Q9FE17 · SIR1_ARATH
- ProteinNAD-dependent protein deacetylase SRT1
- GeneSRT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids473 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
NAD-dependent protein deacetylase (By similarity).
Has deacetylase activity towards H3K9Ac (By similarity).
May have a function in the safeguard against genome instability and DNA damage to ensure plant cell growth (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).
Has deacetylase activity towards H3K9Ac (By similarity).
May have a function in the safeguard against genome instability and DNA damage to ensure plant cell growth (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).
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 | 52-71 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GAGISTSCGIPDFRGPKGIW | ||||||
Binding site | 114-117 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: QNVD | ||||||
Active site | 134 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 142 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 145 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 167 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 172 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 209-211 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GTS | ||||||
Binding site | 235-237 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: NLQ | ||||||
Binding site | 253 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | chromatin DNA binding | |
Molecular Function | metal ion binding | |
Molecular Function | NAD+ binding | |
Molecular Function | NAD-dependent protein lysine deacetylase activity | |
Molecular Function | transferase activity | |
Biological Process | ethylene-activated signaling pathway |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNAD-dependent protein deacetylase SRT1
- 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 accessionQ9FE17
- 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 29 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000417365 | 1-473 | NAD-dependent protein deacetylase SRT1 | |||
Sequence: MSLGYAEKLSFIEDVGQVGMAEFFDPSHLLQCKIEELAKLIQKSKHLVVFTGAGISTSCGIPDFRGPKGIWTLQREGKDLPKASLPFHRAMPSMTHMALVELERAGILKFVISQNVDGLHLRSGIPREKLSELHGDSFMEMCPSCGAEYLRDFEVETIGLKETSRKCSVEKCGAKLKDTVLDWEDALPPKEIDPAEKHCKKADLVLCLGTSLQITPACNLPLKCLKGGGKIVIVNLQKTPKDKKANVVIHGLVDKVVAGVMESLNMKIPPYVRIDLFQIILTQSISGDQRFINWTLRVASVHGLTSQLPFIKSIEVSFSDNHNYKDAVLDKQPFLMKRRTARNETFDIFFKVNYSDGCDCVSTQLSLPFEFKISTEEHVEIIDKEAVLQSLREKAVEESSCGQSGVVERRVVSEPRSEAVVYATVTSLRTYHSQQSLLANGDLKWKLEGSGTSRKRSRTGKRKSKALAEETKA |
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 27-267 | Deacetylase sirtuin-type | ||||
Sequence: SHLLQCKIEELAKLIQKSKHLVVFTGAGISTSCGIPDFRGPKGIWTLQREGKDLPKASLPFHRAMPSMTHMALVELERAGILKFVISQNVDGLHLRSGIPREKLSELHGDSFMEMCPSCGAEYLRDFEVETIGLKETSRKCSVEKCGAKLKDTVLDWEDALPPKEIDPAEKHCKKADLVLCLGTSLQITPACNLPLKCLKGGGKIVIVNLQKTPKDKKANVVIHGLVDKVVAGVMESLNMK | ||||||
Region | 447-473 | Disordered | ||||
Sequence: LEGSGTSRKRSRTGKRKSKALAEETKA |
Sequence similarities
Belongs to the sirtuin family. Class IV subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length473
- Mass (Da)52,642
- Last updated2001-03-01 v1
- ChecksumC265296654DE3E9D
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 14 | in Ref. 4; AAP68206 and 5; BAE99436 | ||||
Sequence: D → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF283757 EMBL· GenBank· DDBJ | AAG44850.1 EMBL· GenBank· DDBJ | mRNA | ||
AB009050 EMBL· GenBank· DDBJ | BAB09243.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED96677.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT008767 EMBL· GenBank· DDBJ | AAP68206.1 EMBL· GenBank· DDBJ | mRNA | ||
AK227432 EMBL· GenBank· DDBJ | BAE99436.1 EMBL· GenBank· DDBJ | mRNA |