Thypedin, the multi copy precursor for the hydra peptide pedin, is a beta-thymosin repeat-like domain containing protein.

Pedin, a peptide of 13 amino acids, stimulates foot formation in hydra, one of the simplest metazoan animals. Here, we show that the corresponding transcripts are 3.8 kb in size encoding a precursor protein with a size of about 110 kDa, which contains 13 copies of the peptide. Interestingly, the deduced amino acid sequence of the precursor comprises 27 copies of a beta-thymosin-like repeat domain. Hence, we named the precursor protein thypedin. Pedin transcripts are present along the body axis of the animal with slightly higher abundance in the foot to bud region and in the head. Pedin is expressed mainly in epithelial cells of the ectoderm and endoderm. During budding it is present in the evaginating bud. The early appearance of transcripts during phases of cell-fate specification like budding indicates that pedin may be involved in differentiation processes in hydra. This is confirmed by the fact that pedin stimulates bud outgrowth. Thymosin-repeat containing proteins are well known for their regulatory influence on actin polymerisation. Here we show the first indirect evidence that thypedin may be able to interact with actin as well. Since actin polymerisation and depolymerisation processes are known to take place during morphogenetic processes, these findings may hint at new aspects of the function of pedin and its precursor in pattern formation in hydra.