ID D3ZVD8_RAT Unreviewed; 1189 AA.
AC D3ZVD8; F1LSE3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Histone deacetylase 6 {ECO:0000313|Ensembl:ENSRNOP00000063689.3};
GN Name=Hdac6 {ECO:0000313|Ensembl:ENSRNOP00000063689.3,
GN ECO:0000313|RGD:619981};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000063689.3, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000063689.3, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000063689.3,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000063689.3}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000063689.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; D3ZVD8; -.
DR STRING; 10116.ENSRNOP00000063689; -.
DR jPOST; D3ZVD8; -.
DR PaxDb; 10116-ENSRNOP00000009295; -.
DR PeptideAtlas; D3ZVD8; -.
DR Ensembl; ENSRNOT00000064924.3; ENSRNOP00000063689.3; ENSRNOG00000048738.3.
DR AGR; RGD:619981; -.
DR RGD; 619981; Hdac6.
DR VEuPathDB; HostDB:ENSRNOG00000048738; -.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000159563; -.
DR HOGENOM; CLU_007727_2_1_1; -.
DR InParanoid; D3ZVD8; -.
DR OMA; MCHLEEL; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000047281; Expressed in jejunum.
DR GO; GO:0016235; C:aggresome; ISO:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005901; C:caveola; ISO:RGD.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0005813; C:centrosome; IDA:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0000118; C:histone deacetylase complex; ISO:RGD.
DR GO; GO:0016234; C:inclusion body; ISO:RGD.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0005875; C:microtubule associated complex; ISO:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:RGD.
DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:RGD.
DR GO; GO:0019213; F:deacetylase activity; IDA:RGD.
DR GO; GO:0070840; F:dynein complex binding; ISO:RGD.
DR GO; GO:0004407; F:histone deacetylase activity; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0051787; F:misfolded protein binding; ISO:RGD.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:RGD.
DR GO; GO:0033558; F:protein lysine deacetylase activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0048156; F:tau protein binding; ISO:RGD.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:RGD.
DR GO; GO:0042903; F:tubulin deacetylase activity; ISO:RGD.
DR GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0070842; P:aggresome assembly; ISO:RGD.
DR GO; GO:0019896; P:axonal transport of mitochondrion; IMP:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:RGD.
DR GO; GO:0071218; P:cellular response to misfolded protein; ISO:RGD.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEP:RGD.
DR GO; GO:0035967; P:cellular response to topologically incorrect protein; ISO:RGD.
DR GO; GO:0061523; P:cilium disassembly; ISO:RGD.
DR GO; GO:0048668; P:collateral sprouting; ISO:RGD.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISO:RGD.
DR GO; GO:0043131; P:erythrocyte enucleation; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR GO; GO:0032418; P:lysosome localization; ISO:RGD.
DR GO; GO:0051646; P:mitochondrion localization; ISO:RGD.
DR GO; GO:0014902; P:myotube differentiation; ISO:RGD.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IMP:RGD.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISO:RGD.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
DR GO; GO:1901984; P:negative regulation of protein acetylation; IMP:RGD.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0043242; P:negative regulation of protein-containing complex disassembly; ISO:RGD.
DR GO; GO:0045861; P:negative regulation of proteolysis; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; ISO:RGD.
DR GO; GO:0070845; P:polyubiquitinated misfolded protein transport; ISO:RGD.
DR GO; GO:1900409; P:positive regulation of cellular response to oxidative stress; IMP:RGD.
DR GO; GO:1904056; P:positive regulation of cholangiocyte proliferation; IMP:RGD.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD.
DR GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:RGD.
DR GO; GO:0090044; P:positive regulation of tubulin deacetylation; IMP:RGD.
DR GO; GO:0031648; P:protein destabilization; ISO:RGD.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISO:RGD.
DR GO; GO:0032984; P:protein-containing complex disassembly; ISO:RGD.
DR GO; GO:0070201; P:regulation of establishment of protein localization; ISO:RGD.
DR GO; GO:0045598; P:regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0016241; P:regulation of macroautophagy; ISO:RGD.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:RGD.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IMP:RGD.
DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR GO; GO:0070848; P:response to growth factor; ISO:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:0051788; P:response to misfolded protein; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISO:RGD.
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 1: Evidence at protein level;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00502};
KW Proteomics identification {ECO:0007829|PeptideAtlas:D3ZVD8};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00502};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00502}.
FT DOMAIN 1085..1183
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 129429 MW; 59B0593FEED5AEF7 CRC64;
MRARGHTGRR EFGGASQGRS LERGQCSSRS RSKGSSAMTS TGQDSSTRQR KSRHNPQSPL
QDSSATLKRG GKKGAVPHSS PNLAEVKKKG KMKKLSQPAE EDLIVGLQGL DLNSETRVPV
GTGLVFDEQL NDFHCLWDDS FPENPERLHA IKEQLILEGL LGRCVSFQAR FAEKEELMLV
HSLEYIDLME TTQYMNEGEL RVLAGTYDSV YLHPNSYSCA CLATGSVLRL VDAVMGAEIR
NGMAVIRPPG HHAQRSLMDG YCMFNHLAVA ARYAQKKHRI QRILIVDWDV HHGQGTQFIF
DQDPSVLYFS IHRYEHGRFW PHLKASNWST TGFGQGQGYT INVPWNQVGM RDADYIAAFL
HILLPVAFEF QPQLVLVAAG FDALHGDPKG EMSATPAGFA HLTHFLMGLA GGKLILSLEG
GYNLHALAKG VSGSLHTLLG DPCPMLESPV APCASAQTSI SCTLEALEPF WEVLERSVEP
QDEDEVEGDM LEDEEEEGHW EATALPMDTW PLLQNRTGLV YDERMMSHCN LWDNHHPETP
QRILRIMCHL EEVGLAARCL ILPARPALDS ELLTCHSAEY VERLRATEKM KTRDLHREGA
NFESIYICPS TFACAQLATG AACRLVEAVL SGEVLNGIAI VRPPGHHAEP DAACGFCFFN
SVAVAARHAQ VIAGRALRIL IVDWDVHHGN GTQHIFEEDP SVLYVSLHRY DRGTFFPMGD
EGASSQVGRA AGTGFTVNVP WNGPRMGDAD YLATWHRLVL PIAYEFNPEL VLISAGFDAA
QGDPLGGCQV TPEGYAHLTH LLMGLAGGRI ILILEGGYNL TSISESMAAC THSLLGDPPP
QLTSLRPPQS GALASISEVI QVHRKYWRSL RLMKMEDKEE RSSSRLVIKK LPQSASPVSA
KGMTTPKGKV LEAGMRKPTA ALPTKESTLG QAKAKTAKAL LAQGQSSEQA AKGTTLDLAT
SKDTVGGATT DQCASVAATE NSANQTTSGE EASGETESFG TSPSSNASKQ TTGASPLHGA
AAQQSPELGL SSTLELSSEA QEVQESEEGL LGEAAGGQDM NSLMLTQGFG DFNTQDVFYA
VTPLSWCPHL MAVCPIPAAG LDVSQPCKTC GSVQENWVCL TCYQVYCSRY VNAHMVCHHE
ASEHPLVLSC VDLSTWCYLC QAYVHHEDLQ DVKNAAHQNK FGEGMPHLQ
//
