The exomer complex is a putative vesicle coat required for the direct transport of a subset of cargoes from the trans-Golgi network (TGN) to the plasma membrane. Exomer comprises Chs5p as well as the ChAPs family of proteins (Chs6p, Bud7p, Bch1p and Bch2p), which are thought to act as cargo receptors, and in particular Chs6p is required for the transport of the chitin synthase Chs3p to the bud neck. However, how the ChAPs associate with Chs5p and recognize cargo is not well understood. Using domain-switch chimeras of Chs6p and Bch2p we show that four tetratricopeptide repeats (TPRs) are involved in interaction with Chs5p. Since these roles are conserved between the ChAPs, the TPRs are interchangeable between different ChAP proteins. In contrast, the N-terminal and the central parts of the ChAPs contribute to cargo specificity. While the entire N-terminal domain of Chs6p is required for Chs3p export at all cell cycle stages, the central part seems to predominantly favor Chs3p export in small-budded cells. The cargo Chs3p probably also uses a complex motif for the interaction with Chs6, as the C-terminus of Chs3p interacts with Chs6p and is necessary, but not sufficient, for TGN export.