ID F1MYR0_BOVIN Unreviewed; 1089 AA.
AC F1MYR0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 83.
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=HDAC4 {ECO:0000313|Ensembl:ENSBTAP00000023621.6,
GN ECO:0000313|VGNC:VGNC:50611};
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:ENSBTAP00000023621.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000023621.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000023621.6,
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:ENSBTAP00000023621.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000023621.6};
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; XP_015318350.1; XM_015462864.1.
DR RefSeq; XP_015323185.1; XM_015467699.1.
DR AlphaFoldDB; F1MYR0; -.
DR SMR; F1MYR0; -.
DR STRING; 9913.ENSBTAP00000023621; -.
DR PaxDb; 9913-ENSBTAP00000023621; -.
DR Ensembl; ENSBTAT00000023621.6; ENSBTAP00000023621.6; ENSBTAG00000017764.6.
DR VEuPathDB; HostDB:ENSBTAG00000017764; -.
DR VGNC; VGNC:50611; HDAC4.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000157440; -.
DR HOGENOM; CLU_006530_2_0_1; -.
DR InParanoid; F1MYR0; -.
DR OMA; XAVASTE; -.
DR TreeFam; TF106174; -.
DR Reactome; R-BTA-350054; Notch-HLH transcription pathway.
DR Reactome; R-BTA-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-BTA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-BTA-8951936; RUNX3 regulates p14-ARF.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000017764; Expressed in cardiac ventricle and 107 other cell types or tissues.
DR ExpressionAtlas; F1MYR0; 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 GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd10162; ClassIIa_HDAC4_Gln-rich-N; 1.
DR CDD; cd10006; HDAC4; 1.
DR Gene3D; 6.10.250.1550; -; 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; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364:SF11; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR Pfam; PF12203; HDAC4_Gln; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 1.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
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 63..152
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 680..997
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 133..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 808
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 674
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 680
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 756
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 981
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1089 AA; 119509 MW; C4292646D8B6AB64 CRC64;
MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVASALPL PVAPPGVPMD LRLDHQFPLP
VAEPGLREQQ LQQELLALKQ KQQLQRQILI AEFQRQHEQL SRQHEAQLHE HIKQQQELLA
MKHQQELLEH QRKLERHRQE QELEKQHREQ KLQQLKNKEK GKESAVASTE VKMKLQEFVL
NKKKALAHRN LNHCMSSDPR YWYGKTQHSS LDQSSPPQSG ASASYNHPVL GMYDAKDDFP
LRKTASEPNL KLRSRLKQKV AERRSSPLLR RKDGPVVTAL KKRPLDVTDS ACSSAPGSAP
SSPNNSSGNV STENGIAPAV PSIPAETSLA HRLVAREGSV GPLPLYTSPS LPNITLGLPA
TGPSTGAAGQ QEAERLALPA LQQRISLFPG THLAPYLGAA PLERDAGAAP GSLLQHVVLL
EQPPTQTPLV TDRYLAGLGA LPLHAQPLVG AERVAPSVHK LRQHRPLGRT QSAPLPQSTQ
ALQHLVIQQQ HQQFLEKHKQ HFQQPQLHLN KMIPKPSEPA RQPESHPEET EEELREHQAL
LEEPFLDRLP GQKEAHTLAG VQVKQEPIES DDEETEPPRE AEPGQRPPTE QELLFRQQAL
LLEQQRIHQL RNYQASMEAA GIPVSFGGHR PLSRAQSSPA SATFPMSVQE PPAKPRFTTG
LVYDTLMLKH QCTCGNTNSH PEHAGRIQSI WSRLQETGLR GKCECIRGRK ATLEELQTVH
SETHALLYGT NPLNRQKLDS KKLLGSLTSV FVRLPCGGVG VDSDTIWNEV HSSGAARLAV
GCVVELVFKV ATGELKNGFA VVRPPGHHAE ESTPMGFCYF NSVAIAAKLL QQRLSVSKTL
VVDWDVHHGN GTQQAFYSDP RVLYISLHRY DDGNFFPGSG APDEVGTGAG VGFNVNMAFT
GGLDPPMGDA EYLAAFRTVV MPIASEFAPD VVLVSSGFDA VEGHPTPLGG YNLSAKCFGY
LTKQLMGLAG GRVVLALEGG HDLTAICDAS EACVSALLGN ELDPLPEKVL QQRPNANAVR
SMEKVIEIHS QYWRSLQRLA STAGYSLVEA QKCENEEAET VTAMASLSVA VKAPEKRPDE
EPMEEEPPL
//
