InterPro domain: IPR039273

Tepsin associates with the adapter-like complex (AP-4) complex, which forms a non-clathrin coat around cytoplasmic vesicles in plants and animals [ 1 ]. Mutagenesis studies have identified two phylogenetically conserved peptide motifs within the C terminus of tepsin that interact with the C-terminal ear (or appendage) domains of the beta4 and epsilon subunits of AP-4 [ 2 ]. The homologue from Arabidopsis thaliana is known as MTV1 (At3g16270), which mediates clathrin-dependent trafficking of vacuolar cargo from the trans-Golgi network [ 3 ].

1. Multivariate proteomic profiling identifies novel accessory proteins of coated vesicles. J. Cell Biol. 197, 141-60
2. Bivalent Motif-Ear Interactions Mediate the Association of the Accessory Protein Tepsin with the AP-4 Adaptor Complex. J. Biol. Chem. 290, 30736-49
3. MTV1 and MTV4 encode plant-specific ENTH and ARF GAP proteins that mediate clathrin-dependent trafficking of vacuolar cargo from the trans-Golgi network. Plant Cell 25, 2217-35