Bc, Black cells, proPO-A1, Mox, Black cell
Please see the JBrowse view of Dmel\PPO1 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.
Gene model reviewed during 5.50
There is only one protein coding transcript and one polypeptide associated with this gene
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\PPO1 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).
PPO1 protein is localized to maturing crystal cells in the lymph gland cortical zone.
JBrowse - Visual display of RNA-Seq signals
View Dmel\PPO1 in JBrowse2-84
2-87.2
2-79.6
2-80.6
2-78.2
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.
monoclonal
polyclonal
New stable cell line derived from S2-unspecified : A stable cell line expressing rBip-PPO1 (PPO1 fused with a signal peptide) was constructed.
PPO1 and PPO2 are the main source of phenoloxidase (PO) activity in the hemolymph (double mutants show no hemolymphatic PO activity upon wounding or after microbial infection). The two genes are not fully redundant: PPO1 is involved in the rapid early delivery of phenoloxidase activity when it is required, while PPO2 protein is accumulated in the crystals of crystal cells and provides a storage form that can be deployed in a second phase. PPO1 and PPO2 have a role in the survival of infection with Gram-positive bacteria and fungi.
Males have a minimum level of phenol oxidase activity that protects them from mechanical damage of cuticle or toxic effects. Females have high levels of phenol oxidase, may be caused by their reproductive function.
Mutants in Bc cause the loss of prophenoloxidase activity. Encapsulation of eggs from the parasitoid strain L.boulardi demonstrate that phenoloxidases are required only for blackening and hardening of haemolytic capsules.
The primary defect in Bc mutants may involve the loss of the physical barrier between phenol oxidase and its substrate in the crystal cells, which results in the melanisation of the cells in the mutant.
Phenol oxidase activity is reduced in heterozygous larval cell-free extracts and undetectable in homozygous larval cell-free extracts.
The Bc[+] product may be required for binding the substrate of phenol oxidase in the paracrystalline structures of the crystal cells so that it is inaccessible to the phenol oxidase enzyme.
Source for merge of: PPO1 Bc
The Bc (Black cells) mutation (FBal0001073) is a gain-of-function mutation in the PPO1 (CG42639) gene. The A480V lesion in PPO1 which is found in the Bc mutant allele is necessary and sufficient to phenocopy both the dominant Bc phenotype of spontaneously melanised crystal cells and the recessive Bc phenotype of defective melanisation after wounding. This indicates that the A480V lesion is the causal mutation of the Black cells phenotype and that Bc is allelic to PPO1.
"Phox" may correspond to "proPO-A1", since they map to the same location and both show monophenol oxidase activity.
It is unlikely that Phox corresponds to proPO-A1 (the A1 component of phenol oxidase described in FBrf0017315).
Source for identity of: proPO-A1 CG42639
Source for identity of: PPO1 proPO-A1
