Fig. 1From: Analysis of splice variants of the human protein disulfide isomerase (P4HB) geneP4HB gene and protein organization. (A). Gene structure of human P4HB gene and predicted splice variants. Exons are represented by boxes; 5′ or 3′ untranslated regions (UTR) are also depicted. ATG indicates the start codon and STOP depicts the stop codon. The underline in P4HB-23 indicates the translated regions. The coding sequence of P4HB-027 includes the 3′ UTR, which does not contain a stop codon. (B). PDIA1 protein domain organization and predicted structure of alternatively processed isoforms. PDIA1 protein is composed of five domains: a, b, b’, a’ and c. The a and a catalytic domains contain the thioredoxin redox-active CGHC motifs (white boxes), while the b and b’ domains (gray boxes) are noncatalytic, structured as thioredoxin folds enriched in hydrophobic residues involved in substrate binding and chaperone activity. An unstructured x-linker stretch is located between b’ and a’ domains and confers flexibility to PDI. The C-terminal c- domain contains the KDEL sequence, an ER retrieval signalBack to article page