DE-cadherin, E-cadherin, E-cad, DE-cad, Ecad
cadherin - regulates cell aggregation preventing mixing of cells at tissue boundaries - Neuroblast niche position is controlled by PI3-kinase dependent DE-Cadherin adhesion - required for the maintenance of ring canals anchoring to mechanically withstand tissue growth during oogenesis
Please see the JBrowse view of Dmel\shg 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 5.51
5.4 (compiled cDNA)
There is only one protein coding transcript and one polypeptide associated with this gene
150 (kD observed)
1507 (aa); 150 (kD observed)
Interacts (via cytoplasmic region) with Inx2 (via cytoplasmic loop) (PubMed:15047872). Interacts with Hakai (PubMed:19682089). Interacts with Myo31DF (PubMed:22491943).
N-glycosylation is important for biosynthesis and function.
Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\shg using the Feature Mapper tool.
Comment: maternally deposited
Comment: anlage in statu nascendi
Comment: reported as procephalic ectoderm anlage in statu nascendi
Comment: reported as procephalic ectoderm anlage in statu nascendi
Comment: reported as procephalic ectoderm anlage in statu nascendi
Comment: reported as procephalic ectoderm anlage
Comment: reported as procephalic ectoderm anlage
Comment: reported as procephalic ectoderm anlage
Comment: reported as procephalic ectoderm anlage
Comment: reported as procephalic ectoderm primordium
Comment: reported as procephalic ectoderm primordium
Comment: reported as procephalic ectoderm primordium
Comment: reported as procephalic ectoderm primordium
Comment: reported as procephalic ectoderm primordium
Comment: reported as procephalic ectoderm primordium
Comment: reported as labial complex specific anlage
Comment: reported as maxillary organ specific anlage
Comment: reported as salivary gland body specific anlage
Comment: reported as salivary gland duct specific anlage
Comment: reported as larval eye primordium
Comment: reported as head epidermis primordium
Comment: reported as head epidermis primordium
Comment: reported as head epidermis primordium
Comment: reported as salivary gland primordium
shg is expressed in border follicle cells at oogenesis stage 9 before border cell migration. Expression shifts from an anterior band (centripetally migrating follicle cells) at stage S10A to strong expression in midline cells and weak expression in floor and roof cells at stage S10B. Expression continues in stages S11 and S12 in cells forming the dorsal anterior eggshell structures and in posterior follicle cells.
In ocelli, shg is concentrated at the distal and proximal ends of rhabdomeres.
In stage 13 embryos shg is expressed in Malpighian tubule Type II (stellate) cells, particularly those that contact the tubule lumen but is lower than in the neighboring Malpighian tubule Type I (principal) cells. All Malpighian tubule Type II cells contact the luminal surface of the tubules in mid stage 14 and express high levels of shg as well as crb, baz, and dlg1.
At the early third instar, secondary axon tracts form bundles of 20 to 50 fibers traversing the cortex and reaching the cortex-neuropile boundary. All early fibers express shg. In later third instar larvae, these axon tracts have grown and matured and no longer express shg. Late born, immature fibers grow at the center of these tracts and these younger fibers express shg.
shg protein concentrates at hub cell junctions. It is expressed in cyst cells and strongly enriched in the hub.
shg protein is concentrated at the apical portion of cell-cell contacts in differentiated epithelial layers.
shg is expressed in the anterior cluster of somatic gonadal precursor cells in the stage 17 embryonic gonad. It is also expressed in the adult hub.
PPO1 protein is localized to maturing crystal cells in the lymph gland cortical zone.
shg is localized to the adherens junctions of the cell-cell interfaces of all cells of the retina.
In stage 13 embryos,shg protein expression is detected on the cell membrane of both somatic germline precursor cells as well as the germline cells in both males and females. This localization is concurrent with the processes of ensheathment and coalescence of the developing gonad. In stage 17 male embryos, shg protein is concentrated in the anterior of the gonad in the region corresponding to the testes hub.
shg protein was first observed along cell-cell boundaries at the cellular blastoderm stage. At germ band elongation, it is present homogeneously in the epidermal ectoderm of the embryo. shg protein expression persists in the ectodermal epithelia including the epidermis, salivary glands, Malpighian tubules, hindgut and tracheal system throughout embryogenesis.
GBrowse - Visual display of RNA-Seq signals
View Dmel\shg in GBrowse 22-99.7
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 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.
polyclonal
polyclonal antibody
monoclonal
shg mutant border follicle cells display dynamic defects in direction sensing.
shg is necessary for normal morphology of wing margin cells.
The shg protein promotes ommatidial rotation.
In RNAi-treated shg flies, cellularisation proceeds until the onset of gastrulation, where the epithelium collapses and becomes multilayered
shg is required during embryonic development for both germ cell ensheathment and gonad compaction.
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
shg regulates several aspects of tracheal tube fusion.
dsRNA made from templates generated with primers directed against this gene is tested in an RNAi screen for effects on actin-based lamella formation.
shg is required for normal development of the optic placode in embryos.
Asymmetrically distributed shg may regulate the orientation of asymmetric cell division in the sensory organ lineage.
shg is required for anchoring somatic stem cells to their niches in the ovary.
Adhesion between opposing rows of cardioblasts is defective in shg mutant embryos, resulting in the absence of lumen formation.
shg expression is required in border follicle cells and centripetal follicle cells as well as in germline cells for migration of the two groups of follicle cells during oogenesis.
The PCCD domain of shg has a role in efficient recruitment to apical area of plasma membranes crucial for dynamic epithelial morphogenesis.
shg mediates oocyte positioning within the follicle.
Some of the proteins of apico-lateral junctions are required both for apico-basal cell polarity and for the signalling mechanisms controlling cell proliferation, whereas others are required more specifically in cell-cell signalling.
esg positively regulates transcription of shg. Overexpression of shg rescues the defect in one of the fusion points in esg mutants, demonstrating an essential role of shg in target recognition and identifying esg as a key regulator of cell adhesion and motility in tracheal morphogenesis. shg has multiple roles during tracheal branch fusion, it is essential for the initial adhesion and expansion of the lumen.
shg is preferentially required during cell rearrangement in the neurectoderm and other morphogenetically active epithelia.
Zygotic shg expression is required for processes of dynamic epithelial cell rearrangement in the embryo.
shg has been cloned and sequenced.
Principal midgut epithelial cells required shg to assume a columnar epithelial morphology.
Phenotypic analysis of mutants suggests that shg functions to direct adhesion between midgut epithelial cells, and that this adhesion is independent of the adhesion between endoderm and visceral mesoderm.