The 𝛾-prolamins are important components of seed storage proteins in wheat and other Triticeae species. Here, the 𝛾-prolamin genes from the diploid Triticeae species were systemically characterized. Most of the 𝛾-prolamins (except 75 K 𝛾-secalins) characterized were defined as 𝛾-gliadin-like 𝛾-prolamins, since they shared same characteristic model structure with 𝛾-gliadins. Over one-third of these putatively functional 𝛾-prolamin peptides contained different number of cysteine residues as compared to the eight residues present in 𝛾-gliadins. Sequence polymorphism and linkage disequilibrium analyses showed the conservation of 𝛾-prolamin genes in Triticeae species under evolutionary selection. Phylogenetic analyses indicated that these 𝛾-prolamin genes can not be clearly separated according to their genomic origins, reflecting the conservation of 𝛾-gliadin-like 𝛾-prolamin genes after the divergence of Triticeae species. A screening of coeliac disease (CD) toxic epitopes shows that the 𝛾-prolamins from some other genomes contain much fewer epitopes than those from the A, S (B) and D genomes of wheat. These findings contribute to better understanding of 𝛾-prolamin family in Triticeae and build a ground for breeding less CD-toxic wheat cultivars.