Reflectins are a family of intrinsically disordered proteins evolved by a certain number of cephalopods including Euprymna scolopes and Doryteuthis opalescens to produce iridescent camouflage and signaling.
The recently identified protein family is enriched in aromatic and sulfur-containing amino acids, and is utilized by certain cephalopods to refract incident light in their environment.
This process is "dynamic" due to its reversible properties, allowing reflectin to change an organism's appearance in response to external factors such as needing to camouflage or send warning signals.
[3] Reflectin is presumed to have originated from a type of transposon (nicknamed jumping genes), which is a DNA sequence that can change positions within genetic material by encoding an enzyme.
Transposons' ability to adapt in a genome and quickly shift its identity is a property that closely resemble the behavior of reflectin.
This change additionally allows initially transparent cells to increase in brightness [8] Reflectin is able to receive information from signals for a continuous process to fine-tune the osmotic pressure of sub-cellular structures of cephlapods.