Spectrin, alpha-spectrin, αSpec, l(3)dre3, alpha Spectrin
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.46
Shares 5' UTR with upstream gene.
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. Interacts with calmodulin in a calcium-dependent manner, interacts with F-actin and also interacts with Lva. Interacts with Ten-m.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\α-Spec using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\α-Spec in GBrowse 2
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.
Source for identity of: α-Spec CG1977
One or more of the processed transcripts for this gene share(s) untranslated sequences with a transcript of an adjacent gene, but encode(s) a single open reading frame (ORF). The non-overlapping ORFs that share untranslated sequences are represented by dlt and α-Spec.
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
The dlt open reading frame is located within the first intron of α-Spec and the two genes share a common first untranslated exon. Overall orientation not stated: Patj- CG12020- Cdc37- α-Spec+ dlt+ α-Spec+
Spectrin is necessary for the capture and tethering of membrane associated proteins required for presynaptic neurotransmitter release.
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.
Four EMS induced alleles were identified in a screen for mutations affecting commissure formation in the CNS of the embryo.
α-Spec is required for ovarian follicle monolayer integrity. 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.
Clonal analysis demonstrates α-Spec is required in the germline (but not in the follicle cells) for cyst formation and oocyte differentiation. Its role in each process is distinct from that of hts protein. The organisation of membrane skeletal proteins is more dependent on α-Spec in the fusome than at the plasma membrane in other cells. The fusome and associated membrane skeleton play a central role in regulating the divisions and differentiation of cyst cells.
The results of clonal analysis suggest that spectrin is involved in the spatial arrangement of the follicle cell population during oocyte development.
Recombinant proteins constructs of α-Spec and β-Spec, whose primary structures correspond to the regions required for tail end interchain binding (segments 19-22 of α-Spec and segments 1-4 of β-Spec), demonstrate that interchain binding depends on multiple sites within both the nonrepetitive segments and adjacent repetitive segments of both chains.
The structure of one of the repetitive segments of α-Spec has been determined at 1.8 angstrom resolution. The segment consists of a three helix bundle. Hydrophobic interactions between two tandem segments may constrain intersegment flexibility.
Various regions of the α-Spec molecule exhibit structural autonomy thus enabling fragments of the molecule to fold properly when expressed in bacteria. Results localise the calmodulin binding and calcium binding sites within specific segments of the protein.
Single repetitive motifs and pairs of motifs can fold into stable conformations similar to that of native α-Spec when their N-terminal ends are 26 residues downstream of the residue that has usually been designated to be the first position of each repetitive motif.
Mutant hemizygotes are larval lethal; dying in the first or (rarely) second instar.
"klotzchen" means "small building block" in German.