Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Like erythrocyte spectrin, the spectrin-like proteins are capable of forming dimers which can further associate to tetramers. Interacts (via C-terminal spectrin repeats) with TRPC4. Interacts with CALM and EMD. Interacts with isoform 1 of ACP1. Identified in a complex with ACTN4, CASK, IQGAP1, MAGI2, NPHS1 and SPTBN1. Interacts with SHANK3 (via ANK repeats). Interacts with CLN3; this interaction regulates the fodrin localization at the plasma membrane (Probable). Expressed along the cell membrane in podocytes and presumptive tubule cells during glomerulogenesis and is expressed along lateral cell margins in tubule cells. Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by calpain in vitro. The disease is caused by variants affecting the gene represented in this entry. Belongs to the spectrin family. Extended N-terminus.