ID A0AAA9TGJ2_BOVIN Unreviewed; 958 AA. AC A0AAA9TGJ2; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 24-JUL-2024, entry version 2. DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911}; DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911}; GN Name=HDAC7 {ECO:0000313|Ensembl:ENSBTAP00000095989.1, GN ECO:0000313|VGNC:VGNC:49060}; 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:ENSBTAP00000095989.1, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000095989.1, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000095989.1, 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:ENSBTAP00000095989.1} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000095989.1}; RG Ensembl; RL Submitted (APR-2024) to UniProtKB. CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the CC N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone CC deacetylation gives a tag for epigenetic repression and plays an CC important role in transcriptional regulation, cell cycle progression CC and developmental events. {ECO:0000256|PIRNR:PIRNR037911}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl- CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA- CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, CC ChEBI:CHEBI:61930; EC=3.5.1.98; CC Evidence={ECO:0000256|PIRNR:PIRNR037911}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, CC ECO:0000256|PIRNR:PIRNR037911}. CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2 CC subfamily. {ECO:0000256|ARBA:ARBA00007738, CC ECO:0000256|PIRNR:PIRNR037911}. 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 Ensembl; ENSBTAT00000094835.1; ENSBTAP00000095989.1; ENSBTAG00000026819.6. DR VGNC; VGNC:49060; HDAC7. DR GeneTree; ENSGT00940000159065; -. DR Proteomes; UP000009136; Chromosome 5. DR CDD; cd10008; HDAC7; 1. DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1. DR InterPro; IPR046949; HDAC4/5/7/9. DR InterPro; IPR050284; HDAC_PDAC. 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:SF44; HISTONE DEACETYLASE 7; 1. DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PIRSF; PIRSF037911; HDAC_II_euk; 3. DR PRINTS; PR01270; HDASUPER. DR SUPFAM; SSF52768; Arginase/deacetylase; 1. PE 3: Inferred from homology; KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Repressor {ECO:0000256|PIRNR:PIRNR037911}; KW Transcription {ECO:0000256|PIRNR:PIRNR037911}; KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037911}. FT DOMAIN 547..865 FT /note="Histone deacetylase" FT /evidence="ECO:0000259|Pfam:PF00850" FT REGION 9..58 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 187..290 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 349..379 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 393..446 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 474..518 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 23..39 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 237..261 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 393..412 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 425..439 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 486..518 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 958 AA; 103698 MW; 97626F6B0C6950E0 CRC64; MRCLCQRAAA DGTQVSPAAP CSSPPIIGWP RPRADTPGPQ PQPMDLRVGQ RPPVEPPPEP TLLALQHPQR LHHHLFLAGL QPQRSAEPMR LSMDTPMPEL QMGQQEQELR QLLNKDKSKR SAVASSVVKQ KLAEVILKKQ QAALERTVHP NSPSVPYRTL EPLETEGAAR SMLSSFLPPV PSLPCDPPEH FPLRKTVSEP NLKLRYKPKK SLERRKNPLL RKESAPPSLR RRPAETLGDS SPSSSSTPAS GCSSPNDSEH GPNPVLGSEA DGDRRTHATL GPRGPVLGNP HAHLFLPHGL EPEAGGPLPS RLQPILLLDP SVTHTPLLTV PGLGPLPFHF AQSLLTTERP SGSGLHRPLS RTRSEPLPPS ATTPSLLGPL QPRLERLKPH VQLIKRSAKP SEKPRLRQIP SAEDLETDGG SVGPLRDDGL EHRESSHGQQ EARGTVPLQQ HQQVFLWEQQ RLAGRLPRGA TGDSVLLPLA PGSHRPLSRA QSSPAAPASL STPEPASQAR ILPSSETPAR TLPFTTGLVY DSVMLKHQCS CGDNSRHPEH AGRIQSIWSR LLERGLRSQC ESLRGRKASL EELQSVHSER HVLLYGTNPL SRLKLDNGKL AGLLAQRMFV MLPCGGVGVD TDTIWNELHS SNAARWAAGS VTDLAFKVAS RELKNGFAVV RPPGHHADHS TAMGFCFFNS VAIACRQLQQ QGKASKILIV DWDVHHGNGT QQTFYQDPNV LYISLHRHDD GNFFPGSGAV DEVGAGSGEG FNVNVAWAGG LDPPMGDPEY LAAFRIVVMP IAREFSPDLV LVSAGFDAAE GHPPPLGGYH VSAKCFGYMT QQLMSLAGGA VVLALEGGHD LTAICDASEA CVAALLGNKV DPLSEEGWKQ KPNLNAIRSL EAVIRVHSEY WGCMQRLASR PDSWVHRVPG ADAEEVEAVT ALASLSVGIL AEERTSGQLV EEEEPMNL //