Cell wall protein which plays an anti-adhesive role and promotes dispersal of yeast forms, which allows the organism to seek new sites for colonization. In yeast cultures, is linked covalently to glucans of the wall matrix, but, as cultures approach stationary phase, accumulates in the medium and is extractable from cells with disulfide-reducing agents. Removed from the cell wall by proteolytic cleavage by SAP9 and SAP10. Expression is greatest during yeast exponential-phase growth, but down-regulated in stationary phase and upon filamentation. Expression is also increased during growth in hypoxic conditions. Expression decreases in biofilm cultures and becomes undetectable through late stage biofilm formation. Up-regulated when the extracellular phosphate concentration is low or in presence of Cis-2-dodecenoic acid (BDSF). Repressed during cell wall regeneration. Expression is positively regulated by EFG1 and EFH1, and negatively regulated by SSN6 and SSK1. The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer. Cleaved by SAP9 and SAP10, which leads to its release from the cell wall. N-glycosylated. Leads to increased adhesion and biofilm formation. Belongs to the flocculin family.