I am not sure if the signal sequence of your plant peptide would serve the purpose while expressing in yeast. However, for heterologous expression in yeast, the available vectors would have a signal sequence for efficient expression.
I’m afraid that your question relates to a matter that is a bit more complicated than ‘just’ the choice of the signal sequence. See for an excellent review:
Cereghino, J. L., & Cregg, J. M. (2000). Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS microbiology reviews, 24(1), 45-66.
However coming back to your question. It is clear that several different secretion signal sequences have been used successfully although success rates varied. The S. cerevisiaeα-factor prepro peptide has been used with the most success.
One of the reasons why the native (plant) sequence most likely will not work is because of the differences between signal sequences in different species. We know this thanks to the ground-breaking work of Gunnar von Heijne and his co-workers. See for example:
Emanuelsson, O., Nielsen, H., Brunak, S., & Von Heijne, G. (2000). Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. Journal of molecular biology, 300(4), 1005-1016.