A0A074Z035 · A0A074Z035_9TREM

  • Protein
    Alpha-tubulin N-acetyltransferase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Features

Showing features for site, binding site.

TypeIDPosition(s)Description
Site55Crucial for catalytic activity
Binding site116-129acetyl-CoA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmicrotubule
Molecular Functiontubulin N-acetyltransferase activity
Biological Processneuron development
Biological Processregulation of microtubule cytoskeleton organization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-tubulin N-acetyltransferase
  • EC number
  • Short names
    Alpha-TAT
    ; TAT
  • Alternative names
    • Acetyltransferase mec-17 homolog

Gene names

    • ORF names
      T265_11140

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Spiralia > Lophotrochozoa > Platyhelminthes > Trematoda > Digenea > Opisthorchiida > Opisthorchiata > Opisthorchiidae > Opisthorchis

Accessions

  • Primary accession
    A0A074Z035

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain1-182N-acetyltransferase
Region206-313Disordered
Compositional bias215-284Polar residues
Compositional bias285-307Basic and acidic residues

Sequence similarities

Belongs to the acetyltransferase ATAT1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    361
  • Mass (Da)
    41,576
  • Last updated
    2014-10-01 v1
  • Checksum
    C2A26821AB4F617F
MEFAFRIRDFLNNEIAHLTPDLLNKPPFTHGNVNTTWNNIRELIDTMGEYSAHAQNLPHVVTNFKKFSASDHNLYVLSDVNLNRVIGFLKTGKKRLFMHDSQGLCTEAEPLCVLDFYIHESCQRKGHGKRLFDYMLQVENVAPPSLAIDSPSRKMLHFLSRHYHLDRPIFSSNNFVIYPGFFSFSNNIRKVYQDFRTVYSTNDRKTVLPYGDRSSPRKSRSSQLVRTVDNRVQPHHSTPHTEITVRSAMELTSPSQAKTDWKPSSLAHTNEQSITSTNPRNKTSKSIDSDCKNPEKSSKDDVDKNPSGHFPCIDTKARENYSVISSQELRLLRGLPDGRRTSHEYSYLNAVRNHNGHRKLW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias215-284Polar residues
Compositional bias285-307Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KL597072
EMBL· GenBank· DDBJ
KER20278.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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