The (Pro)renin receptor (PRR) has been identified as a cell surface protein capable of binding and non-proteolytically activating prorenin. Surprisingly, PRR is associated with H⁺-ATPases and alternative functions in H⁺-ATPase regulation as well as in Wnt signalling have been suggested. The kidneys express very high levels of H⁺-ATPase which are involved in multiple functions such as endocytosis, membrane protein recycling as well as urinary acidification and salt absorption. Here we investigated the expression pattern of PRR in kidney and its possible effect on H⁺-ATPase function. qPCR and immunohistochemistry demonstrated expression of the PRR along the entire mouse and rat nephron with highest levels in the collecting system colocalizing with H⁺-ATPases. Further experiments demonstrated expression of PRR in all types of intercalated cells.. Next, wild-type mice were treated with either NH₄Cl, NaHCO₃, KHCO₃, NaCl, or DOCA for 7 days. NaHCO₃ treatment resulted in an increase of mRNA and protein abundance of PRR and the B1 H⁺-ATPase subunit in both cortex and medulla, respectively, whereas NH₄Cl diet reduced PRR and B1 expression only in cortex. Lastly, microperfusion experiments of isolated cortical collecting ducts and exposure to 1 nM prorenin did not stimulate H⁺-ATPase activity. Our results suggest that the PRR may form a complex with H⁺-ATPases in renal intercalated cells but prorenin appears to have no direct or acute effect on H⁺-ATPase activity.