Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation (PubMed:9393828). Plays an important role in the pathogenesis of C.albicans infections. Forms amyloid structures, essential for cell-cell association and cell-substrate adhesion to polystyrene (By similarity). Forms homodimers through the tandem repeats. Aggregates in amyloid-like structures, with self-propagating secondary-structure changes, amyloid-characteristic dye binding, and induced birefringence. Identified as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. Each ALS protein has a similar three-domain structure, including a N-ter domain of 433-436 amino acids that is 55-90 percent identical across the family and which mediates adherence to various materials; a central domain of variable numbers of tandemly repeated copies of a 36 amino acid motif; and a C-ter domain that is relatively variable in length and sequence across the family. N-glycosylated and O-glycosylated. 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. Belongs to the ALS family.