Naa80

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Crystal structure of Drosophila melanogaster Naa80. Substrate peptide is shown as yellow sticks and CoA is shown as cyan sticks. Enzyme is displayed as cyan cartoon. (PDB ID: 5WJE)
NAA80
Identifiers
AliasesNAA80, FUS-2, FUS2, N-acetyltransferase 6, NAT6, N(alpha)-acetyltransferase 80, NatH catalytic subunit, HsNAAA80, N-alpha-acetyltransferase 80, NatH catalytic subunit
External IDsOMIM: 607073 MGI: 1888902 HomoloGene: 36325 GeneCards: NAA80
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for NAA80
Genomic location for NAA80
Band3p21.31Start50,296,402 bp[1]
End50,299,421 bp[1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_012191
NM_001200016
NM_001200018

NM_019750

RefSeq (protein)

NP_062724

Location (UCSC)Chr 3: 50.3 – 50.3 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

N-acetyltransferase 80 (also known as NAT6 or FUS2) is a protein that in humans is encoded by the NAA80 gene.[4] It acetylates the N-terminus of mature actin.[5]

Function[edit]

This gene encodes a member of the N-acetyltransferase family. N-acetyltransferases modify proteins by transferring acetyl groups from acetyl-CoA to the N-termini of protein substrates. The encoded protein is a cytoplasmic N-acetyltransferase with a substrate specificity for N-termini that are enriched for acidic residues.[6] This gene is located in the tumor suppressor gene region on chromosome 3p21.3, and the encoded protein may play a role in cancer. Alternatively spliced transcript variants encoding multiple isoforms have been observed. This gene overlaps and is on the same strand as hyaluronoglucosaminidase 3, and some transcripts of each gene share a portion of the first exon. [provided by RefSeq, Jan 2011].

Naa80 acetylates the N-terminus of mature actin. This N-terminal acetylation affects the rates of actin filament depolymerization and elongation, and the overall morphology of the cell.[5]

Structure[edit]

Naa80 is a member of the GNAT family of acetyltransferases.[7] It has an overall fold similar to the other N-terminal acetyltransferases, but has a more open, basic active site to accommodate the acidic N-terminus of actin. Naa80 can acetylate peptides with different N-terminal residues, but the presence of acidic residues in positions 2 and 3 is important for substrate specificity.[7][6] Most Naa80 orthologs have an extended polyproline loop which may be important for actin binding through profilin.[5][7]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000243477 - Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Entrez Gene: N-acetyltransferase 6 (GCN5-related)".
  5. ^ a b c Drazic, A.; Aksnes, H.; Marie, M.; Boczkowska, M.; Varland, S.; Timmerman, E.; Foyn, H.; Glomnes, N.; Rebowski, G.; Impens, F.; Gevaert, K.; Dominguez, R.; Arnesen, T. (2018). "NAA80 is actin's N-terminal acetyltransferase and regulates cytoskeleton assembly and cell motility". Proceedings of the National Academy of Sciences of the United States of America. 115 (17): 4399–4404. doi:10.1073/pnas.1718336115. PMC 5924898. PMID 29581253.
  6. ^ a b Wiame, E.; Tahay, G.; Tyteca, D.; Vertommen, D.; Stroobant, V.; Bommer, G. T.; Van Schaftingen, E. (2018). "NAT6 acetylates the N-terminus of different forms of actin". The FEBS Journal. 285 (17): 3299–3316. doi:10.1111/febs.14605. PMID 30028079.
  7. ^ a b c Goris, M.; Magin, R. S.; Foyn, H.; Myklebust, L. M.; Varland, S.; Ree, R.; Drazic, A.; Bhambra, P.; Støve, S. I.; Baumann, M.; Haug, B. E.; Marmorstein, R.; Arnesen, T. (2018). "Structural determinants and cellular environment define processed actin as the sole substrate of the N-terminal acetyltransferase NAA80". Proceedings of the National Academy of Sciences of the United States of America. 115 (17): 4405–4410. doi:10.1073/pnas.1719251115. PMC 5924903. PMID 29581307.

Further reading[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.