A0A803KKY0 · A0A803KKY0_PANTR
- ProteinAlpha-tubulin N-acetyltransferase 1
- GeneATAT1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids411 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
- acetyl-CoA + L-lysyl-[alpha-tubulin] = CoA + H+ + N6-acetyl-L-lysyl-[alpha-tubulin]
Features
Showing features for site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | clathrin-coated pit | |
Cellular Component | cytoplasm | |
Cellular Component | focal adhesion | |
Cellular Component | microtubule | |
Cellular Component | spindle | |
Molecular Function | tubulin N-acetyltransferase activity | |
Biological Process | neuron development | |
Biological Process | regulation of microtubule cytoskeleton organization |
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 > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pan
Accessions
- Primary accessionA0A803KKY0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-15 | |||||
Sequence: MWLTWPFCFLTITLR | ||||||
Chain | PRO_5031132834 | 16-411 | Alpha-tubulin N-acetyltransferase 1 | |||
Sequence: EEGVCHLESVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARPAGKGAIIGFIKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVNNFVIFEGFFAHQHRPPAPSLRATRHSRAAAVDPTPTAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPLNRAPRRATPPAHPPPRSSSLGNSPERGPLRPFVPEQELLRSLRLCPPHPTARLLLAADPGGSPAQRRRTRGTPPGLVAQSCCYSRHGGVNSSSPNTGNQDSKQGEQETKNRSASEEQALSQDGSGEKPMHTAPPQAPAPAPPAQSWTVGGDILNARFIRNLQERRSTRPW | ||||||
Modified residue | 44 | N6-acetyllysine; by autocatalysis | ||||
Sequence: K | ||||||
Modified residue | 134 | N6-acetyllysine; by autocatalysis | ||||
Sequence: K |
Post-translational modification
Autoacetylation strongly increases tubulin acetylation.
Keywords
- PTM
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 domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-178 | N-acetyltransferase | ||||
Sequence: LTWPFCFLTITLREEGVCHLESVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARPAGKGAIIGFIKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVNNFVIFEGFF | ||||||
Region | 184-227 | Disordered | ||||
Sequence: PPAPSLRATRHSRAAAVDPTPTAPARKLPPKRAEGDIKPYSSSD | ||||||
Compositional bias | 212-226 | Basic and acidic residues | ||||
Sequence: PPKRAEGDIKPYSSS | ||||||
Region | 240-272 | Disordered | ||||
Sequence: PLNRAPRRATPPAHPPPRSSSLGNSPERGPLRP | ||||||
Compositional bias | 243-258 | Pro residues | ||||
Sequence: RAPRRATPPAHPPPRS | ||||||
Region | 294-390 | Disordered | ||||
Sequence: LLLAADPGGSPAQRRRTRGTPPGLVAQSCCYSRHGGVNSSSPNTGNQDSKQGEQETKNRSASEEQALSQDGSGEKPMHTAPPQAPAPAPPAQSWTVG | ||||||
Compositional bias | 325-344 | Polar residues | ||||
Sequence: SRHGGVNSSSPNTGNQDSKQ |
Sequence similarities
Belongs to the acetyltransferase ATAT1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length411
- Mass (Da)45,772
- Last updated2021-06-02 v1
- Checksum6326A4295293C993
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 212-226 | Basic and acidic residues | ||||
Sequence: PPKRAEGDIKPYSSS | ||||||
Compositional bias | 243-258 | Pro residues | ||||
Sequence: RAPRRATPPAHPPPRS | ||||||
Compositional bias | 325-344 | Polar residues | ||||
Sequence: SRHGGVNSSSPNTGNQDSKQ |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
NBAG03000221 EMBL· GenBank· DDBJ | PNI76367.1 EMBL· GenBank· DDBJ | Genomic DNA |