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_4883	LECT_SOLTU	--NA--	"Solanum tuberosum"	Solanaceae	--NA--	Signaling-peptide	"Chitin-binding; Direct protein sequencing; Glycoprotein; Hydroxylation; Lectin; Repeat; Signal | Chitin-binding lectin 1 precursor (PL-I)."	--NA--	CPGPYPEGRCGWQANGKSCPTGTGHCCSNAGWCGTTSDYCAPVNCQAQCNGPYPEGRCGWQANGKSCPTGTGQCCSNGGWCGTTSDYCASKNCQSQCKLPMKETAISVLALLTLFLLEVVSANELSLPFHLPINETIGLEVFQGINNASPPPPPPPALPYPQCGIKKGGGKCIKTGECCSIWGWCGTTNAYCSPGYCQKQPSPSPLPYPQCGMKKGGGKCIKTGECCSIWGWCGTTNAYCSPGYCQKQCPSPPPPPPPPSPPPPSPPSPPPPSPPPPPPPSPPPPSPPPPSPSPPPPPASTTTLTSPIKNRMRGIESFMLNVV	323	"Experimental evidence at protein level"	33554.47	33531.5	8.4	--NA--	"FUNCTION:This protein might function as a defense against chitin containing pathogens. Binds to several branched or linear N- acetyllactosamine-containing glycosphingolipids and also to lactosylceramide with sphingosine and non-hydroxy fatty acids.SUBUNIT:Homodimer (Probable).PTM:Heavily glycosylated with beta-arabinose on hydroxyprolines and with alpha-galactose on serines of the extensin-like domain.As no other sugars could be detected in the native lectin, it is unlikely that the three putative N-glycosylation sites are actually glycosylated.PTM:The N-terminus is blocked. The N-terminal sequences proposed in PubMed:9022287 and PubMed:11056399 originate probably from truncated proteins.SIMILARITY:In the central section; belongs to the extensin family.SIMILARITY:Contains 4 chitin-binding type-1 domains."