| Literature DB >> 27294183 |
Nicola Franchi1, Francesca Ballin1, Lucia Manni1, Filippo Schiavon1, Loriano Ballarin1.
Abstract
The data described are related to the article entitled "Recurrent phagocytosis-induced apoptosis in the cyclical generation change of the compound ascidian Botryllus schlosseri" (Franchi et al., 2016) [1]. Four apoptosis-related genes, showing high similarity with mammalian Bax (a member of the Bcl-2 protein family), AIF1 (apoptosis-inducing factor-1), PARP1 (poly ADP ribose polymerase-1) and IAP7 (inhibitor of apoptosis-7) were identified from the analysis of the trascriptome of B. schlosseri. They were named BsBax, BsAIF1, BsPARP1 and BsIAP7. Here, their deduced amino acid sequence were compared with known sequences of orthologous genes from other deuterostome species together with a study of their identity/similarity.Entities:
Keywords: AIF1; Alignments; Apoptosis-related transcripts; BLAST analysis; Bax; Botryllus schlosseri; IAP7; PARP1; Sequence databases
Year: 2016 PMID: 27294183 PMCID: PMC4889877 DOI: 10.1016/j.dib.2016.05.017
Source DB: PubMed Journal: Data Brief ISSN: 2352-3409
Fig. 1Alignments of the deduced amino acid sequence of BsBax with known orthologous sequences from both vertebrate and invertebrates.
Fig. 2cDNA and deduced amino acid sequence of BsBax. START and STOP codon are in green and red, respectively; 5′ and 3′ UTR are in grey. In yellow, the Bcl-2 domain and, within this, BH1, BH2 and BH3 domains are underlined. Light blue: transmembrane domain.
Fig. 3Alignments of the deduced amino acid sequence of BsAIF1 with known orthologous sequences from both vertebrate and invertebrates.
Fig. 4cDNA and deduced amino acid sequence of BsAIF1. START and STOP codon are in green and red, respectively; 5′ and 3′ UTR are in grey. Orange: pyridine nucleotide-disulphide domain (PNDD); yellow: NADH-binding PNDD; light blue: C-terminal domain of dimerisation; light purple: nuclear localisation motif. Bold: the N-terminal transmembrane domain.
Fig. 5Alignments of the deduced amino acid sequence of BsPARP1 with known orthologous sequences from both vertebrate and invertebrates.
Fig. 6cDNA and deduced amino acid sequence of BsPARP1. START and STOP codon are in green and red, respectively; 5′ and 3′ UTR are in grey. Light blue: N-terminal zinc-finger domains; pink: PADR1 (poly(ADP-ribose)-synthase 1) domain; bold: BRCT (BRCA1 (breast cancer susceptibility protein C-terminus) domain; light purple: WGR (tryptophane-, glycine-, arginine-rich) motif; orange; C-terminal regulatory PARP domain; yellow: C-terminal catalytic PARP domain.
Fig. 7Alignments of the deduced amino acid sequence of BsIAP7 with known orthologous sequences from both vertebrate and invertebrates.
Fig. 8cDNA and deduced amino acid sequence of BsIAP7. START and STOP codon are in green and red, respectively; 5′ and 3′ UTR are in grey. Orange: BIR domain; blue: RING (really interesting new gene) finger domain.
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