Skip to main content
. 2019 Mar 6;20:175. doi: 10.1186/s12864-019-5514-7

Fig. 3.

Fig. 3

Complete or partial acid sequences of four LWamide preprohormones from T. cystophora, A. alata, C. xaymacana, and C. fleckeri. Residues and peptide sequences are highlighted as in Fig. 1. These preprohormones can be processed into a number of peptides with either the LWamide or MWamide C-terminus, while the N-termini of some of these peptides are somewhat uncertain (Table 1). Interestingly, the second neuropeptide sequence (counted from the N-terminus), pQPGMWamide, is completely identical in all four cubomedusan preprohormones. These sequences are preceded by L residues, which again would imply processing C-terminally from L [21, 29]. Similarly, the third peptide sequence (counted from the N-terminus) from each preprohormone constitute a peptide subfamily of nearly identical sequences. Table 2 gives our proposal for their structures, although there are uncertainties about their N-termini. The proposed peptide subfamilies have discrete structures, which enable us to identify the first peptide sequences in the C. xaymacana and C. fleckeri preprohormone fragments as peptides-2 (belonging to peptide family-2) followed by peptides-3 and -4