Proline is the most abundant amino acid in wine and beer, because the yeast Saccharomyces cerevisiae hardly assimilates proline during fermentation processes. Our previous studies showed that arginine induces endocytosis of the proline transporter Put4, resulting in inhibition of proline utilization. We here report a possible role of arginine sensing in the inhibition of proline utilization. We first found that two basic amino acids, ornithine, and lysine, inhibit proline utilization by inducing Put4 endocytosis in a manner similar to arginine, but citrulline does not. Our genetic screening revealed that the arginine transporter Can1 is involved in the inhibition of proline utilization by arginine. Intriguingly, the arginine uptake activity of Can1 was not required for the arginine‐dependent inhibition of proline utilization, suggesting that Can1 has a function beyond its commonly known function of transporting arginine. More importantly, our biochemical analyses revealed that Can1 activates signaling cascades of protein kinase A in response to extracellular arginine. Hence, we proposed that Can1 regulates proline utilization by functioning as a transceptor possessing the activity of both a transporter and receptor of arginine. Proline is mainly transported to the cells by the proline‐specific transporter Put4. In the presence of basic amino acids, Put4 is endocytosed dependent on the ubiquitin ligase Rsp5 and its adaptor Art3, leading to the inhibition of proline utilization. The transceptor function of Can1 plays a role in the mechanism for sensing basic amino acids that regulate the inhibition of proline utilization. Take‐away Basic amino acids inhibit proline utilization by inducing Put4 endocytosis. Can1 is involved in the inhibition of proline utilization in yeast. Can1 is a transceptor acting as both a transporter and receptor of arginine.