- Tools
- Downloads
- Links
- Community
- About
- Help
FB2026_01
,
released March 12, 2026
sry α, sryα, serendipity alpha, srya, sry
Please see the JBrowse view of Dmel\Sry-α 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 6.02
Gene model reviewed during 5.47
Gene model reviewed during 6.05
1.9 (northern blot)
58 (kD observed)
530 (aa); 59 (kD predicted)
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Sry-α 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).
Sry-α is expressed at the maternal to zygotic transition in a pulse that just conincides with cellularization.
Sry-α is expressed at the maternal to zygotic transition in a pulse that just conincides with cellularization.
Sry-α protein is first detected in embryonic cycle 14. Like nullo protein, Sry-α protein forms a co-linear array with the hexagonal actin network, but unlike nullo protein, Sry-α protein localizes to the sides, rather than the vertices of the hexagon. During early cellularization, Sry-α protein is associated with the entire plasma membrane. Additional staining is seen above each cycle 14 nucleus. Sry-α protein remains associated with the invaginating hexagonal array until late in the fast phase of cellularization. Towards the end of the fast phase, the protein becomes dispersed throughout the cytoplasm. It remains detectable until the start of germ band extension.
In embryos, the Sry-alpha protein is detected after nuclear cycle 12, and disappears during gastrulation. During cellularization, the Sry-alpha protein is associated mainly with the apical and furrow membranes, although it does not appear to be an integral membrane protein. It is also found at low levels in the cytoplasm during cellularization, and becomes cytoplasmic at the end of cellularization. Sry-alpha protein co-localizes with F-actin.
JBrowse - Visual display of RNA-Seq signals
View Dmel\Sry-α in JBrowse
3-100
3-97.4
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
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
The molecular organization of the 'rp49-Sry-jan' gene cluster, including gene order, direction of transcription and partial overlap of the janA and janB genes is strictly conserved between D.melanogaster and D.pseudoobscura.pseudoobscura.
The structure and expression of Sry-α has been compared in D.melanogaster, D.pseudoobscura.pseudoobscura and D.subobscura. Highly conserved diverged regions are dispersed throughout the protein. Two out of four conserved 7-13bp motifs found in the 5' promoter region are also found in the nullo gene, which is also involved in cellularization.
Sry-α is required for the reorganization of microfilaments at the onset of membrane invagination in the cellularizing embryo.
Deficiency homozygotes display cellularization defects resulting in multinuclear cells at blastoderm.
The expression pattern and subcellularisation of Sry-α protein suggest that it is involved in the localisation of actin filaments just prior to and during plasma membrane invagination.
Dpse\Sry-α can rescue defects in D.melanogaster Sry-α deletion mutants (Df(3R)X3F), even though the two RNAs have different subcellular distributions.
