Please see the JBrowse view of Dmel\Cf2 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 5.48
Annotated transcripts do not represent all supported alternative splices within 5' UTR.
Low-frequency RNA-Seq exon junction(s) not annotated.
Annotated transcripts do not represent all possible combinations of alternative exons and/or alternative promoters.
Tissue-specific extension of 3' UTRs observed during later stages (FBrf0218523, FBrf0219848); all variants may not be annotated
Stop-codon suppression (UAG) postulated; protein extension supported (FBrf0223513).
Gene model reviewed during 6.16
3.6, 2.65 (northern blot); 3.8 (compiled cDNA)
3.5, 2.5 (northern blot)
514, 510, 482 (aa)
One of several products generated by alternative splicing.
The binding properties of the Cf2 protein
isoform I was studied in binding studies with oligonucleotides. Each
finger of the COOH-terminal domain recognizes a contiguous nucleotide
triplet in an antiparallel manner. The optimal targets are GTA for finger
6, TAT for fingers 5 and 5', and ATA for finger 4. The consensus binding
site is GTA.TAT.TAT.ATA where the dots delimit the triplets recognized by
each finger. Protein isoforms I and II recognize different DNA sequences,
suggesting that in vivo these isoforms regulate distinct genes.
The binding properties of Cf2 protein isoform II was studied in binding studies with oligonucleotides. Each finger of the COOH-terminal domain recognizes a contiguous nucleotide triplet in an antiparallel manner. The optimal targets are GTA for finger 6, TAT for finger 5, and ATA for finger 4. The consensus binding site is GTA.TAT.ATA where the dots delimit the triplets recognized by each finger. Protein isoforms I and II recognize different DNA sequences, suggesting that in vivo these isoforms regulate distinct genes.
The binding properties of the Cf2 protein isoform I was studied in binding studies with oligonucleotides. Each finger of the COOH-terminal domain recognizes a contiguous nucleotide triplet in an antiparallel manner. The optimal targets are GTA for finger 6, TAT for fingers 5 and 5'', and ATA for finger 4. The consensus binding site is GTA.TAT.TAT.ATA where the dots delimit the triplets recognized by each finger. Protein isoforms I and II recognize different DNA sequences,suggesting that in vivo these isoforms regulate distinct genes.
Three different protein isoforms of Cf2 are generated as a result of alternate splicing of the Cf2 transcript. All three contain three amino-terminal Zn fingers which do not appear to contribute to specific DNA sequence recognition. Isoform III contains no other Zn-fingers as a result of the absence of exon 3 and the resultant frameshift.
Three different protein isoforms of Cf2 are generated as a result of alternate splicing of the Cf2 transcript. All three contain three amino-terminal Zn fingers which do not appear to contribute to specific DNA sequence recognition. Isoform II contains 3 additional fingers, each of which recognizes a contiguous nucleotide triplet in an antiparallel manner. The preferred DNA binding sites were defined in a companion paper (FBrf 57626). A nearly perfect consensus sequence for isoform II is found in the Cp15 promoter. Protein isoforms I and II recognize different DNA sequences, suggesting that in vivo these isoforms regulate distinct genes.
Three different protein isoforms of Cf2 are generated as a result of alternate splicing of the Cf2 transcript. All three contain three amino-terminal Zn fingers which do not appear to contribute to specific DNA sequence recognition. Isoform I contains 4 additional fingers, each of which recognizes a contiguous nucleotide triplet in an antiparallel manner. The preferred DNA binding sites were defined in a companion paper (FBrf 57626). The Cf2 gene itself has a possible Cf2 isoform I protein recognition sequence suggesting that isoform I may be used to autoregulate Cf2 expression. Protein isoforms I and II recognize different DNA sequences, suggesting that in vivo these isoforms regulate distinct genes.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Cf2 using the Feature Mapper tool.
Comment: maternally deposited
GBrowse - Visual display of RNA-Seq signals
View Dmel\Cf2 in GBrowse 22-14
2-15.4
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 merge of: Cf2 BcDNA:GM09668
Source for merge of Cf2 BcDNA:GM09668 was a shared cDNA ( date:030728 ).
RNAi generated by PCR using primers directed to this gene causes a cell growth and viability phenotype when assayed in Kc167 and S2R+ cells.
Cf2 zinc fingers function in DNA binding in vitro and in vivo and site-specific mutagenesis and binding site selection define the critical amino acid-base interactions in detail.
Cf2 protein functions as a repressor of dorsally expressed genes.
Ectopic expression or depletion of Cf2 alters the dorsoventral polarity of the egg chamber. Mosaic analysis suggests that loss of Cf2 can lead to overproduction of dorsal appendage material. Ectopic expression of Cf2 counteracts the dorsalising effect of fs(1)K10 mutants but exacerbates heterozygous Egfr torpedo mutant phenotypes.
Cf2-I and Cf2-II, the two major forms of chorion transcription factor, differ by an extra Zn-finger within DNA binding domain, due to alternative splicing. Preferred DNA binding sites were determined for each by in vitro binding studies and are distinguished by internal duplication of TAT in the site recognised by form with extra finger. Modular interactions between fingers and trinucleotides together with alternative splicing of Cf2 cause altered binding specificity and target site recognition by DNA binding domains. Cf2-II binding is to AT-rich regions in the Cp15 promoter.
Cf2 transcripts are subject to developmentally regulated alternative splicing, to generate protein isoforms that differ in the number of Zn fingers. These different products bind to distinct promoters and DNA target sequences: Cf2-II isoform binds tightly to Cp15 chorion gene promoter whereas Cf2-I binds only weakly, but Cf2-I binds to the Cf2 promoter itself whereas Cf2-II doesn't.
Encodes a protein that binds the promoter region of Cp15.
