E1BF91 · E1BF91_BOVIN
- ProteinAlpha-tubulin N-acetyltransferase 1
- GeneATAT1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids377 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released. Required for normal sperm flagellar function. Promotes directional cell locomotion and chemotaxis, through AP2A2-dependent acetylation of alpha-tubulin at clathrin-coated pits that are concentrated at the leading edge of migrating cells. May facilitate primary cilium assembly.
Catalytic activity
- L-lysyl-[alpha-tubulin] + acetyl-CoA = N6-acetyl-L-lysyl-[alpha-tubulin] + CoA + H+
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 102 | Crucial for catalytic activity | |||
Binding site | 168-181 | acetyl-CoA (UniProtKB | ChEBI) | |||
Binding site | 204-213 | acetyl-CoA (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | clathrin-coated pit | |
Cellular Component | cytosol | |
Cellular Component | focal adhesion | |
Cellular Component | Golgi apparatus | |
Cellular Component | microtubule | |
Cellular Component | microtubule bundle | |
Cellular Component | mitotic spindle | |
Molecular Function | lysine N-acetyltransferase activity, acting on acetyl phosphate as donor | |
Molecular Function | tubulin N-acetyltransferase activity | |
Biological Process | alpha-tubulin acetylation | |
Biological Process | dentate gyrus development | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | neuron development | |
Biological Process | NLRP3 inflammasome complex assembly | |
Biological Process | positive regulation of NLRP3 inflammasome complex assembly | |
Biological Process | regulation of fat cell differentiation | |
Biological Process | regulation of microtubule cytoskeleton organization | |
Biological Process | response to mechanical stimulus | |
Biological Process | response to pain | |
Biological Process | spermatogenesis |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-tubulin N-acetyltransferase 1
- EC number
- Short namesAlpha-TAT ; Alpha-TAT1 ; TAT
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionE1BF91
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 100 | N6-acetyllysine; by autocatalysis | |||
Modified residue | 190 | N6-acetyllysine; by autocatalysis | |||
Post-translational modification
Autoacetylation strongly increases tubulin acetylation.
Keywords
- PTM
Expression
Gene expression databases
Interaction
Subunit
Component of the BBSome complex. Interacts with AP2 alpha-adaptins, including AP2A2, but not with AP1 gamma-adaptin (AP1G1/AP1G2); this interaction is required for efficient alpha-tubulin acetylation, hence clathrin-coated pits are sites of microtubule acetylation.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-36 | Disordered | |||
Domain | 45-234 | N-acetyltransferase | |||
Region | 241-283 | Disordered | |||
Compositional bias | 268-282 | Basic and acidic residues | |||
Region | 296-331 | Disordered | |||
Compositional bias | 299-314 | Pro residues | |||
Region | 347-377 | Disordered | |||
Sequence similarities
Belongs to the acetyltransferase ATAT1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length377
- Mass (Da)41,908
- Last updated2024-05-29 v3
- Checksum613D68F2F34C48CD
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 268-282 | Basic and acidic residues | |||
Compositional bias | 299-314 | Pro residues | |||
Keywords
- Technical term