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Ferritin-2, chloroplastic

Pisum sativum (Garden pea)
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli


Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity).By similarity

Catalytic activityi

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni


Keywords - Biological processi

Iron storage

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ferritin-2, chloroplastic (EC:
OrganismiPisum sativum (Garden pea)Curated
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

  • Plastidchloroplast inner membrane 1 Publication

  • Note: And other plastids.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Plastid inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›13›13Ferritin-2, chloroplasticPRO_0000201084Add


Tissue specificityi

Leaves.Curated1 Publication


Subunit structurei

Oligomer of 24 subunits. There are two types of subunits: L (light) chain and H (heavy) chain. The major chain can be light or heavy, depending on the species and tissue type. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited (By similarity).By similarity

Family & Domainsi

Sequence similaritiesi

Belongs to the ferritin family.Curated


Sequence statusi: Fragment.

Mass (Da):1,246
Last modified:October 1, 2002 - v1

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei13 – 131Curated


3D structure databases


Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases


Entry informationi

Entry nameiFRI2_PEA
AccessioniPrimary (citable) accession number: P83445
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: October 1, 2002
Last modified: January 7, 2015
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program



On the 2D-gel the determined pI of this protein is: 4.74, its MW is: 25.7 kDa.Curated

Keywords - Technical termi

Direct protein sequencing


  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.