dCaM, CalA, lincRNA.S2634, D-CaM
calcium ion binding signaling protein - regulation of cellular processes dependent on Ca2+ - An Abnormal spindle-CaM complex is required for centrosome-pole cohesion and centrosome inheritance in neural stem cells - affects sensitization of odorant receptors - interacts synergistically with Abelson tyrosine kinase and Calmodulin to transduce midline guidance cues in the Drosophila embryonic CNS
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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.
Tissue-specific extension of 3' UTRs observed during later stages (FBrf0218523, FBrf0219848); all variants may not be annotated
Stage-specific extension of 3' UTRs observed during embryogenesis (FBrf0215804); all variants may not be annotated.
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.46
Gene model reviewed during 5.55
4.2 (northern blot)
1.6 (compiled cDNA)
148 (aa)
Methionine only
Site directed mutagenesis was used to create 4 mutants. In each, a conserved glutamic acid residue within one of the Ca2+-binding sites has been replaced with glutamine, thus creating four Cam proteins with analagous mutations in each of the Ca2+-binding sites. Conformational studies on these mutants confirm that the carboxy-terminal two sites show cooperative Ca2+ binding which produces a major change in the protein conformation. The amino terminal Ca2+-binding sites show more independent properties with respect to Ca2+ binding and conformational change. Mutants at the amino-terminal sites were shown to affect conformational change induced by Ca2+ binding at the carboxy-terminal end. This work supports the idea that the carboxy-terminal sites are high affinity for Ca2+ binding and the amino-terminal sites are lower affinity.
Interacts with Crag (PubMed:18331716). Interacts with stac (PubMed:9813038). Interacts with Akap200; the interaction is calcium-dependent and is inhibited by PKC-mediated phosphorylation of Akap200 (PubMed:10480937).
Trimethylation of Lys-116 observed in other calmodulins is absent here, but does occur at Lys-95 specifically in the compound eye.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Cam using the Feature Mapper tool.
The testis specificity index was calculated from modENCODE tissue expression data by Vedelek et al., 2018 to indicate the degree of testis enrichment compared to other tissues. Scores range from -2.52 (underrepresented) to 5.2 (very high testis bias).
Comment: maternally deposited
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 hindgut proper anlage
Comment: extended 3' UTR isoform
Comment: reported as dorsal/lateral sensory complexes
Zygotic-specific isoforms of Cam with long 3' UTR extensions were observed.
Northern analysis reveals a strongly-expressed doublet of Cam transcript from early embryonic stages through early third instar larval stage (0-89hr AEL), then drops precipitously in late third instar larvae (90-120 hr AEL). Expression increases to a moderate level during pupal stages 7-8 (150-176 hr AEL). Maternally expressed Cam transcript is homogenously distributed through embryonic stage 6. From embryonic stage 14, Cam transcript is expressed in developing central nervous system. In adults Cam transcript is localized to the cell bodies surrounding the lamina, medulla, and lobula, and in cell bodies of the subesophageal ganglion and photoreceptor cells.
Comment: expression throughout adult brain neuropil, concentrated around outside areas
Comment: expression in all neuropil areas ( adult subesophageal ganglion, supraesophageal ganglion ), higher in localised areas possibly layered or punctate
Comment: expression in all neuropil areas ( adult subesophageal ganglion, supraesophageal ganglion ), higher in localised areas possibly layered or punctate
JBrowse - Visual display of RNA-Seq signals
View Dmel\Cam in JBrowse2-66
2-68.0
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 JBrowse 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.
Cam is involved in centriole duplication and is required for efficient recruitment of pericentriolar material.
RNAi screen using dsRNA made from templates generated with primers directed against this gene results in unfocused spindle microtubules and pole detachment when assayed in S2 cells. This phenotype can be observed when the screen is performed with or without Cdc27 dsRNA.
RNAi screen using dsRNA made from templates generated with primers directed against this gene results in kinetochore-fiber unfocusing and centrosome detachment phenotypes when assayed in S2 cells.
