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FB2026_01
,
released March 12, 2026
actin, Arthrin, F-actin, E
Please see the JBrowse view of Dmel\Act88F for information on other features
To submit a correction to a gene model please use the Contact FlyBase form
AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Gene model reviewed during 5.47
1.77 (northern blot)
There is only one protein coding transcript and one polypeptide associated with this gene
N-terminal cleavage of acetylated cysteine of immature actin by ACTMAP.
Oxidation of Met-45 by Mical to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Act88F using the Feature Mapper tool.
The testis specificity index was calculated from modENCODE tissue expression data by Vedelek et al., 2018 to indicate the degree of testis enrichment compared to other tissues. Scores range from -2.52 (underrepresented) to 5.2 (very high testis bias).
JBrowse - Visual display of RNA-Seq signals
View Dmel\Act88F in JBrowse
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see JBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
Haploinsufficient locus (not associated with strong haplolethality or haplosterility).
S2 cells treated with dsRNA generated against this gene show reduced phagocytosis of Candida albicans compared to untreated cells.
Mutants show decreased walking ability and delayed/reduced oviposition.
In a sample of 79 genes with multiple introns, 33 showed significant heterogeneity in G+C content among introns of the same gene and significant positive correspondence between the intron and the third codon position G+C content within genes. These results are consistent with selection adding against preferred codons at the start of genes.
Age related changes in Act88F expression have been studied by Northern analysis.
Ecol\lacZ reporter gene constructs have been used to label larval muscle fibres. A laser microbeam is used to ablate the muscle fibres singly and in combination. The results show that the persistent larval muscle fibres are not required to initiate the fusion of imaginal myoblasts, to indicate the correct placement of the resulting fibers in the thorax or to designate the identity of the fibres. Persistent larval muscle fibres are required to determine the correct number of fibres formed.
Interaction of wild type and mutant actin with rabbit myosin and its proteolytic subfragments is investigated.
A modified pair of optical tweezers, transducer based, is used to compare the response of wild type and mutant actins and the fibre attachment and detachment forces.
Sequence analysis demonstrates insect muscle actins form a distinct family of closely related proteins significantly diverged from cytoplasmic actins.
Properties of mutant proteins transcribed in vitro are studied.
The effects of missense Act88F mutants on the structure and function of indirect flight muscles was examined.
Combined in vitro and in vivo studies are used to investigate the relationship between amino acid sequence and function for the specificity of Act88F. Act88F protein expressed in vitro and in vivo binds to DNaseI with equal affinity and are able to copolymerise with bulk rabbit actin equally well. Unprocessed actins are less able to copolymerize with bulk actins. Results suggest that individual actins do interact, even in nonpolymerizing conditions. The reduced ability of unprocessed actin to polymerize shows that correct post-translational modification of the N terminus is required for normal actin function.
Translation of actin RNA in early embryos injected with initiation factors has been studied.
Myofibril degeneration is not the primary cause of anomalous heat shock gene activation by mutant actins.
Genetic analysis of muscle contraction using the indirect flight muscles of D.melanogaster.
In vitro mutagenesis was performed on Act88F to generate mutations that can assemble into virtually normal myofibrils.
An equivalent mutation found in human β-actin was constructed in Act88F to investigate the nature of the mutation in vivo. The mutation caused defects in the actin molecule that could be visualized as a disturbance of the filament lattice.
Expressed only in the indirect flight muscles. Act88F mutant flight muscle has an unusual configuration of myosin crossbridges under EM.
Encodes the indirect flight muscle actin (FBrf0038990; FBrf0042420). Haplo-insufficient; heterozygotes for null mutations or Act88F deficiencies are flightless; flightlessness is apparently caused by imbalance between myosin heavy chains and Act88F protein; whereas hemizygosity for either Mhc or Act88F leads to complex myofibrillar defects and flightlessness, double hemizygotes have nearly normal fibrillar structure and are able to fly (FBrf0049803). Heterozygotes and to a greater degree, homozygotes and heteroallelic heterozygotes for antimorphic alleles Act88F4 and Act88F5 show constitutive synthesis of heat-shock proteins, with Hsp26 and Hsp27 less actively synthesized than Hsp22, Hsp70 and Hsp83; response to heat shock normal (FBrf0042420).
Source for identity of: Act88F CG5178
