWRSLRVMKR
KNKEELSSSK LITKKPSQPA SPGLANVTTT VEGNILETGM GQAASEASVK ESTPDQTESA
TAPVELTQGQ SSDTATQGAA LDQTISEGAT GGAELIQNPP ASCINNRIPP ALPVQGATAQ
TSPSKLMANL RILDLDSTTQ EPSEEEGLLG EAAGGQDTNE SVPVQVFGDH ADTDEVMFYA
VRPLLWCPHL AAVCPIPETG LNVTQPCQDC GTLQENWVCL SCYQVYCGRY INAHMLQHHE
GSGHPLVLSY ADLSAWCYHC QAYVHHKDLL AVKNIAHQNK FGEDIPHSD
//
