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Proposed prestin topologies. A and B, 10- and 12-pass models of prestin secondary structure have been proposed based on data suggesting phosphorylation sites (11) and conflicting reports of N-linked glycosylation (13, 14). Residue numbers for cysteine locations are shown, and all but 52, 395, and 679 are unique to prestin in comparison with PAT1 (SLC26A6).
