Q94AQ6 · SIR4_ARATH
- ProteinNAD-dependent protein deacylase SRT2
- GeneSRT2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids373 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues (By similarity).
Involved in responses to ethylene leading to the transcriptional repression of some ethylene-responsive genes via the regulation of histone acetylation H3K9Ac (PubMed:29298835).
Negatively regulates plant basal defense against plant pathogens, possibly by suppressing salicylic acid biosynthesis (PubMed:20573705).
Involved in responses to ethylene leading to the transcriptional repression of some ethylene-responsive genes via the regulation of histone acetylation H3K9Ac (PubMed:29298835).
Negatively regulates plant basal defense against plant pathogens, possibly by suppressing salicylic acid biosynthesis (PubMed:20573705).
Catalytic activity
- H2O + N6-acetyl-L-lysyl-[protein] + NAD+ = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 100-120 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGVSTECGIPDYRSPNGAYS | ||||||
Binding site | 179-182 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: QNVD | ||||||
Active site | 196 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 204 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 207 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 271 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 274 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 311-313 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GSS | ||||||
Binding site | 337-339 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: NIG | ||||||
Binding site | 355 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | nucleus | |
Molecular Function | deacetylase activity | |
Molecular Function | NAD+ binding | |
Molecular Function | NAD-dependent protein lysine deacetylase activity | |
Molecular Function | transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | defense response to bacterium | |
Biological Process | ethylene-activated signaling pathway | |
Biological Process | negative regulation of defense response |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Is a mitochondrial protein deacetylase.
Names & Taxonomy
Protein names
- Recommended nameNAD-dependent protein deacylase SRT2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ94AQ6
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Reduced ethylene sensitivity in the double mutant srt1 srt2.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 35 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-47 | Mitochondrion | ||||
Sequence: MNMRRVFGGVSTDLFPSRSMYRPLQSGGNLVMLFKGCRRFVRTTCRV | ||||||
Chain | PRO_0000417348 | 48-373 | NAD-dependent protein deacylase SRT2 | |||
Sequence: SIPGGSLGNESKAPPRFLRDRKIVPDADPPNMEDIHKLYRLFEQSSRLTILTGAGVSTECGIPDYRSPNGAYSSGFKPITHQEFTRSSRARRRYWARSYAGWRRFTAAQPGPAHTALASLEKAGRINFMITQNVDRLHHRAGSDPLELHGTVYTVMCLECGFSFPRDLFQDQLKAINPKWAEAIESIDHGDPGSEKSFGMKQRPDGDIEIDEKFWEEGFHIPVCEKCKGVLKPDVIFFGDNIPKERATQAMEVAKQSDAFLVLGSSLMTMSAFRLCRAAHEAGAMTAIVNIGETRADDIVPLKINARVGEILHRVLDVGSLSVPAL |
Proteomic databases
Expression
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 75-373 | Deacetylase sirtuin-type | ||||
Sequence: DPPNMEDIHKLYRLFEQSSRLTILTGAGVSTECGIPDYRSPNGAYSSGFKPITHQEFTRSSRARRRYWARSYAGWRRFTAAQPGPAHTALASLEKAGRINFMITQNVDRLHHRAGSDPLELHGTVYTVMCLECGFSFPRDLFQDQLKAINPKWAEAIESIDHGDPGSEKSFGMKQRPDGDIEIDEKFWEEGFHIPVCEKCKGVLKPDVIFFGDNIPKERATQAMEVAKQSDAFLVLGSSLMTMSAFRLCRAAHEAGAMTAIVNIGETRADDIVPLKINARVGEILHRVLDVGSLSVPAL |
Sequence similarities
Belongs to the sirtuin family. Class II subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 3 isoforms produced by Alternative splicing.
Q94AQ6-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length373
- Mass (Da)41,536
- Last updated2001-12-01 v1
- Checksum6DD937F4237A5A43
Q94AQ6-2
- Name2
- Differences from canonical
- 1-1: M → MLSM
Q94AQ6-3
- Name3
- Differences from canonical
- 1-19: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL391712 EMBL· GenBank· DDBJ | CAC05449.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002688 EMBL· GenBank· DDBJ | AED91355.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED91356.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED91358.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED91360.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY045873 EMBL· GenBank· DDBJ | AAK76547.1 EMBL· GenBank· DDBJ | mRNA | ||
AY122995 EMBL· GenBank· DDBJ | AAM67528.1 EMBL· GenBank· DDBJ | mRNA | ||
AK316908 EMBL· GenBank· DDBJ | BAH19614.1 EMBL· GenBank· DDBJ | mRNA |