Sulfur-rich seed storage protein that remains undegraded at germination. Two-subunit monomeric unit made of alpha and beta subunits coupled by disulfide bonds (at pH 4.5 and under non-reducing conditions) (PubMed:29635768, PubMed:25664733, PubMed:22264085). Can also form oligomers including dimer, tetramer and cyclic hexamer (trimer of dimers) (at pH > 5.5) (PubMed:22264085, PubMed:25664733). Component of globulins complexes which accumulate in seeds (PubMed:22264085). Interacts with flavonoids (e.g. apigenin glucosides) present in globulins complexes (PubMed:22264085, PubMed:24054261). Forms a static complex with vitexin (PubMed:24054261). Expressed in developing cotyledons and in the embryonic axis of germinating seeds (PubMed:9247543). Accumulates in seeds, especially in the protein bodies of developing cotyledonary cells (at protein level) (Ref.2, PubMed:28863333). Also detected, at low levels, in plumules and radicles (PubMed:9247543). Accumulates during seed development (PubMed:21457583, PubMed:9247543). In seeds, localized to the embryo tissues and to a layer of cells adjacent to the seed coat (PubMed:9247543). By sulfur deficiency. Undergoes very complex post-translational maturation; the proteolytic processing leading to the formation of two alpha and beta subunits is incomplete, leaving a certain amount of the protein in an uncut form. Glycosylated on alpha chain. Causes an allergic reaction in human. May be used in antidiabetic therapies and diets for type 2 diabetes (T2D). Capable of reducing glycaemia in mammals. Resistant to pancreatin-mediated digestion. Belongs to the peptidase A1 family. Truncated N-terminus.