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- W2890899507 abstract "Members of the serpin superfamily of proteins occur in animals, plants, bacteria, archaea and some viruses. They adopt a variety of physiological functions, including regulation of immune system, modulation of apoptosis, hormone transport and acting as storage proteins. Most members of the serpin family are inhibitors of serine proteinases. In this study, we searched the genome of Manduca sexta and identified 32 serpin genes. We analyzed the structure of these genes and the sequences of their encoded proteins. Three M. sexta genes (serpin-1, serpin-15, and serpin-28) have mutually exclusive alternatively spliced exons encoding the carboxyl-terminal reactive center loop of the protein, which is the site of interaction with target proteases. We discovered that MsSerpin-1 has 14 splicing isoforms, including two undiscovered in previous studies. Twenty-eight of the 32 M. sexta serpins include a putative secretion signal peptide and are predicted to be extracellular proteins. Phylogenetic analysis of serpins in M. sexta and Bombyx mori indicates that 17 are orthologous pairs, perhaps carrying out essential physiological functions. Analysis of the reactive center loop and hinge regions of the protein sequences indicates that 16 of the serpin genes encode proteins that may lack proteinase inhibitor activity. Our annotation and analysis of these serpin genes and their transcript profiles should lead to future advances in experimental study of their functions in insect biochemistry." @default.
- W2890899507 created "2018-09-27" @default.
- W2890899507 creator A5004764136 @default.
- W2890899507 creator A5016059940 @default.
- W2890899507 creator A5028420844 @default.
- W2890899507 creator A5051412865 @default.
- W2890899507 creator A5068243804 @default.
- W2890899507 creator A5077986501 @default.
- W2890899507 creator A5081348758 @default.
- W2890899507 date "2018-11-01" @default.
- W2890899507 modified "2023-10-14" @default.
- W2890899507 title "The Manduca sexta serpinome: Analysis of serpin genes and proteins in the tobacco hornworm" @default.
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- W2890899507 doi "https://doi.org/10.1016/j.ibmb.2018.09.008" @default.
- W2890899507 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6249112" @default.