Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinase GIN4. Septins are also involved in cell morphogenesis, chlamydospores morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization, and spore wall formation. CDC11 is required for the correct localization of SEC3 at bud tips and bud necks. Plays a key role in invasive growth and virulence. Component of the septin complex which consists of CDC3, CDC10, CDC11, CDC12 and probably SEP7. The purified septin complex appeared to have a stoichiometry of 2 CDC3, 1 to 2 CDC10, 1 CDC11, 2 CDC12, and 1 or none SEP7 subunit. Interacts with HSL1. Localizes to a tight ring at the bud and pseudohyphae necks and as a more diffuse array in emerging germ tubes of hyphae. Hyphal induction causes immediate phosphorylation at Ser-395 by GIN4 and at Ser-394 by CDC28-CCN1. GIN4 phosphorylation at Ser-395 primes CDC11 for further phosphorylation by CDC28-CCN1. CDC28-HGC1 then maintains CDC11 phosphorylation throughout hyphal growth. Ser-4 is also phosphorylated in yeast cells but not hyphal cells. Met-1 is acetylated. Causes greater curvature of cells growing in a filamentous manner and morphological defects in suspensor cells and chlamydospores. Leads to reduced tissue penetration and non-invasive fungal masses in mice infected kidneys. Leads also to hypersusceptibility to caspofungin. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.