PPepDB-ID	"Peptide Name"	PMID	"Plant source"	"Plant Family"	"Peptide Family"	"Peptide function"	"Peptide function description"	"Activity against"	Sequence	"Sequence Length"	Validation	"Avg. Molecular wt(Da)"	"Monoisotopic molecular wt(Da)"	pI	Method	"Additional information"
PPepDB_5918	FKB15_VICFA	--NA--	"Vicia faba"	Fabaceae	--NA--	Signaling-peptide	"Direct protein sequencing; Endoplasmic reticulum; Isomerase; Rotamase; Signal; Stress response | FK506-binding protein 2 precursor (EC 5.2.1.8) (Peptidyl-prolyl cis-,trans isomerase) (PPIase) (Rotamase) (15 kDa FKBP) (FKBP-15).Endoplasmic reticulum lumen (Potential)."	--NA--	KRKLKIPAKLGYGEQGSPPTIPGGATLIFDTELVGVNDKSLSEEKSTSSEKVKVHYRGKLTDGTVFDSSFERNSPIDFELGGGQVIKGWDQGLLGMCLGELMKLFSIFLIFTIFIIASALVAAKSAADVTELQIGVKYKPASCEVQAHKGD	151	"Experimental evidence at protein level"	16223.71	16213.51	6.93	--NA--	"FUNCTION:PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.CATALYTIC ACTIVITY:Peptidylproline (omega=180) = peptidylproline (omega=0).ENZYME REGULATION:Inhibited by both FK506 and rapamycin.TISSUE SPECIFICITY:Ubiquitously expressed.INDUCTION:By heat shock.SIMILARITY:Belongs to the FKBP-type PPIase family. FKBP2 subfamily.SIMILARITY:Contains 1 PPIase FKBP-type domain."