Additional file 1: of New genomic data and analyses challenge the traditional vision of animal epithelium evolution
Creators: name: Hassiba Belahbib
name: Renard, Emmanuelle
name: Santini, Sébastien
name: Jourda, Cyril
name: Jean-Michel Claverie
name: Borchiellini, Carole
name: Bivic, André Le
Publisher: name: figshare
Year: 2018
Subjects: subject: Biophysics
subject: Biochemistry
subject: Microbiology
subject: FOS: Biological sciences
subject: FOS: Biological sciences
subject: Genetics
subject: Molecular Biology
subject: Evolutionary Biology
subject: 69999 Biological Sciences not elsewhere classified
subject: Developmental Biology
subject: Cancer

description: Figure S1A. Comparison of p120 sequences. Residues involved in interaction with E-cadherin are boxed in red. Most of them are conserved. Figure S1B. Comparison of β-catenin sequences. A single β-catenin gene copy was identified in every studied species except for calcareous sponges that exhibit a duplication. All residues essential for E-cadherin interaction are boxed in pink and are highly conserved except for the R386 and N387 residues (replaced by L and T, respectively) in two hexactinellids and a more anecdotal change from A656 to S in placozoans. Residues boxed in blue are involved in α-catenin binding and in orange for the DTDL PDZ binding motif. Figure S1C. Analyses of α-catenins and vinculins sequences. Sequences of α-catenins and vinculins were aligned based on the structural domains helix0 to helix5 in Mus musculus α-catenin and vinculin. Helices are boxed and the numbers at the end of each sequence indicate the range encompassed in the alignment. Secondary structure prediction by JNet (Jalview option) identified six helices in all sponge α-catenin sequences except for A. queenslandica (missing the 4 first helices) and A. vastus (missing helix0). All species analyzed in this study have one copy of α-catenin and one copy of vinculin well-separated in Bayesian tree with high support (pp = 1) (bottom). Figure S2. Structure of Par3 proteins in metazoans. Par3 exhibits a conserved N-terminal domain (CR1), three central PDZ domains, and a C-terminal region containing multiple protein binding sites including the aPKC-binding motif. Figure S5. Domain composition of PatJ (D. melanogaster), INADL and MUPP1 (M. musculus) and Multiple PDZ containing protein (MPDZ) (O. lobularis, S. ciliatum, A. queenslandica and O. minuta). Note that only O. lobularis exhibits an MPDZ with a well-detected L27 domain (Evalue = 8.5 10− 4) as bilaterians. A. queenslandica and S. ciliatum MPDZ have a low-scoring L27 domain (shaded in grey) according to the HMM profile search. There is no recognizable similarity to the L27 domain in the N- terminal region of O. minuta MPDZ. Tables S1. and S2. Information on the domain structures of the Lethal giant larvae (LGL) and Scribble (Src) proteins in various metazoans. Spreadsheet containing Tables S3. and S4. The spreadsheet contains information on the characteristics of the new private databases and public databases (nature = genome/transcriptome) and links for new sequences used in this study. Spreadsheet containing Tables S5. and S6. The spreadsheet contains information on the accession numbers or contig/scaffold references where candidate genes were identified. In bold accession numbers of sequences annotated from our new transcriptomic and genomic sponge datasets. Links for new sequences used in this study are provided. (PDF 2610 kb)