Vesicle tethers are long coiled-coil proteins or multisubunit complexes that provide specificity to the membrane fusion process by linking cargo-containing vesicles to target membranes. Transport protein particle (TRAPP) is a well-characterized multisubunit tethering complex that acts as a GTP exchange factor and is present in two cellular forms: a 7 subunit TRAPP I complex required for ER-to-Golgi transport, and a 10 subunit TRAPP II complex that mediates post-Golgi trafficking. In this work, we have identified Tca17, which is encoded by the non-essential ORFYEL048c, as a novel binding partner of the TRAPP complex. Loss of Tca17 or any of the non-essential TRAPP subunits (Trs33, Trs65 and Trs85) leads to defects in the Golgi-endosomal recycling of Snc1. We show that Tca17, a Sedlin_N family member similar to the TRAPP subunit Trs20, interacts with the TRAPP complex in a Trs33- and Trs65-dependent manner. Mutation ofTCA17orTRS33perturbs the association of Trs65 with the rest of the TRAPP complex and alters the localization of the Rab GTPase Ypt31. These data support a model in which Tca17 acts with Trs33 and Trs65 to promote the assembly and/or stability of the TRAPP complex and regulate its activity in post-Golgi trafficking events.