Q99P96 (HDAC7_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone deacetylase 7
Short name=HD7
EC=3.5.1.98

Alternative name(s):
Histone deacetylase 7A
Short name=HD7a

Gene names

Name:	Hdac7
Synonyms:	Hdac7a

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	238 AA.
Sequence status	Fragment.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors By similarity.
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Interacts with KAT5 and EDNRA. Interacts with HDAC1, HDAC2, HDAC3, HDAC4, HDAC5, NCOR1, NCOR2, SIN3A, SIN3B, RBBP4, RBBP7, MTA1L1, SAP30 and MBD3. Interacts with the 14-3-3 protein YWHAE, MEF2A, MEF2B and MEF2C. Interacts with KDM5B By similarity. Interacts with ZMYND15 By similarity. Interacts with PML By similarity.
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Note: In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation By similarity.
Domain	The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm By similarity.
Post-translational modification	May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-164 by MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and export from the nucleus. Phosphorylation at Ser-164 is a prerequisite for phosphorylation at Ser-190 By similarity.
Miscellaneous	Its activity is inhibited by Trichostatin A (TSA), a known histone deacetylase inhibitor By similarity.
Sequence similarities	Belongs to the histone deacetylase family. HD type 2 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Traceable author statement PubMed 12711221. Source: UniProtKB histone H3 deacetylation Inferred from electronic annotation. Source: GOC histone H4 deacetylation Inferred from electronic annotation. Source: GOC inflammatory response Traceable author statement PubMed 12711221. Source: UniProtKB negative regulation of striated muscle tissue development Traceable author statement PubMed 12711221. Source: UniProtKB negative regulation of transcription, DNA-dependent Traceable author statement PubMed 12711221. Source: UniProtKB nervous system development Traceable author statement PubMed 12711221. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB histone deacetylase complex Traceable author statement PubMed 12711221. Source: UniProtKB
Molecular_function	14-3-3 protein binding Inferred from sequence or structural similarity. Source: UniProtKB NAD-dependent histone deacetylase activity (H3-K14 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K18 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K9 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H4-K16 specific) Inferred from electronic annotation. Source: EC histone deacetylase activity Traceable author statement PubMed 12711221. Source: UniProtKB transcription factor binding Traceable author statement PubMed 12711221. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›238	›238	Histone deacetylase 7		PRO_0000114707
Amino acid modifications
	Modified residue	118	1	Phosphoserine By similarity
	Modified residue	164	1	Phosphoserine; by MARK2, MARK3 and PKD/PRKD1 By similarity
	Modified residue	190	1	Phosphoserine; by PKD/PRKD2 By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	238	1

Sequences

	Sequence		Length	Mass (Da)
	Q99P96 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: B8869B96FBD040C5	FASTA	238	26,101
	10 20 30 40 50 60 TPGSQPQPMD LRVGQRPTVE PPPEPALLTL QHPQRLHRHL FLAGLQQQQR SAEPMRLSMD 70 80 90 100 110 120 PPLPELQGGQ QEQELRQLLN KDKSKRSAVA SSVVKQKLAE VILKKQQAAL ERTVHPSSPS 130 140 150 160 170 180 IPYRTLEPLD TEGAARSVLS SFLPPVPSLP TEPPEHFPLR KTVSEPNLKL RYKPKKSLER 190 200 210 220 230 RKNPLLRKES APPSLRRRPA ETLGDSSPSS SSTPASGCSS PNDSEHGPNP ALGSEADG

References

[1]	"Expression pattern of rat histone deacetylases." Wilquet V., Chavez M., Korbers R., Geerts A. Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. Tissue: Testis.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF321135 mRNA. Translation: AAK11188.1.
IPI	IPI01016416.
UniGene	Rn.203327.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000011322.
Proteomic databases
PaxDb	Q99P96.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	RGD:619982. rat.
Organism-specific databases
RGD	619982. Hdac7.
Phylogenomic databases
eggNOG	COG0123.
HOGENOM	HOG000232065.
Gene expression databases
ArrayExpress	Q99P96.
Genevestigator	Q99P96.
GermOnline	ENSRNOG00000008308. Rattus norvegicus.
Family and domain databases
ProtoNet	Search...
Other
ChEMBL	CHEMBL2914.

Entry information

Entry name

HDAC7_RAT

Accession

Primary (citable) accession number: Q99P96

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program