Non-HFE haemochromatosis

Figure 1 Structure of human hemojuvelin and positions of mutations. A: The exon structure of human hemojuvelin is shown with positions of known mutations marked[6,13-24,30,39]. *Q6H was found associated with C321X; B: Predicted structure of the full length HJV protein, showing the positions of structural domains and motifs. SP, signal peptide; PG, poly-glycine sequence; RGD, RGD motif; PP, poly-proline sequence; vWF, partial von Willebrand factor type D domain; N, potential N-linked glycosylation sites; GPI, GPI-attachment site; TM, transmembrane domain, cleaved after GPI attachment.

Figure 2 Structure of human hepcidin and positions of mutations. A: The exon structure of human hepcidin is shown with positions of known mutations marked[5,29-37]. B: Predicted structure of the hepcidin peptide. SP, signal peptide; Pro, pro-region; Mature, 25 amino acid mature hepcidin peptide.

Figure 3 Structure of human transferrin receptor 2 (TfR2) and positions of mutations. A: The exon structure of human TfR2 is shown with positions of known mutations marked[7,30,40-52]. The frameshift mutations R30fsX60 and P555fsX561 are also known as E60X and V561X respectively. G792R may be associated with R396X; B: Predicted structure of TfR2 protein. YQRV, endocytosis signal; TM, transmembrane domain; RGD, RGD motif; S, predicted interchain disulphide bonds; N, potential N-linked glycosylation sites.

Figure 4 Structure of human ferroportin and positions of mutations. A: The exon structure of human ferroportin is shown with positions of known mutations marked[8,9,60-85]. IRE, iron response element; B: Predicted structure of ferroportin protein. Predicted transmembrane domains are shaded; N, potential N-linked glycosylation sites.