SLC15A2 encodes a proton-coupled peptide transporter that mediates cellular uptake of di- and tripeptides, with particular affinity for dipeptides. In the kidney, it is involved in reabsorption of circulating peptides from the glomerular filtrate. Beyond peptide transport, SLC15A2 has broad pharmacological relevance: it transports beta-lactam antibiotics such as cefadroxil and amoxicillin 1, as well as carnosine and other peptidomimetic drugs including antivirals and anticancer agents. The transporter also mediates innate immune responses by facilitating bacterial peptidoglycan transport, enabling detection of pathogens like muramyl dipeptide by NOD-like receptors. Recent evidence demonstrates SLC15A2's role in radiation protection: exercise-generated carnosine is transported via SLC15A2 to hematopoietic stem cells, where it inhibits p53-mediated injury and senescence 2. Clinically, SLC15A2 variants associate with warfarin maintenance dose variability in Han-Chinese populations 3, and reduced expression correlates with early biochemical recurrence and poor survival in prostate cancer 4. Notably, cefadroxil competitively targeting SLC15A2 can protect kidney function from colistin nephrotoxicity 5, suggesting therapeutic potential for modulating drug transport. These findings position SLC15A2 as both a biomarker for disease risk stratification and a target for pharmacological intervention across multiple clinical contexts.