Conserved Site

Thaumatin, conserved site (IPR017949)

Short name: Thaumatin_CS

Description

Thaumatin [PMID: 7049841] is an intensely sweet-tasting protein, 100,000 times sweeter than sucrose on a molar basis [PMID: 7049841] 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 [PMID: 7049841]. Several stress-induced proteins of plants have been found to be related to thaumatins:

  • A maize alpha-amylase/trypsin inhibitor
  • Two tobacco pathogenesis-related proteins: PR-R major and minor forms,which are induced after infection with viruses
  • Salt-induced protein NP24 from tomato
  • Osmotin, a salt-induced protein from tobacco [PMID: 16666857]
  • Osmotin-like proteins OSML13, OSML15 and OSML81 from potato [PMID: 7630973]
  • P21, a leaf protein from soybean
  • PWIR2, a leaf protein from wheat [PMID: 1650615]
  • Zeamatin, a maize antifungal protein [PMID: 7846159]

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 [PMID: 1463856]. The proteins are involved in systematically acquired resistance and stress responses in plants, although their precise role is unknown [PMID: 1463856].

This entry represents a conserved site that includes three cysteine residues known to be involved in disulphide bonds.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns