Manduca sexta serpin-7, a putative regulator of hemolymph prophenoloxidase activation.

ABSTRACT: Serpins regulate various physiological reactions in humans and insects, including certain immune responses, primarily through inhibition of serine proteases. Six serpins have previously been identified and characterized in the tobacco hornworm Manduca sexta. In this study, we obtained a full-length cDNA sequence of another Manduca serpin, named serpin-7. The open reading frame of serpin-7 encodes a polypeptide of 400 amino acid residues with a predicted signal peptide of the first 15 residues. Multiple protein sequence alignment of the reactive center loop region of the M. sexta serpins indicated that serpin-7 contains Arg-Ile at the position of the predicted scissile bond cleaved by protease in the serpin inhibition mechanism. The same residues occur in the scissile bond of the reactive c

SUBMITTER: Suwanchaichinda C 

PROVIDER: S-EPMC3760416 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature