Fig. 1.

Location of pathogenic rare tenascin XB (TNXB) sequence variants within the TNXB protein domains. Five heterozygous TNXB missense variations were identified in the 49 children with vesicoureteric reflux who underwent sequencing and their corresponding amino acid changes and locations within the protein are shown. Most of the variants affect the fibronectin type III (FNIII) modules that are implicated in binding to decorin and in mediating extensibility of the TNX protein, which imparts elasticity to the tissue. One amino acid variant, R4173Q, affects the fibrinogen-like (FBG) domain, which directly binds to collagen fibrils and promotes the formation of collagen fibrils. The symbol under exon 2 depicts the N-terminal oligomerization domain. The diamonds depict the epidermal growth factor (EGF)-like repeats. The rectangular boxes depict the FNIII repeats, and the oval depicts the fibrinogen (FBG).