Journal ArticleOpen Access
<i>In silico</i> analysis of selenoprotein N (<i>Gallus gallus</i>): absence of EF-hand motif and the role of CUGS-helix domain in antioxidant protection
Authors
Author Affiliations
Northeast Agricultural University, Heilongjiang University of Chinese Medicine, Patuakhali Science and Technology University
Published InMetallomics
Year2021
Citations28
Abstract
Selenoprotein N (SEPN1) is critical to the normal muscular physiology. Mutation of SEPN1 can raise congenital muscular disorder in human. It is also central to maturation and structure of skeletal muscle in chicken. However, human SEPN1 contained an EF-hand motif, which was not found in chicken. And the biochemical and molecular characterization of chicken SEPN1 remains unclear. Hence, protein domains, transcription factors, and interactions of Ca2+ in SEPN1 were analyzed in silico to provide the divergence and homology between chicken and human in this work. The results showed that vertebrates' SEPN1 evolved from a common ancestor. Human and chicken's SEPN1 shared a conserved CUGS-helix domain with function in antioxidant protection. SEPN1 might be a downstream target of JNK pathway, and…
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