The Dispanin family has several conserved motifs across subfamilies that are also detected in bacteria (Figure 4) . One of the most prominent is the double cysteine motif (C-C) in the first transmembrane helix. This motif has recently been shown to undergo post-translational modification through S-palmitoylation in DSPA2C (IFITM3), which increases hydrophobicity [23] . Further, Yount and colleagues shows that the antiviral activity of DSPA2C (IFITM3) is dependent on this modification, which induces clustering of the proteins. As this motif is highly conserved, it is likely that S-palmitoylation is an important regulatory mechanism also among the other subfamilies. Intriguingly, this motif is also found in the bacterial Dispanins even though bacterial proteins do not undergo S-palmitoylation. Hence, the cysteine motif of the may have other means of structural and functional importance apart of from the S-palmitoylation.