APP, APP-like, dAβ, EG:65F1.5 , Amyloid Precursor Protein-like
β amyloid homolog - contributes to synapse formation, maintenance, and plasticity - crucial N- and C-terminal specific sequences result in neurotoxicity and aggregation
Please see the JBrowse view of Dmel\Appl for information on other features
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AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Transposon inserted in intron
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.46
Gene model reviewed during 5.55
6.5 (unknown)
None of the polypeptides share 100% sequence identity.
886 (aa); 145, 130 (kD)
886 (aa); 98 (kD)
The 145kD and 130kD forms of the protein are made
from the same gene as shown by the presence of both forms in S2 cells
transfected with a heat shock Appl gene construct. The 145kD form was
shown to be a precursor which is rapidly converted to the 130kD form.
The 130kD Appl protein is a secreted form which
lacks the cytoplasmic domain and the membrane-spanning domain. It was
shown to accumulate in the culture medium of cultured embryonic cells.
Interacts (via the intracellular domain, ICD) with APP-BP1.
The NPTY motif mediates the interaction with clathrin (By similarity). The clathrin-binding site is essential for its association with X11-alpha, -beta, and -gamma. The sequence specific recognition extends to peptide residues that are C-terminal to the NPXY motif. This interaction appears to be independent of phosphorylation (By similarity).
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Appl 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).
The 145kD precursor form of the Appl protein is membrane-associated.
Appl protein is observed in a punctate pattern in the cytoplasm of neuronal cell bodies in larvae. This pattern is present in the ventral ganglion, the brain lobes and the photoreceptors. In the neuropil, the staining is not as homogenous. Strong uniform staining is observed in the neuropil of the three thoracic and eighth abdominal neuromeres. Staining is also observed in the neuropil of the brain lobes. Appl protein is observed in certain axons e.g. in the photoreceptor axons in the eye stalk. The membrane form appears to be enriched in regions where Appl protein is associated with neuronal processes (optic stalk and optic lobe). The pattern of Appl protein staining in the neuropil undergoes dynamic changes during metamorphosis. In the adult, the highest levels are found in the neuropil of the mushroom bodies. Staining is also observed in the brain, thoracic ganglion, lamina, and medulla.
Appl protein is observed in a punctate pattern in the cytoplasm of neuronal cell bodies in larvae. This pattern is present in the ventral ganglion, the brain lobes and the photoreceptors. In the neuropil, the staining is not as homogenous. Strong uniform staining is observed in the neuropil of the three thoracic and eighth abdominal neuromeres. Staining is also observed in the neuropil of the brain lobes. Appl protein is observed in certain axons e.g. in the photoreceptor axons in the eye stalk. The secreted form appears to be enriched in regions where Appl protein is not associated with neuronal processes (thoracic neuromeres). The pattern of Appl protein staining in the neuropil undergoes dynamic changes during metamorphosis. In the adult, the highest levels are found in the neuropil of the mushroom bodies. Staining is also observed in the brain, thoracic ganglion, lamina, and medulla.
The 130kD form of Appl protein is secreted into the culture medium of primary embryonic cells and S2 cells.
Appl protein is nervous system specific. In embryos, it is abundant in the axon tracts of commissures in the brain and ventral cord. In larvae, it is present in the brain and ventral cord. In the eye disc, it is localized behind the morphogenetic furrow. There is a gap of several columns between the morphogenetic furrow and cells containing Appl protein.
JBrowse - Visual display of RNA-Seq signals
View Dmel\Appl 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.
Appl is not required for learning but is specifically involved in long-term memory.
The Appl cytoplasmic domain is required to promote synapse formation, being essential for both the satellite bouton-promoting activity and the formation of extra parent boutons caused when Appl is overexpressed. The satellite bouton-promoting activity depends on the presence of the internalization signal, the formation of extra parent boutons depends on the presence of an intact extracellular domain. The distribution of Appl is altered in hyperexcitable mutants.
Appl promotes synapse differentiation at the neuromuscular junction.
Appl defines a locus in the position 1B that has previously been shown to be important for neural development.
The Appl gene is important for neural development.
The Appl gene is known to be homologous to the human protein associated with Alzheimer disease.
The APPL-encoding gene initially suggested (FBrf0050824) to correspond to vnd, but this has been disproved, since a terminal deletion which retains vnd+ function removes most of the Appl coding sequences (FBrf0051559).
