Amino-acid permease with broad substrate specificity (PubMed:21764911, PubMed:28028545). GAP2 is the only amino-acid permease with very broad substrate specificity, none of the other GAP permeases is able to transport such a variety of amino acids (PubMed:21764911, PubMed:28028545). GAP2 is also able to transport thialysine, and thus probably also lysine (PubMed:21764911). Functions as a sensor via detection of some amino acids including methionine, leading to a rapid activation of trehalase, a downstream target of PKA (PubMed:21764911). Under nitrogen starvation conditions, the permease is no longer in the membrane but seems to be degraded in the vacuole (PubMed:28028545). Expression is under control of the CSY1 amino-acid sensor (PubMed:14871944, PubMed:28028545). Induced during biofilm development (PubMed:22265407). Expression is repressed by nitrogen sources (PubMed:28028545). Expression is repressed by the antifungal agents ketoconazole and flucytosine (PubMed:15917516). Expression is also regulated by NRG1 and TUP1 (PubMed:15814841). Leads to a growth defect on medium containing phenylalanine, valine, leucine, or methionine as sole nitrogen source (PubMed:28028545). Belongs to the amino acid-polyamine-organocation (APC) superfamily. YAT (TC 2.A.3.10) family.