Immunolocalization shows prestin is expressed in the lateral plasma membrane of the outer hair cells, the region where electromotility occurs.

[9] The prestin protein shows several parallel amino acid replacements in bats, whales, and dolphins that have independently evolved ultrasonic hearing and echolocation, and these represent rare cases of convergent evolution at the sequence level.

[12] Prestin is a transmembrane protein that mechanically contracts and elongates leading to electromotility of outer hair cells (OHC).

[16] A recent study supports the IVS model showing that mutations of 12 residues that span the intracellular side of prestin's core membrane resulted in significant decrease in NLC.

[14] Although previously thought to be absent, anion transport has also been shown to be an important aspect of prestin's ability to drive electromotility of hair cells.

[14][15] This mechanism is independent of prestin's voltage-sensing capabilities based upon mutagenesis experiments showing that different mutations lead to effects in either anion-uptake or NLC, but not both.

[14] It is suggested that prestin contains an intrinsic anion-uptake mechanism based upon research showing concentration dependent [14C]formate uptake in Chinese hamster ovary (CHO) cells.

[14][17] Prestin was discovered by Peter Dallos's group in 2000 and named from the musical notation presto because of the speed of the protein.