GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0G2QC41_RAT
LinkDB: A0A0G2QC41_RAT
Original site: A0A0G2QC41_RAT 
ID   A0A0G2QC41_RAT          Unreviewed;      1152 AA.
AC   A0A0G2QC41;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   28-MAR-2018, entry version 20.
DE   RecName: Full=Histone deacetylase {ECO:0000256|SAAS:SAAS00894283};
DE            EC=3.5.1.98 {ECO:0000256|SAAS:SAAS00894283};
GN   Name=Hdac6 {ECO:0000313|Ensembl:ENSRNOP00000009295,
GN   ECO:0000313|RGD:619981};
GN   Synonyms=LOC103689963 {ECO:0000313|RGD:619981}, LOC108348065
GN   {ECO:0000313|RGD:11442569};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000009295, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000009295, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000009295,
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.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   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.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   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.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000009295}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000009295};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [3] {ECO:0000213|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.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC       {ECO:0000256|SAAS:SAAS00894227}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00894298}.
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DR   EMBL; AABR07037193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_001057931.1; XM_001057931.5.
DR   RefSeq; XP_003752058.1; XM_003752010.3.
DR   RefSeq; XP_003754788.1; XM_003754740.3.
DR   RefSeq; XP_006227351.1; XM_006227289.3.
DR   RefSeq; XP_006256817.1; XM_006256755.2.
DR   RefSeq; XP_006256818.1; XM_006256756.3.
DR   RefSeq; XP_006256820.1; XM_006256758.2.
DR   RefSeq; XP_006256821.1; XM_006256759.3.
DR   RefSeq; XP_228753.4; XM_228753.8.
DR   UniGene; Rn.13453; -.
DR   Ensembl; ENSRNOT00000009295; ENSRNOP00000009295; ENSRNOG00000048738.
DR   GeneID; 108348065; -.
DR   GeneID; 84581; -.
DR   KEGG; rno:108348065; -.
DR   KEGG; rno:84581; -.
DR   CTD; 10013; -.
DR   RGD; 619981; Hdac6.
DR   RGD; 11442569; LOC108348065.
DR   GeneTree; ENSGT00530000062809; -.
DR   KO; K11407; -.
DR   OMA; QPHGFCI; -.
DR   TreeFam; TF106173; -.
DR   Reactome; R-RNO-3371511; HSF1 activation.
DR   Reactome; R-RNO-5617833; Cilium Assembly.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000048738; -.
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:0044297; C:cell body; ISO:RGD.
DR   GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR   GO; GO:0005813; C:centrosome; IDA: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:0043005; C:neuron projection; ISO:RGD.
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:0043234; C:protein 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:0001047; F:core promoter 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:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:RGD.
DR   GO; GO:0048156; F:tau protein 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: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:0034599; P:cellular response to oxidative stress; IEP: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:0048668; P:collateral sprouting; ISO:RGD.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; ISO:RGD.
DR   GO; GO:0016575; P:histone deacetylation; ISO:RGD.
DR   GO; GO:0070846; P:Hsp90 deacetylation; 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:0048843; P:negative regulation of axon extension involved in axon guidance; IMP: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:0043242; P:negative regulation of protein complex disassembly; ISO:RGD.
DR   GO; GO:0045861; P:negative regulation of proteolysis; ISO:RGD.
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:0034983; P:peptidyl-lysine deacetylation; ISO:RGD.
DR   GO; GO:0070845; P:polyubiquitinated misfolded protein transport; ISO:RGD.
DR   GO; GO:0090035; P:positive regulation of chaperone-mediated protein complex assembly; ISO: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:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; ISO:RGD.
DR   GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; ISO:RGD.
DR   GO; GO:1903223; P:positive regulation of oxidative stress-induced neuron death; IMP:RGD.
DR   GO; GO:0010870; P:positive regulation of receptor biosynthetic process; ISO:RGD.
DR   GO; GO:0009967; P:positive regulation of signal transduction; 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:0043241; P:protein complex disassembly; ISO:RGD.
