The described sequences will account for most of the avenin and globulin seed proteins in oat cultivar CDC Dancer, and will provide the most of the functional properties of the seed related to protein content. The globulin high-glutamine region is similar to the avenin variable regions in having, at least within the same globulin, repeats of discernible simple motifs. Although this feature is not as pronounced as in prolamins, it indicates such repeats can evolve separately in different seed protein classes in addition to the prolamins – which are members of the AAI_LTSS protein superfamily that is unique to higher plants and includes members related to a number of pathologies including celiac disease and allergies. The development of such repeat regions may thus be related more to biological roles and the development and tissue site of synthesis rather than evolutionary history. This separate history is also indicated since the globulins lack the conserved cysteine core characteristic of the AAI_LTSS superfamily. The CDC AMN107 Dancer globulins all share five conserved cysteines distributed over the amino acid sequence. In addition, many globulins have a sixth cysteine at position 173 and Glo-9 has a seventh cysteine at position 423. The pattern of intraand intermolecular disulfide bonds is not known, but the frequency of globulins with an odd number of cysteines raises the question of whether at least some of the globulins can aggregate through disulfide bonds. It was noted that two of the CDC Dancer globulins have slightly truncated C-termini due to premature stop codons, resulting in polypeptides that would be 9 and 17 amino acids shorter than assumed to have existed prior to DNA mutations that introduced premature stop codons. Such 39 mutations in other cereal seed protein coding sequences have recently been reported for a barley B-hordein and a wheat c-gliadin. In those two cases the mutations involved frame shifts that created new stop codons and slightly shorter or longer polypeptides, respectively. Defective mRNAs tend to be removed via a nonsense-mediated-decay mechanism that prevents aberrant protein synthesis. Avenins, as a group, are known to be present as both monomers and in disulfide-linked aggregates. Assuming that CDC Dancer Avenins 1–7 have all eight cysteines occupied by four intramolecular disulfide bonds characteristic of many members of the AAI_LTSS superfamily of proteins that form four intramolecular bonds presumably to stabilize the core structure, those seven avenins would exist as monomers in the oat seed. On the other hand, Avenins 8–9 have the ninth cysteine in the final Cterminal position available for external bonds and are likely the aggregating members of the avenin complement – at least for cv CDC Dancer. However, the aggregation would be limited to dimers if the conserved eight cysteines are completely occupied by intramolecular bonds. Larger aggregates would require either some avenins to not completely form the four conserved bonds or the previously reported pattern of bonds is incorrect.