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_4383	CALR1_ARATH	--NA--	"Arabidopsis thaliana"	Brassicaceae	--NA--	Signaling-peptide	"Alternative splicing; Calcium; Chaperone; Complete proteome; Endoplasmic reticulum; Glycoprotein; Lectin; Metal-binding; Repeat; Signal; Zinc | Calreticulin-1 precursor.Endoplasmic reticulum lumen (By similarity)."	--NA--	AKKPEDWDDEEDGEWTAPTIPNPEYNGEWKPKKIKNPAYKGKWKAPMIDNGEWKHTAGNWSGDANDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFSVKHEQKLDCGGGYMKLLSDDVDQTKFGGDTPYSIMFGPDICGYSTKKVHAILTYNGTNHLIKKEVPCETDQLTHVYTFVLRPDATYSILIDNVEKQTGSLYMAKLNPKFISLILFALVVIVSAEVIFEEKFEDGWEKRWVKSDWKKDDNTAPEFKDDPELYVFPKLKYVGVELWQVKSGSLFDNVLVSDDPEYAKKLAEETSDWDLLPAKKIKDPSAKKPEDWDDKEYIPDPEDTKPAGYDDIPKEIPDTDSKSEETKEAEETKEAEETDAAHDELWGKHKDAEKAAFDEAEKKREEEESKDAPAESDAEEEAEDDDNEGDDSDNE	425	"Experimental evidence at protein level"	48527.35	48497.35	4.46	--NA--	"FUNCTION:Molecular calcium binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).ALTERNATIVE PRODUCTS:Event=Alternative splicing; Named isoforms=1; Comment=A number of isoforms are produced. According to EST sequences; Name=1; IsoId=O04151-1; Sequence=Displayed;DOMAIN:Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity).DOMAIN:The interaction with glycans occurs through a binding site in the globular lectin domain (By similarity).DOMAIN:The zinc binding sites are localized to the N-domain (By similarity).SIMILARITY:Belongs to the calreticulin family."