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_5475	IRT1_ARATH	--NA--	"Arabidopsis thaliana"	Brassicaceae	--NA--	Signaling-peptide	"Alternative splicing; Complete proteome; Ion transport; Iron; Iron transport; Membrane; Signal; Transmembrane; Transport | Fe(2) transport protein 1 precursor (Fe(II) transport protein 1),(Iron-regulated transporter 1).Cell membrane; Multi-pass membrane protein."	--NA--	FFFAVTTPFGIALGIALSTVYQDNSPKALITVGLLNACSAGLLIYMALVDIGLSLGATSDTCTIKGLIAALCFHQMFEGMGLGGCILQAEYTNMKKFVMAILIASMIGVGAPLFSRNVSFLQPDGNIFTIIKCFASGIILGTGFMHVLPDIMPHGHGHGHGPANDVTLPIKEDDSSNAQLLRYRVIAMVLELGIIVHSVVLLAAEFMGPKLQGSIKMQFKCLIAALLGCGGMSIIAKWAMKTIFLVLIFVSFAISPATSTAPEECGSESANPCVNKAKALPLKVIAIFVSFEMLSSICLEENPWHKFPFSGFLAMLSGLITLAIDSMATSLYTSKNAVG	339	"Experimental evidence at protein level"	35938.74	35914.64	6.76	--NA--	"FUNCTION:High-affinity iron transporter that plays a key role in the uptake of iron from the rhizosphere across the plasma membrane in the root epidermal layer. Acts as the principal regulator of iron homeostasis in planta. Also mediates the heavy metals uptake under iron-deficiency by its ability to transport cobalt, cadmium, manganese and/or zinc ions.ALTERNATIVE PRODUCTS:Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q38856-1; Sequence=Displayed; Name=2; IsoId=Q38856-2; Sequence=VSP_008361, VSP_008362; Note=May be due to an intron retention;TISSUE SPECIFICITY:Expressed in the external cell layers of the root including the lateral branching zone. Also detected in flowers before pollination.INDUCTION:In roots by iron starvation.MISCELLANEOUS:Inhibited by cadmium and Fe(2) ions and at 100- fold excess inhibited by cobalt, manganese and zinc ions. Loss-of- function mutant exhibits a lethal chlorotic phenotype.SIMILARITY:Belongs to the ZIP transporter (TC 2.A.5) family."