DR   GO; GO:0006476; P:protein deacetylation; 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: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:0040029; P:regulation of gene expression, epigenetic; 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:0010469; P:regulation of receptor activity; ISO:RGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
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:0010033; P:response to organic substance; ISO:RGD.
DR   GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0090042; P:tubulin deacetylation; 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   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.800.20; -; 2.
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; PTHR10625; 4.
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; SSF52768; 2.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator {ECO:0000256|SAAS:SAAS00894233};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002494};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00870288};
KW   Nucleus {ECO:0000256|SAAS:SAAS00894277};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:A0A0G2QC41};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transcription {ECO:0000256|SAAS:SAAS00894309};
KW   Transcription regulation {ECO:0000256|SAAS:SAAS00894290}.
FT   DOMAIN     1068   1129       UBP-type. {ECO:0000259|PROSITE:PS50271}.
FT   ZN_FING    1068   1129       UBP-type. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00502}.
SQ   SEQUENCE   1152 AA;  125495 MW;  62A42C1D96C5303A CRC64;
     MTSTGQDSST RQRKSRHNPQ SPLQDSSATL KRGGKKGAVP HSSPNLAEVK KKGKMKKLSQ
     PAEEDLIVGL QGLDLNSETR VPVGTGLVFD EQLNDFHCLW DDSFPENPER LHAIKEQLIL
     EGLLGRCVSF QARFAEKEEL MLVHSLEYID LMETTQYMNE GELRVLAGTY DSVYLHPNSY
     SCACLATGSV LRLVDAVMGA EIRNGMAVIR PPGHHAQRSL MDGYCMFNHL AVAARYAQKK
     HRIQRILIVD WDVHHGQGTQ FIFDQDPSVL YFSIHRYEHG RFWPHLKASN WSTTGFGQGQ
     GYTINVPWNQ VGMRDADYIA AFLHILLPVA FEFQPQLVLV AAGFDALHGD PKGEMSATPA
     GFAHLTHFLM GLAGGKLILS LEGGYNLHAL AKGVSGSLHT LLGDPCPMLE SPVAPCASAQ
     TSISCTLEAL EPFWEVLERS VEPQDEDEVE GDMLEDEEEE GHWEATALPM DTWPLLQNRT
     GLVYDERMMS HCNLWDNHHP ETPQRILRIM CHLEEVGLAA RCLILPARPA LDSELLTCHS
     AEYVERLRAT EKMKTRDLHR EGANFESIYI CPSTFACAQL ATGAACRLVE AVLSGEVLNG
     IAIVRPPGHH AEPDAACGFC FFNSVAVAAR HAQVIAGRAL RILIVDWDVH HGNGTQHIFE
     EDPSVLYVSL HRYDRGTFFP MGDEGASSQV GRAAGTGFTV NVPWNGPRMG DADYLATWHR
     LVLPIAYEFN PELVLISAGF DAAQGDPLGG CQVTPEGYAH LTHLLMGLAG GRIILILEGG
     YNLTSISESM AACTHSLLGD PPPQLTSLRP PQSGALASIS EVIQVHRKYW RSLRLMKMED
     KEERSSSRLV IKKLPQSASP VSAKGMTTPK GKVLEAGMRK PTAALPTKES TLGQAKAKTA
     KALLAQGQSS EQAAKGTTLD LATSKDTVGG ATTDQCASVA ATENSANQTT SGEEASGETE
     SFGTSPSSNA SKQTTGASPL HGAAAQQSPE LGLSSTLELS SEAQEVQESE EGLLGEAAGG
     QDMNSLMLTQ GFGDFNTQDV FYAVTPLSWC PHLMAVCPIP AAGLDVSQPC KTCGSVQENW
     VCLTCYQVYC SRYVNAHMVC HHEASEHPLV LSCVDLSTWC YLCQAYVHHE DLQDVKNAAH
     QNKFGEGMPH LQ
//
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