ID   F1N616_BOVIN            Unreviewed;       988 AA.
AC   F1N616;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 2.
DT   27-MAR-2024, entry version 81.
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:ENSBTAP00000038136.4,
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:ENSBTAP00000038136.4, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000038136.4, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000038136.4,
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:ENSBTAP00000038136.4}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000038136.4};
RG   Ensembl;
RL   Submitted (NOV-2023) 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}.
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DR   RefSeq; NP_001180070.1; NM_001193141.1.
DR   AlphaFoldDB; F1N616; -.
DR   SMR; F1N616; -.
DR   iPTMnet; F1N616; -.
DR   PaxDb; 9913-ENSBTAP00000038136; -.
DR   Ensembl; ENSBTAT00000038321.5; ENSBTAP00000038136.4; ENSBTAG00000026819.5.
DR   GeneID; 509843; -.
DR   KEGG; bta:509843; -.
DR   CTD; 51564; -.
DR   VEuPathDB; HostDB:ENSBTAG00000026819; -.
DR   VGNC; VGNC:49060; HDAC7.
DR   eggNOG; KOG1343; Eukaryota.
DR   GeneTree; ENSGT00940000159065; -.
DR   HOGENOM; CLU_006530_1_0_1; -.
DR   TreeFam; TF106174; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000026819; Expressed in thymus and 107 other cell types or tissues.
DR   ExpressionAtlas; F1N616; baseline and differential.
DR   GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
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   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR046949; HDAC4/5/7/9.
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|PIRNR:PIRNR037911};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
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};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT   DOMAIN          577..895
FT                   /note="Histone deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF00850"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..37
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..442
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        706
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT   BINDING         569
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT   BINDING         571
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT   BINDING         577
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT   BINDING         654
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT   SITE            879
FT                   /note="Contributes to catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ   SEQUENCE   988 AA;  106852 MW;  D0718D2FE4795A26 CRC64;
     MLGNHLDPDG TQVSPAAPCS SPPIIGWPRP RADTPGPQPQ PMDLRVGQRP PVEPPPEPTL
     LALQHPQRLH HHLFLAGLQP QRSAEPMRLS MDTPMPELQM GQQEQELRQL LNKDKSKRSA
     VASSVVKQKL AEVILKKQQA ALERTVHPNS PSVPYRTLEP LETEGAARSM LSSFLPPVPS
     LPCDPPEHFP LRKTVSEPNL KLRYKPKKSL ERRKNPLLRK ESAPPSLRRR PAETLGDSSP
     SSSSTPASGC SSPNDSEHGP NPVLGSEALL GQRLRLQETS LAPFALLPTI TLGLPAPARA
     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
//