Conclusion for haloacid dehalogenase-like hydrolase domain containing 2

Structure

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Function

The protein is named after its function of molecular hydrolase activity. It involves acting as catalysis to breakdown various bonds such as Carbon-Oxygen, Carbon-Nitrogen, Carbon-Carbon and phosphoric anhydride bonds. The latter part “domain containing 2” in the name refers to it having 2 domains in expressing the protein allocated mainly in the immune system but also in the brain. The name of the protein is directly related to the function. There’s evidence this protein not only exist in human speciestherefore it is possible to study other species to examine it's function in future research. From the basis structure of Haloacid dehalogenase superfamily, we understand the importance of hydrolases contains enzymes, phosphate ion and metal ion in the functional process. But unfortunately, there is still low level academic research proving its function in different part of body system.

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Evolution

The mouse version of the gene is the closest to the ancestrial gene as indicated by the BLAST search and subsequent phylogenetic tree. There are 4 versions of the gene found in mice, one is well studied and seems to be the closest to the ancestor gene, one is an isoform and 2 are yet unnamed and thus unstudied. However, the closeness of the match suggests that it is of similar function. The human version is most closely resembling the chimpanzee and orangutan versions which is expected as those are the 2 animals most closely resembling the human genome overall.

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Overall

True to its name this protein is a haloacid dehalogenase-like hydrolase with similar properties. The main function is as a catalyst although the specific function is still not well studied. It is known that it is a conserved gene and the brief examination showed that the mouse versions of this gene are the closest to the ancestral gene.