Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the biofilm formation and pathogenesis of C.albicans infections. Necessary for C.albicans to bind to N-cadherin on endothelial cells and E-cadherin on oral epithelial cells and subsequent endocytosis by these cells. During disseminated infection, mediates initial trafficking to the brain and renal cortex and contributes to fungal persistence in the kidneys. Covers the surface of the germ tube. Expression is under the positive control of the biofilm regulator BCR1, RLM1, TOR1 and TPK2; and under the negative control of SFL1. Induced during germ tube formation. Highly expressed in oropharyngeal candidiasis (OPC), a biofilm-like infection of the oral mucosa. Induced in the initial stages of biofilm formation. Down-regulated by human serum, as well as by bacterial quorum sensing quencher thiazolidinedione-8, pterostilbene, lipopeptides biosurfactant produced by B.amyloliquefaciens, and Riccardin D, a macrocyclic bisbibenzyl isolated from Chinese liverwort D.hirsute, which has an inhibitory effect on biofilms and virulence. 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. 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. Reduces adhesion and damage to both human umbilical vein endothelial cells (HUVEC) and oral epithelial cells. Belongs to the ALS family.