2.A.49.3.1
NO₃^-:H⁺ (or less efficiently, Cl^-:H⁺) antiporter, ClC-A or CLCa (De Angeli et al., 2006; Bergsdorf et al., 2009). Responsible for nitrate uptake into vacuoles (Zifarelli and Pusch, 2009b).  It is up-regulated under salt stress conditions (Yang et al. 2018) and may play a role in nitrate and Cd²⁺ resistance (Liao et al. 2019). The cryoEM structure has been solved at 2.8 Å resolution. An almost identical sequence has Uniprot acc # P92941 and differs from the one included in TCDB between residues 380 and 430, possibly due to sequencing errors. The central nitrate is shifted by approximately 1.4 Å from chloride, which is likely caused by a weaker interaction between the anion and Pro160; the side chains of aromatic residues around the central binding site are rearranged to accommodate the larger nitrate (Yang et al. 2018) and may play a role in nitrate and Cd²⁺ resistance (Liao et al. 2019). The cryoEM structure has been solved at 2.8 Å resolution. An almost identical sequence has Uniprot acc # P92941 and differs from the one included in TCDB between residues 380 and 430, possibly due to sequencing errors. The central nitrate is shifted by approximately 1.4 Å from chloride, which is likely caused by a weaker interaction between the anion and Pro160; the side chains of aromatic residues around the central binding site are rearranged to accommodate the larger nitrate (He et al. 2022).