Gene model reviewed during 5.45
None of the polypeptides share 100% sequence identity.
1047 (aa); 77, 35 (kD observed)
A 112kD proprotein is processed into two peptides of 35kD (amino-terminal) and 77kD (carboxy-terminal).
The 77kD mas protein is a carboxy-terminal peptide processed from the FBgn0011653:mas @ proprotein.
Proteolytically cleaved and thereafter secreted.
The CLIP domain consists of 37-55 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\mas using the Feature Mapper tool.
The 77kD mas peptide is detected in the attachment sites of somatic embryonic muscles starting in stage 16 and persisting until the beginning of pupation. It is thought to be secreted into the intercellular region of the attachment site by the epidermal cells. The polypeptide is also found in the tracheal lumen. In the CNS, the mas peptide is found in midline cells and in the axons of the longitudinal connectives, again consistent with it being secreted.
GBrowse - Visual display of RNA-Seq signalsView Dmel\mas in GBrowse 2
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 GBrowse 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.
mas is expressed in relevant cell types during embryonic, larval and pupal life. Total loss of mas function in the embryo results in defects in the axonal connectivities of the motor as well as sensory axons. Defects in information processing by the neuronal pathways is the underlying cause for the aberrant taste behaviour exhibited by larvae and adults mutant for mas.
Total loss of mas function causes defective muscle attachment, this suggests mas normally acts to stabilise cell-matrix interaction and represents a novel functional and limiting component in the adhesion process.