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Database: UniProt
Entry: B4DJ18_HUMAN
LinkDB: B4DJ18_HUMAN
Original site: B4DJ18_HUMAN 
ID   B4DJ18_HUMAN            Unreviewed;       296 AA.
AC   B4DJ18;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=cDNA FLJ54798, highly similar to Histone deacetylase 6 {ECO:0000313|EMBL:BAG58680.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG58680.1};
RN   [1] {ECO:0000313|EMBL:BAG58680.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Hippocampus {ECO:0000313|EMBL:BAG58680.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AK295884; BAG58680.1; -; mRNA.
DR   AlphaFoldDB; B4DJ18; -.
DR   MaxQB; B4DJ18; -.
DR   PeptideAtlas; B4DJ18; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; IEA:UniProt.
DR   GO; GO:0033558; F:protein lysine deacetylase activity; IEA:UniProt.
DR   GO; GO:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 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   PANTHER; PTHR10625:SF22; HISTONE DEACETYLASE 6; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   2: Evidence at transcript level;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        264..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          51..276
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
SQ   SEQUENCE   296 AA;  33325 MW;  05A02B102B835B56 CRC64;
     MKKLGQAMEE DLIVGLQGMD LNLEAEALAG TGLVLDEQLN EFHCLWDDSF PEGPERLHAI
     KEQLIQEGLL DRCVSFQARF AEKEELMLVH SLEYIDLMET TQYMNEGELR VLADTYDSVY
     LHPNSYSCAC LASGSVLRLV DAVLGAEIRN GMAIIRPPGH HAQHSLMDGY CMFNHVAVAA
     RYAQQKHRIR RVLNVDWDVH HGQGTQFTFD QDPSVLYFSI HRYEQGRFWP HLKASNWSTT
     GFGQGQGYTI NVPWNQVGMR DADYIAAFLH VLLPVALEVL GIWGVLGGGV ALKVRL
//
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