Q8LRK8 (HDA18_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone deacetylase 18
EC=3.5.1.98

Gene names

Name:	HDA18
Ordered Locus Names:	At5g61070
ORF Names:	MAF19.8

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	682 AA.
Sequence status	Complete.
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. Required for appropriate cellular patterning in the root epidermis. Histone deacetylases act via the formation of large multiprotein complexes By similarity. Ref.4
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subcellular location	Nucleus By similarity.
Miscellaneous	HDA5, a tandem duplication of HDA18, is not required for the cellular patterning in the root epidermis.
Sequence similarities	Belongs to the histone deacetylase family. HD type 2 subfamily.
Sequence caution	The sequence BAB10370.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Coiled coil
Molecular function	Chromatin regulator Hydrolase Repressor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin remodeling Inferred from sequence or structural similarity Ref.1. Source: TAIR histone H3 deacetylation Inferred from electronic annotation. Source: GOC histone H4 deacetylation Inferred from electronic annotation. Source: GOC regulation of epidermal cell differentiation Inferred from mutant phenotype Ref.4. Source: TAIR regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW root epidermal cell differentiation Inferred from mutant phenotype PubMed 23362208. Source: TAIR transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay PubMed 23362208. Source: TAIR nucleus Inferred from direct assay PubMed 23362208. Source: TAIR
Molecular_function	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 Inferred from direct assay PubMed 23362208. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 682	682	Histone deacetylase 18		PRO_0000280093
Regions
	Region	59 – 382	324	Histone deacetylase
	Coiled coil	430 – 608	179	Potential
Sites
	Active site	191	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8LRK8 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 67D91533AB998840	FASTA	682	76,634
	10 20 30 40 50 60 MLLKFEASSE LRLVDPSVSL TVLRKIRLSH LPDMTMTSES SGKKCGEGDG KVAGKSQRKV 70 80 90 100 110 120 GLVYDETMCK HDTPNGKVDV ECPDRIRVIW EKLQLAGVTQ RCVVLGGSKA EDKHLKLVHT 130 140 150 160 170 180 KKHVNLVKSI STKKKDSRRN KIASQLDSIY LNGGSSEAAY LAAGSVVKVA EKVAEGELDC 190 200 210 220 230 240 GFAIVRPPGH HAESDEAMGF CLFNNVAVAA SFLLNERPDL DVKKILIVDW DIHHGNGTQK 250 260 270 280 290 300 MFWKDSRVLI FSVHRHDHGS FYPFGDDGDF NMVGEGPGEG FNINVPWEQG GCGDADYLAV 310 320 330 340 350 360 WNHILIPVTK EFKPDIILLS AGFDAAIGDP LGGCCVTPYG YSVMLKKLME FAHGKIVLAL 370 380 390 400 410 420 EGGYNLESLG KSSLACVQVL LEDKQIHGSS ETYPLESTRR VIQAVRERLC TYWPSLDASM 430 440 450 460 470 480 ASNENLKNPS AERNSADALL REVEELKSLM AARDGELEAR RKELKAKNKE LEANEKELEA 490 500 510 520 530 540 GLMLIRARED VICGLHAKIE SLQQERDEAV AKAERIDKEL QEDRARSQEF KEDTEFCLST 550 560 570 580 590 600 LRREKELAIM AKNKDLEAKE KELEARLMLV HAREDKIHAK IERLQQERDE AVAKAERIDK 610 620 630 640 650 660 ELQEDRSRSR VGNGSFAFSQ EFYEDMDLDE LEPLSPEFNE DMDSEELEPF QVIKKNMERS 670 680 HKKFIKDMEC IKFIASERAR VL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes." Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S., Richards E.J., Bender J., Mount D.W., Jorgensen R.A. Nucleic Acids Res. 30:5036-5055(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones." Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., Tabata S. DNA Res. 4:291-300(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Histone acetylation affects expression of cellular patterning genes in the Arabidopsis root epidermis." Xu C.-R., Liu C., Wang Y.-L., Li L.-C., Chen W.-Q., Xu Z.-H., Bai S.-N. Proc. Natl. Acad. Sci. U.S.A. 102:14469-14474(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF510670 mRNA. Translation: AAM34783.1. AB006696 Genomic DNA. Translation: BAB10370.1. Sequence problems. CP002688 Genomic DNA. Translation: AED97419.1.
IPI	IPI00530796.
RefSeq	NP_200915.2. NM_125500.2.
UniGene	At.29127.
3D structure databases
HSSP	HSSP built from PDB template 1WT6 based on UniProtKB Q09013.
ProteinModelPortal	Q8LRK8.
SMR	Q8LRK8. Positions 61-413.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT5G61070.1-P.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G61070.1; AT5G61070.1; AT5G61070.
GeneID	836228.
KEGG	ath:AT5G61070.
Organism-specific databases
TAIR	At5g61070.
Phylogenomic databases
eggNOG	COG0123.
InParanoid	Q8LRK8.
KO	K11407.
OMA	AVRERLC.
PhylomeDB	Q8LRK8.
ProtClustDB	CLSN2915013.
Gene expression databases
Genevestigator	Q8LRK8.
Family and domain databases
Gene3D	3.40.800.20. 1 hit.
InterPro	IPR000286. His_deacetylse. IPR023801. His_deacetylse_dom. [Graphical view]
PANTHER	PTHR10625. PTHR10625. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PRINTS	PR01270. HDASUPER.
ProtoNet	Search...

Entry information

Entry name

HDA18_ARATH

Accession

Primary (citable) accession number: Q8LRK8
Secondary accession number(s): Q9FNQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program