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_5234	SCP24_ARATH	--NA--	"Arabidopsis thaliana"	Brassicaceae	--NA--	Signaling-peptide	"Carboxypeptidase; Complete proteome; Glycoprotein; Hydrolase; Protease; Secreted; Signal; Zymogen | Serine carboxypeptidase 24 precursor (EC 3.4.16.6) (Serine,carboxypeptidase II) (Carboxypeptidase D) (Bri1 suppressor 1),[Contains: Serine carboxypeptidase 24 chain A (Serine carboxypeptidase,II chain A); Serine carboxypeptidase 24 chain B (Serine,carboxypeptidase II chain B)].Secreted, extracellular space."	--NA--	DVLIKTWKDSDKTMLPIYKELAASGLRIWIFSGDTDSVVPVTATRFSLSHFSKPIINLKGFLVGNAVTDNQYDSIGTVTYWWTHAIISDKSYKSILKYCNFTVERVSDDCDNAVNYAMNHEFGDIDQYSIYTPTCVAAQQKKNTTGFFVRLFRSFLAGKELPRSYLNLPVKTRWYPWYTDNQVGGWTEVYKGLTFATVRGAGHEVPLFEPKRALIMARTHFIFLLLVALLSTTFPSSSSSREQEKDRIKALPGQPKVAFSQYSGYMKNTLLRRRLVSGYDPCTESYAEKYFNRPDVQRAMHANVTGIRYKWTACSPFRINKTGSNLYLNKFAWNKDANLLFLESPAGVGYSYTNTSSDLKDSGDERTAQDNLIFLIKWLSRFPQYKYRDFYIAGESYAGHYVPQLAKKINDYNKAVNVNQSHGRALFYWLTESSSPSPHTKPLLLWLNGGPGCSSIAYGASEEIG	465	"Experimental evidence at protein level"	52844.97	52811.7	9.21	--NA--	"FUNCTION:Active serine carboxypeptidase with broad substrate preference, including basic and hydrophilic groups. Processes a protein involved in an early event in the brassinosteroid signaling pathway.CATALYTIC ACTIVITY:Preferential release of a C-terminal arginine or lysine residue.ENZYME REGULATION:Completely inhibited by phenylmethylsulphonylfluoride (PMSF) and partially by leupeptin.BIOPHYSICOCHEMICAL PROPERTIES:pH dependence: Optimum pH is 5.5; Temperature dependence: Optimum temperature is 50 degrees Celsius;SUBUNIT:Heterodimer (Potential).TISSUE SPECIFICITY:Expressed in shoots, leaves, cauline leaves, siliques and flowers. Expressed a low levels in roots and stems.PTM:N-glycosylated.MISCELLANEOUS:The serine carboxypeptidase activity is necessary for suppression of bri1 mutant phenotype.SIMILARITY:Belongs to the peptidase S10 family."