ID A0A3P9DNR0_9CICH Unreviewed; 1104 AA.
AC A0A3P9DNR0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Histone deacetylase 6 {ECO:0000313|Ensembl:ENSMZEP00005035847.1};
GN Name=HDAC6 {ECO:0000313|Ensembl:ENSMZEP00005035847.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005035847.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005035847.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005035847.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3P9DNR0; -.
DR STRING; 106582.ENSMZEP00005035847; -.
DR Ensembl; ENSMZET00005037112.1; ENSMZEP00005035847.1; ENSMZEG00005026767.1.
DR GeneTree; ENSGT00940000159563; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000265160; LG20.
DR GO; GO:0030955; F:potassium ion binding; IEA:Ensembl.
DR GO; GO:0042903; F:tubulin deacetylase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IEA:Ensembl.
DR GO; GO:0036269; P:swimming behavior; IEA:Ensembl.
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:UP000265160};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00502};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00502}.
FT DOMAIN 1000..1098
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1104 AA; 120475 MW; E93E01666DC1C594 CRC64;
MQSGSDPPGH GPKPVRRSPR LSPQVGSSEG TQENKGGNSL QELKRRGRME RTREEREEEL
SGKLKTLDLS SRSAASGTGL VYSEIFTHHK NEWDPSHPES PDRVTAIMKE LERQDLLPLC
IRVEPREATE EELLLAHMKH YVDLIKSTQT MTLAELQTLS NKYDSIYLHP ESFQVSVTAV
GAVLQLVDRV MTSELKNGFA IIRPPGHHAQ ANECNGYSIF NNVAIAARYA QTRHAISRVL
IVDWDVHHGQ GIQYRFQEDP SVLYFSVHRY EQGSFWPHLP ESDSHFVGSG PAEGRNINLP
WNQTGMTDAD YIAAFQQVLL PVAYEFQPQL VLVSAGFDAA VGDLKGEMCV SPQCFQVLTH
MLMSLAEGRL VLALEGGYNY ESSAESAAAC IRALLGGPCP PLTTPTAPSD SALQSISQTI
SALYPHWASL QVLEGSPSAE GRAISTSSNQ KNTMKPNLAP SVATTTGLVY DERMMEHSNL
WDRHHPEQPQ RIFKIFSKHQ QLGLVDRCQR IPVRLATEEE LSLCHSMQHI EQMKATAMMK
PRELHKLGDE FVSIYLNQQS FQCAQLAAGS CLNALDQILC GQVTNAVAIV RPPGHHAERD
YPCGFCLFNT AALAARYAKK ASHDPLMRIL ILDWDVHHGN GTQHMFEDDG SVLYISLHRY
DNGAFFPSSE DAAPDKVGVA KGAGFNVNVA WSGGRMGDSD YLAAFHRVVM PIATEFNPSL
VLVSAGFDAA RGDPLGGYNV TPEGYAHLTH MLMSLAGGRV LVILEGGYNL STISDSMAMC
TSMLLGDPPP ALVTPLPPPH HSAVATINEV IRYHVPYWRS LRIDVPESVR AALPTLKHRG
KRSSKGKGRK SEQGSNDKPP VPPARPDDST TVSSLEQLTQ GLASLDIGQT SANQNPASSP
VGGARPKVPL SSEKPTCEEV KKESDDSTPA CSESADSMSC QPVGVATPES VAGVDKVEAG
AGAEPEPEGA CGWSKPQTSL ELMCGADADG STLYVVDPLS WCPHLDAVKP LPSSGIDVFR
PCQDCGSEAE NWICLTCYQV FCGRYVNEHM VNHGVVSEHP LVLSFCDLSA WCYLCEAYVH
NQILFEAKNA AHCGKFGEEI PPWS
//
