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_4125	RLK90_ARATH	--NA--	"Arabidopsis thaliana"	Brassicaceae	--NA--	Signaling-peptide	"ATP-binding; Complete proteome; Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Repeat; Signal; Transmembrane | Probable inactive receptor kinase RLK902 precursor (Receptor-like,kinase 902).Cell membrane; Single-pass membrane protein."	--NA--	ADREFKEKIEVVGAMDHENLVPLRAYYYSGDEKLLVYDFMPMGSLSALLHAENEFSGEISSGFKNLTRLKTLYLENNKLSGSLLDLDLSLDQFNVSNNLLFGNATKVFDLEDLLRASAEVLGKGTFGTAYKAVLDAVTLVAVKRLKDVTMGNKGAGRPPLNWEVRSGIALGAARGLDYLHSQDPLSSHGNVKSSNILLTNGSEEKKKRKKLSGGAIAGIVIGCVVGLSLIVMILMVLFRKKGNERTRAIDLATIKHHEVEIPGEKAAVEAPENRSYVNEYSPSAVKAVEVNSSGMKKLVFLWDVKQTSPCNWTGVLCDGGRVTALRLPGETLSGHIPEGIFGNLTQLRTLMRLFFTPSMSNLSIFFSILLLSLPLPSIGDLAADKSALLSFRSAVGGRTLNGSIPKSLQKFDSDSFVGTSLCGKPLVVCSNEGTVPSQPISVGNIPGTVESHDARVSDFGLAQLVSASSTTPNRATGYRAPEVTDPRRVSQKADVYSFGVSLRLNGLTGSLPLDLGSCSDLRRLYLQGNRFSGEIPEVLFSLSNLVRLNLVLLELLTGKAPSNSVMNEEGMDLARWVHSVAREEWRNEVFDSELMSIETVVSVEEEMAEMLQLGIDCTEQHPDKRPVMVEVVRRIQELRQSGADRVG	647	"Experimental evidence at protein level"	70405.68	70361.54	6.16	--NA--	"SUBUNIT:Interacts with At3g17950, At3g27210 and At5g05190.TISSUE SPECIFICITY:Expressed in root tips, lateral root primordia, stipules, and floral organ abscission zones.INDUCTION:By wounding. Rapid but transient down-regulation by salicylic acid treatment or pathogen infection.DOMAIN:The protein kinase domain is predicted to be catalytically inactive.PTM:Autophosphorylation.MISCELLANEOUS:Loss-of-function mutant (T-DNA insertion) does not show any phenotype alteration.SIMILARITY:Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.SIMILARITY:Contains 5 LRR (leucine-rich) repeats.SIMILARITY:Contains 1 protein kinase domain.CAUTION:Autophosphorylation is proposed (PubMed:15618630) although the protein kinase domain is predicted to be catalytically inactive."