Please see the JBrowse view of Dmel\snk 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 5.47
Multiphase exon postulated: exon reading frame differs in alternative transcripts.
1.65 (northern blot)
430 (aa)
The carboxy terminus of snk protein has sequence similarity to serine proteases such as rat preproelastase and trypsinogen. The amino terminus has a short region of amino acid identity with troponin C, and a highly acidic region reminiscent of the calcium binding region of troponin C and calmodulin, suggesting that there may be a calcium-binding site near the amino terminus of snk.
Interacts (via N-terminal prodomain) with ea/easter (via Peptidase domain); leads to proteolytic activation of ea by snk (PubMed:20605458). This interaction does not require sulfation of a vitelline membrane component by pip but proteolytic cleavage of ea by snk does (PubMed:20605458).
Proteolytically activated by gd (PubMed:20605458). May also be cleaved by another protease (PubMed:20605458).
The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\snk 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).
Comment: reference states 0-4 hr AEL
JBrowse - Visual display of RNA-Seq signals
View Dmel\snk in JBrowsePlease 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.
The level of activated snk protease can define cell fates along the dorsal-ventral axis in a concentration-dependent manner. Asymmetric injection of activated snk protease into wild type embryos suggests that the embryos may generate a snk activation gradient with a high point on the ventral side and a low point on the dorsal side. snk and ea proteases are members of a sequential protease activation pathway, snk and ea interact with other components of the dorsal-ventral pathway.
Responds most strongly of all maternal dorsalized mutants to rescue by injection of cytoplasm and poly(A)+ RNA from wild-type embryos. Injection of wild-type cytoplasm or cytoplasm from other dorsalizing maternal-effect mutants into pre-pole-cell snake embryos fully restores the normal dorsal-ventral pattern and more than 20% can develop into normal adults; the site of injection appears to be unimportant. Partial rescue also achieved by the injection of polyA+ but not poly(A)- RNA isolated from cleaving embryos.
Strong dorsalizing mutants of snk have wild type axial ratios in pupae.
Mutations in maternal dorsal class gene snk do not interact with RpII140wimp.
Involved in the regulatory hierarchy responsible for the asymmetric distribution and function of zygotic regulatory gene products along the DV axis of early embryos.
Molecular cloning and analysis of snk.
FlyBase curator comment: the insertion in the "e03379" Exelixis line (PBac{RB}CG11670e03379) was originally assigned to the snk gene in FBrf0179797, resulting in the "snke03379" (FBal0158624) allele. However, FBrf0184340 shows that the insertion is actually within CG11670.