This entry represents the GEM and GEM-like (GER 1-8) proteins from plants. They contain a GRAM domain. GEM binds to phospholipids and its expression can be regulated by ABA []. GER5 has been shown to be involved in seed development and inflorescence architecture [].
Proteins in this family are disulphide-rich peptides expressed in Gemmula venom ducts in the gem turrids (venomous snails in the family Turridae) [].There are more than 10,000 species of predatory marine snail that use venom as their primary weapon for prey capture. Based on shell morphology, they are traditionally divided into 3 groups: cone snails, augers and turrids. Most molluscan taxonomies assign cone snails to a single large genus, Conus, while augers are assigned to several different genera; by contrast, the turrids represent a group that is much more diverse, and is now thought to comprise the vast majority of conoidean biodiversity [].The venom peptides from several species in the genus Gemmula, the gem turrids, have been characterised. Their translated open reading frames show characteristics typical of the venom peptides from Conus: an N-terminal signal sequence; a C-terminal cysteine-rich mature peptide; and an intervening pro-region. Two of these sequences, Gsp9.1 and Gsp9.2, have highly similar signal and propeptide regions, while their predicted mature peptides are more divergent (although the cysteine residues are completely conserved) []. This pattern of highly conserved and more variable regions is characteristic of gene superfamilies encoding the toxin peptides found in Conus venoms.
