Globins are small, globular, heme-containing proteins, ubiquitously found within all kingdoms of life​. The oxygen carrying function of hemoglobin and myoglobin is very well characterized, but over the last decades, it became clear that oxygen binding is only a derived, specialized function of some globins.  Members of this broad family have been found to be involved in a variety of other functions, such as NO production and scavenging, reactive oxygen species (ROS) detoxification, sulfide transport, peroxidation, and oxygen sensing​. Yet, the function of many globins remain enigmatic and not understood. 

The model organism Caenorhabditis elegans expresses an unusually large number of 34 globin (glb) genes, of which twelve have one or more predicted isoforms, resulting in 55 different globin proteins in this 1-millimeter nematode​. In silico research has revealed a striking variation in sequence, length, intron position, and size of the predicted N- and C-terminal extensions in the C. elegans glb genes​​. This enormous diversity may be the result of multiple gene duplication events, followed by subfunctionalization​​. The largely neglected globin gene family in the otherwise genetically well-characterized and malleable C. elegans model holds great potential to unravel globin functionality. 

Based on earlier experimental data and/or algorithmic predictions we will focus on the functional characterization of a few C. elegans globins: glb-1, the smallest and most ubiquitous globin for its role in stress resistance; the two isoforms of glb-3, for their putative roles in neuronal function and reproduction; and glb-4, for its role in locomotion and reproduction.  In case new phenotypic data becomes available, our attention may also focus on other members of this family.