HDAC7_RAT
ID HDAC7_RAT Reviewed; 238 AA.
AC Q99P96;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Histone deacetylase 7;
DE Short=HD7;
DE EC=3.5.1.98;
DE AltName: Full=Histone deacetylase 7A;
DE Short=HD7a;
DE Flags: Fragment;
GN Name=Hdac7; Synonyms=Hdac7a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Testis;
RA Wilquet V., Chavez M., Korbers R., Geerts A.;
RT "Expression pattern of rat histone deacetylases.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Histone deacetylases act via the formation of
CC large multiprotein complexes. Involved in muscle maturation by
CC repressing transcription of myocyte enhancer factors such as MEF2A,
CC MEF2B and MEF2C. During muscle differentiation, it shuttles into the
CC cytoplasm, allowing the expression of myocyte enhancer factors.
CC Positively regulates the transcriptional repressor activity of FOXP3.
CC Serves as a corepressor of RARA, causing its deacetylation and
CC inhibition of RARE DNA element binding (By similarity). In association
CC with RARA, plays a role in the repression of microRNA-10a and thereby
CC in the inflammatory response (By similarity).
CC {ECO:0000250|UniProtKB:Q8C2B3, ECO:0000250|UniProtKB:Q8WUI4}.
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 -!- SUBUNIT: Interacts with KAT5 and EDNRA. Interacts with HDAC1, HDAC2,
CC HDAC3, HDAC4, HDAC5, NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1,
CC SAP30 and MBD3. Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B
CC and MEF2C. Interacts with KDM5B. Interacts with ZMYND15. Interacts with
CC PML. Interacts with FOXP3. Interacts with RARA (By similarity).
CC {ECO:0000250|UniProtKB:Q8C2B3, ECO:0000250|UniProtKB:Q8WUI4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=In the nucleus, it associates with distinct subnuclear dot-like
CC structures. Shuttles between the nucleus and the cytoplasm. In muscle
CC cells, it shuttles into the cytoplasm during myocyte differentiation.
CC The export to cytoplasm depends on the interaction with the 14-3-3
CC protein YWHAE and is due to its phosphorylation (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The nuclear export sequence mediates the shuttling between the
CC nucleus and the cytoplasm. {ECO:0000250}.
CC -!- PTM: May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases
CC PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-164 by
CC MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and
CC export from the nucleus. Phosphorylation at Ser-164 is a prerequisite
CC for phosphorylation at Ser-190 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Its activity is inhibited by Trichostatin A (TSA), a
CC known histone deacetylase inhibitor. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; AF321135; AAK11188.1; -; mRNA.
DR AlphaFoldDB; Q99P96; -.
DR SMR; Q99P96; -.
DR STRING; 10116.ENSRNOP00000011322; -.
DR BindingDB; Q99P96; -.
DR ChEMBL; CHEMBL2095943; -.
DR DrugCentral; Q99P96; -.
DR iPTMnet; Q99P96; -.
DR PaxDb; Q99P96; -.
DR PRIDE; Q99P96; -.
DR UCSC; RGD:619982; rat.
DR RGD; 619982; Hdac7.
DR eggNOG; KOG1343; Eukaryota.
DR InParanoid; Q99P96; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0004407; F:histone deacetylase activity; TAS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0005080; F:protein kinase C binding; ISO:RGD.
DR GO; GO:0033558; F:protein lysine deacetylase activity; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
DR GO; GO:0007043; P:cell-cell junction assembly; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; TAS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR GO; GO:0051402; P:neuron apoptotic process; IEP:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0006476; P:protein deacetylation; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
DR InterPro; IPR033660; HDAC4/7.
DR InterPro; IPR017320; Histone_deAcase_II_euk.
DR PANTHER; PTHR45364; PTHR45364; 1.
DR PANTHER; PTHR45364:SF3; PTHR45364:SF3; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN <1..>238
FT /note="Histone deacetylase 7"
FT /id="PRO_0000114707"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUI4"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 190
FT /note="Phosphoserine; by PKD/PRKD2"
FT /evidence="ECO:0000250|UniProtKB:Q8WUI4"
FT NON_TER 1
FT NON_TER 238
SQ SEQUENCE 238 AA; 26101 MW; B8869B96FBD040C5 CRC64;
TPGSQPQPMD LRVGQRPTVE PPPEPALLTL QHPQRLHRHL FLAGLQQQQR SAEPMRLSMD
PPLPELQGGQ QEQELRQLLN KDKSKRSAVA SSVVKQKLAE VILKKQQAAL ERTVHPSSPS
IPYRTLEPLD TEGAARSVLS SFLPPVPSLP TEPPEHFPLR KTVSEPNLKL RYKPKKSLER
RKNPLLRKES APPSLRRRPA ETLGDSSPSS SSTPASGCSS PNDSEHGPNP ALGSEADG