Expression is enriched in embryonic gonads.
The interaction of Cam domains with target peptides derived from the target sequence of sk-MLCK is investigated.
Identification: Enhancer trap expression pattern survey for loci expressed in the ring gland.
The complex expression patterns of Cam are examined.
The effects of Ca-Cam on light adaptation, light- and chemically induced Ca2+ release from internal stores, and the resulting inward current are examined using whole cell patch-clamp and fluorimetric recordings from photoreceptor cells. Negative regulation of Ca-Cam on Ca2+ release from ryanodine-sensitive stores is essential for light excitation and light adaptation and for keeping the store-operated current (ISOC) under a tight control.
The stability of Cam can be dramatically reduced by mutation of a single highly conserved residue, but changes in solvent or in the binding of a target sequences can readily compensate for this, restoring the wild-type properties.
Cam protein coordinates termination of the light response in photoreceptor cells by modulating receptor and ion channel activity.
Isoforms of CaMKII have similar biochemical properties, they exhibit differential activity by mutant Cam proteins. Data supports a role for the C-terminal variable region of CaMKII in the mechanism of activation and demonstrate that stimulation of CaMKII catalytic activity by Cam is a multistep process, with separate binding and activation steps.
The spontaneous avoidance behaviour of Cam null mutants has striking similarities to the enhanced avoidance response produced by some calmodulin mutations in Paramecium. This suggests evolutionary conservation of a role for calmodulin in membrane excitability and linked behavioural responses.
UV-difference spectroscopy and near-UV CD are used to monitor conformational changes to Tyr-138. The ability of Cam mutants to activate one of the target enzymes of Cam, Strn-Mlck, is examined. Results provide strong evidence that events in the N-terminal lobe of Cam are detected in the C-terminal lobe, as monitored by Tyr-138.
Clonal analysis suggests that Cam null clones in the PNS result in abnormal differentiation of the sense organs, and that null clones in all tissues are generally small, if not deleted.
Null Cam individuals die as first larval instar. Larvae display a locomotor defect, they have backward movements 50% of the time and these occur spontaneously in the absence of any overt stimulus.
Calcium signaling in the growth cone is required for proper axon pathfinding. Calcium may in part regulate certain growth cone decisions, including whether or not to cross the midline.
Backbone dynamics of Cam, studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy, reveal the central helix is flexible.
The pattern of Cam RNA expression during embryogenesis has been analysed.
Stopped-flow kinetic methods have been used to study the Ca2+ binding properties of Cal mutants.
Circular dichroism measurements were used to assess Ca2+-induced changes in secondary and tertiary structure of calmodulin. In vitro mutagenesis alleles assayed in cell free translation systems revealed significant interaction between N and C terminal domains required for Ca2+ binding.
Calcium binding properties and calcium induced conformation changes of mutant proteins is studied.
Comparison of CpG distribution in the coding region of 121 genes from six species supports the mCpG mutational hotspot explanation of CpG suppression in methylated species at position II-III and III-I.
Calcium-induced conformational changes have been studied in Cal by the use of a hydrophobic reporter molecule 9AC, this results in the exposure of hydrophobic surfaces on the protein.
Complete 1H and 13C side chain assignments and the secondary structure of Cam in solution are determined using NMR spectroscopy.
The crystal structure of Cal as expressed in a bacterial system has been determined and refined at 2.2-A resolution. This structure is compared with the structure of the mammalian calmodulin protein.
Structure and expression studies of the single Cal gene have found that the gene encodes a tiny additional 5' exon encoding only 50 residues of the 5' leader. Two transcript classes are derived from the gene as a result of alternative polyadenylation site usage, the sites are developmentally regulated.
The structure and sequence of the Cal gene has been determined.
The structural gene for the calcium-binding protein, calmodulin.
Source for merge of: Cam anon- EST:Posey59
l(2)k08317 may correspond to Cam: the P{lacW}l(2)k08317k08317 insertion maps within the transcription unit.