Reflectin
protein family
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. The reflectin protein is responsible for dynamic pigmentation and iridescence in organisms. 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.
Reflectin proteins are likely distributed in the outer layer of cells called "sheath cells" that surround an organism's pigment cells also known as chromatocyte. Specific sequences of reflectin enable cephalopods to communicate and camouflage by adjusting color and reflectivity.
Origin
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. The encoded enzyme detaches transposon from one location in a genome and ligates (binds) it to another. "Jumps" of transposon can create or reverse mutations that alter a cell's genetic identity which can result in new characteristics. This process can be thought of as a "cut and paste" mechanism.
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This entry incorporates text from “Reflectin” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.