ID A0AAA9T6A2_BOVIN Unreviewed; 986 AA. AC A0AAA9T6A2; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 27-NOV-2024, entry version 4. 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:ENSBTAP00000091309.1, 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:ENSBTAP00000091309.1, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000091309.1, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000091309.1, 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:ENSBTAP00000091309.1} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000091309.1}; RG Ensembl; RL Submitted (AUG-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=N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] + CC acetate; 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 RefSeq; XP_005206431.1; XM_005206374.3. DR Ensembl; ENSBTAT00000133998.1; ENSBTAP00000091309.1; ENSBTAG00000026819.6. DR GeneID; 509843; -. DR VGNC; VGNC:49060; HDAC7. DR GeneTree; ENSGT00940000159065; -. DR Proteomes; UP000009136; Chromosome 5. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro. DR CDD; cd10008; HDAC7; 1. DR FunFam; 3.40.800.20:FF:000002; Histone deacetylase; 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; 2. DR PRINTS; PR01270; HDASUPER. DR SUPFAM; SSF52768; Arginase/deacetylase; 1. PE 3: Inferred from homology; KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853, KW ECO:0000256|PIRNR:PIRNR037911}; Hydrolase {ECO:0000256|PIRNR:PIRNR037911}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|PIRNR:PIRNR037911}; KW Transcription {ECO:0000256|PIRNR:PIRNR037911}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, KW ECO:0000256|PIRNR:PIRNR037911}; Zinc {ECO:0000256|PIRSR:PIRSR037911-2}. FT DOMAIN 575..893 FT /note="Histone deacetylase" FT /evidence="ECO:0000259|Pfam:PF00850" FT REGION 1..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 183..263 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 294..313 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 377..474 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 502..546 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 19..35 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 233..257 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 416..440 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 453..467 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 514..546 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 704 FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1" FT BINDING 567 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2" FT BINDING 569 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2" FT BINDING 575 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2" FT BINDING 652 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2" FT SITE 877 FT /note="Contributes to catalysis" FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3" SQ SEQUENCE 986 AA; 106555 MW; 439C30AB8A2F3691 CRC64; MHSPGADGTQ VSPAAPCSSP PIIGWPRPRA DTPGPQPQPM DLRVGQRPPV EPPPEPTLLA LQHPQRLHHH LFLAGLQPQR SAEPMRLSMD TPMPELQMGQ QEQELRQLLN KDKSKRSAVA SSVVKQKLAE VILKKQQAAL ERTVHPNSPS VPYRTLEPLE TEGAARSMLS SFLPPVPSLP CDPPEHFPLR KTVSEPNLKL RYKPKKSLER RKNPLLRKES APPSLRRRPA ETLGDSSPSS SSTPASGCSS PNDSEHGPNP VLGSEALLGQ RLRLQETSLA PFALLPTITL GLPAPARADG DRRTHATLGP RGPVLGNPHA HLFLPHGLEP EAGGPLPSRL QPILLLDPSV THTPLLTVPG LGPLPFHFAQ SLLTTERPSG SGLHRPLSRT RSEPLPPSAT TPSLLGPLQP RLERLKPHVQ LIKRSAKPSE KPRLRQIPSA EDLETDGGSV GPLRDDGLEH RESSHGQQEA RGTVPLQQHQ QVFLWEQQRL AGRLPRGATG DSVLLPLAPG SHRPLSRAQS SPAAPASLST PEPASQARIL PSSETPARTL PFTTGLVYDS VMLKHQCSCG DNSRHPEHAG RIQSIWSRLL ERGLRSQCES LRGRKASLEE LQSVHSERHV LLYGTNPLSR LKLDNGKLAG LLAQRMFVML PCGGVGVDTD TIWNELHSSN AARWAAGSVT DLAFKVASRE LKNGFAVVRP PGHHADHSTA MGFCFFNSVA IACRQLQQQG KASKILIVDW DVHHGNGTQQ TFYQDPNVLY ISLHRHDDGN FFPGSGAVDE VGAGSGEGFN VNVAWAGGLD PPMGDPEYLA AFRIVVMPIA REFSPDLVLV SAGFDAAEGH PPPLGGYHVS AKCFGYMTQQ LMSLAGGAVV LALEGGHDLT AICDASEACV AALLGNKVDP LSEEGWKQKP NLNAIRSLEA VIRVHSEYWG CMQRLASRPD SWVHRVPGAD AEEVEAVTAL ASLSVGILAE ERTSGQLVEE EEPMNL //