polypeptide GalNAc transferase 4
O-glycosyltransferase - initiates the formation of mucin-type O-linked glycans - regulates secretion of components of the peritrophic/mucous membrane in the larval digestive tract - mutation can be rescued by expression of conserved cargo receptor Tango1 and partially rescued by supplementation with exogenous mucins or treatment with antibiotics - mutants exhibit disruption of the mucosal barrier, resulting in epithelial expression of the IL-6-like cytokine Upd3, leading to activation of JAK/STAT signaling, differentiation of cells that form the progenitor cell niche and abnormal proliferation of progenitor cells
Gene model reviewed during 5.46
There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Pgant4 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Pgant4 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.
Source for identity of: pgant4 CG31956