Spectrin, l(1)G0074, karussell, βspec, l(1)G0108
Gene model reviewed during 5.47
Low-frequency RNA-Seq exon junction(s) not annotated.
None of the polypeptides share 100% sequence identity.
Native spectrin molecule is a tetramer composed of two antiparallel heterodimers joined head to head so that each end of the native molecule includes the C-terminus of the alpha subunit and the N-terminus of the beta subunit.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\β-Spec using the Feature Mapper tool.
β-Spec protein is expressed in the axon at the neuromuscular junction into a lattice-like structure.
GBrowse - Visual display of RNA-Seq signalsView Dmel\β-Spec 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 merge of β-Spec anon- EST:fe1B3 was sequence comparison ( date:030620 ).
β-Spec is essential in neurons, but is not required in other cells for development of fertile adult males, although females lacking non-neural spectrin are sterile.
β-Spec is required for normal axonal morphogenesis and is required to establish or maintain the normal structure of growth cones needed for precise axonal patterning.
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
The absence of spectrins disrupts neurotransmission but does not alter postsynaptic glutamate receptor field function or the ultrastructural localization of presynaptic vesicles. The subcellular location of many synaptic proteins is affected.
Spectrin is necessary for the capture and tethering of membrane associated proteins required for presynaptic neurotransmitter release.
Mutations in β-Spec are lethal during late embryonic/early larval development and produce subtle defects in midgut morphology and stomach acid secretion.
Four EMS induced alleles were identified in a screen for mutations affecting commissure formation in the CNS of the embryo.
Elimination of α-Spec from follicle cells does not appear to prevent the assembly of conventional β-Spec and Ank products at the lateral domain of the follicle cell plasma membrane. However α-Spec is required for the correct localization of ΒH-spectrin to the apical surface.
The distribution of β-Spec product suggests roles in establishing an apicolateral membrane domain that is known to be rich in intercellular junctions and in establishing a unique membrane domain associated with contractile processes.
Recombinant proteins constructs of α-Spec and β-Spec, whose primary structures correspond to the regions required for tail end interchain binding, demonstrate that interchain binding depends on multiple sites within both the nonrepetitive segments and adjacent repetitive segments of both chains.
A β-Spec cDNA has been sequenced and the predicted amino acid sequence has been compared with a number of other spectrins.
β-spectrin forms an elongated heterodimer with α-spectrin to form an important cytoskeletal component.
"karussell" means "merry-go-round" in German.