A0A074Z035 · A0A074Z035_9TREM
- ProteinAlpha-tubulin N-acetyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids361 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
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 | microtubule | |
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
- EC number
- Short namesAlpha-TAT ; TAT
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Platyhelminthes > Trematoda > Digenea > Opisthorchiida > Opisthorchiata > Opisthorchiidae > Opisthorchis
Accessions
- Primary accessionA0A074Z035
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-182 | N-acetyltransferase | ||||
Sequence: MEFAFRIRDFLNNEIAHLTPDLLNKPPFTHGNVNTTWNNIRELIDTMGEYSAHAQNLPHVVTNFKKFSASDHNLYVLSDVNLNRVIGFLKTGKKRLFMHDSQGLCTEAEPLCVLDFYIHESCQRKGHGKRLFDYMLQVENVAPPSLAIDSPSRKMLHFLSRHYHLDRPIFSSNNFVIYPGFF | ||||||
Region | 206-313 | Disordered | ||||
Sequence: TVLPYGDRSSPRKSRSSQLVRTVDNRVQPHHSTPHTEITVRSAMELTSPSQAKTDWKPSSLAHTNEQSITSTNPRNKTSKSIDSDCKNPEKSSKDDVDKNPSGHFPCI | ||||||
Compositional bias | 215-284 | Polar residues | ||||
Sequence: SPRKSRSSQLVRTVDNRVQPHHSTPHTEITVRSAMELTSPSQAKTDWKPSSLAHTNEQSITSTNPRNKTS | ||||||
Compositional bias | 285-307 | Basic and acidic residues | ||||
Sequence: KSIDSDCKNPEKSSKDDVDKNPS |
Sequence similarities
Belongs to the acetyltransferase ATAT1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length361
- Mass (Da)41,576
- Last updated2014-10-01 v1
- ChecksumC2A26821AB4F617F
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 215-284 | Polar residues | ||||
Sequence: SPRKSRSSQLVRTVDNRVQPHHSTPHTEITVRSAMELTSPSQAKTDWKPSSLAHTNEQSITSTNPRNKTS | ||||||
Compositional bias | 285-307 | Basic and acidic residues | ||||
Sequence: KSIDSDCKNPEKSSKDDVDKNPS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KL597072 EMBL· GenBank· DDBJ | KER20278.1 EMBL· GenBank· DDBJ | Genomic DNA |