D-mannose/D-glucose-binding lectin which binds alpha-methyl-D-mannoside, D-mannose and D-glucose in that order (PubMed:24519628, PubMed:27737777). Also binds to serum fetuin and ovalbumin (PubMed:24519628). Has hemagglutinating activity towards rabbit erythrocytes (PubMed:24519628). Is not toxic towards larvae of the brine shrimp Artemia (PubMed:24519628). Induces relaxation in rat endothelized aorta (PubMed:24519628). Shows a transient edematogenic effect in rat (PubMed:27737777). Optimum pH is 7-9 with activity decreasing quickly at higher or lower pH. Hemagglutinating activity stable up to incubation at 80 degrees Celsius for 1 hour but diminishes with higher temperatures and is absent at 100 degrees Celsius. Homotetramer. Concanavalin A-like lectins of the Diocleinae subtribe undergo proteolytic processing referred to as circular permutation. The propeptide is split into an N-terminal and a C-terminal part, the gamma and beta chain, respectively. These are then religated in beta-gamma order to form the mature alpha chain. The beta and gamma chains can often be detected in cell extracts (By similarity). Residues 1-118 of the mature chain, as displayed here, probably constitute the beta chain in the propeptide, residues 119-237 the gamma chain (Probable). Alpha chain. Binds one manganese (or another transition metal) ion and one calcium ion. The metal ions are essential for the saccharide-binding and cell-agglutinating activities. Belongs to the leguminous lectin family.