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. SEP7 is required to convert hyphal septin rings into the hyphal-specific state and is necessary for CDC10 turnover during hyphal growth. 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. Induction of hyphal growth brings about important modifications in septin ring dynamics, because the rings were found in a different state from those of yeast cells. This hyphal-specific state contains a core of stable septins (SEP7, CDC3, and CDC12), and it shows a high CDC10 turnover between the ring and the cytoplasm. Interacts with GIN4. Present at the bud neck during cell division. Phosphorylated by GIN4 which stabilizes the GIN4-SEP7 interaction. Leads to a minor reduction in agar invasion ability. Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.