D-mannose-binding lectin that also binds alpha-methyl-D-mannoside with even higher affinity (PubMed:24008245). Has hemagglutinating activity against rabbit erythrocytes (PubMed:24008245). Shows toxicity against the brine shrimp A.nauplii (PubMed:24008245). Induces reversible paw edema and hypernociceptivity in rats (PubMed:28196677). Optimum pH for hemagglutinating activity is 8. Activity drops with more acidic and basic pH and is lost at pH 5 and pH 8, respectively. Hemagglutinating activity is stable after incubation at 70 degrees Celsius for 1 hour but lost at higher temperatures. The mature chain consists of residues 163-280 followed by residues 29-147. 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. The mature chain consists of residues 163-280 followed by residues 29-146. The measured range is 1-237. LD(50) is 45.85 ug/ml against the brine shrimp A.nauplii. 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.