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_5735	PAPA4_CARPA	--NA--	"Carica papaya"	Caricaceae	--NA--	Signaling-peptide	"3D-structure; Direct protein sequencing; Hydrolase; Protease; Signal; Thiol protease; Zymogen | Papaya proteinase 4 precursor (EC 3.4.22.25) (Papaya proteinase IV),(PPIV) (Papaya peptidase B) (Glycyl endopeptidase)."	--NA--	GSLLNAIAHQPVSVVVESAGRDFQNYKGGIFEGSCGTKVDHAVTAVGYGKMAIICSFSKLLFVAICLFGHMSLSYCDFSIVGYSQDDLTSTERLIQLFNSNDEFKEKYVGSLPEDYTNQPYDEEFVNEDIVDLPESVDWRAKGAVTPVKHQGYCESCWAFSTVATVEGINKIKTGNLVELSEQELVDCDKQSYGCNRGYQSGGKGYILIKNSWGPGWGENGYIRIRRASGNSPGVCGVYRSSYYPIKNSTSLQYVAQNGIHLRAKYPYIAKQQTCRANQVGGPKVKTNGVGRVQSNNEWMLKHNKNYKNVDEKLYRFEIFKDNLKYIDERNKMINGYWLGLNEFSDLS	348	"Experimental evidence at protein level"	39023.9	38999.18	7.11	--NA--	"FUNCTION:Thiol protease with a substrate specificity very different from the other thiol proteases.CATALYTIC ACTIVITY:Preferential cleavage: Gly-|-Xaa, in proteins and in small molecule substrates.ENZYME REGULATION:Not inhibited by cystatin.MISCELLANEOUS:Substitution of the conserved Gly residue by Glu- 155 could possibly explain the unusual specificity.SIMILARITY:Belongs to the peptidase C1 family."