HMW glutenin (IPR001419)

Short name: Glutenin

Overlapping homologous superfamilies


Family relationships



Gluten is the protein component of wheat flour. It consists of numerous proteins, which are of two different types responsible for different physical properties of dough: the glutenins, which are primarily responsible for the elasticity, and the gliadins, which contribute to the extensibility.

The glutenins are of two different types, termed low (LMW) and high molecular weight (HMW) subunits [PMID: 3840588]. The glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterised by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm [PMID: 11084370].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0045735 nutrient reservoir activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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