| Type: | Conserved_site | Name: | Thaumatin, conserved site |
| Description: | Thaumatin [] is an intensely sweet-tasting protein, 100,000 times sweeter than sucrose on a molar basis [] found in berries from Thaumatococcus daniellii, a tropical flowering plant known as Katemfe, it is induced by attack by viroids, which are single-stranded unencapsulated RNA molecules that do not code for protein.Thaumatin consists of about 200 residues and contains 8 disulphide bonds. Like other PR proteins, thaumatin is predicted to have a mainly beta structure, with a high content of beta-turns and little helix []. Several stress-induced proteins of plants have been found to be related to thaumatins: A maize alpha-amylase/trypsin inhibitorTwo tobacco pathogenesis-related proteins: PR-R major and minor forms,which are induced after infection with viruses Salt-induced protein NP24 from tomatoOsmotin, a salt-induced protein from tobacco []Osmotin-like proteins OSML13, OSML15 and OSML81 from potato []P21, a leaf protein from soybeanPWIR2, a leaf protein from wheat []Zeamatin, a maize antifungal protein []This protein is also referred to as pathogenesis-related group 5 (PR5), as many thaumatin-like proteins accumulate in plants in response to infection by a pathogen and possess antifungal activity []. The proteins are involved in systematically acquired resistance and stress responses in plants, although their precise role is unknown [].This entry represents a conserved site that includes three cysteine residues known to be involved in disulphide bonds. | Short Name: | Thaumatin_CS |
