ID FRI2_PEA Reviewed; 13 AA. AC P83445; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 24-JAN-2024, entry version 54. DE RecName: Full=Ferritin-2, chloroplastic; DE EC=1.16.3.1; DE Flags: Fragment; OS Pisum sativum (Garden pea) (Lathyrus oleraceus). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum. OX NCBI_TaxID=3888 {ECO:0000305}; RN [1] {ECO:0000305} RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=cv. Laxton's Progress; TISSUE=Leaf; RA Shingles R., McCarty R.E.; RL Submitted (SEP-2002) to UniProtKB. CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form. CC Important for iron homeostasis. Has ferroxidase activity. Iron is taken CC up in the ferrous form and deposited as ferric hydroxides after CC oxidation (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O; CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1; CC -!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits: L CC (light) chain and H (heavy) chain. The major chain can be light or CC heavy, depending on the species and tissue type. The functional CC molecule forms a roughly spherical shell with a diameter of 12 nm and CC contains a central cavity into which the insoluble mineral iron core is CC deposited (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane CC {ECO:0000269|Ref.1}. Note=And other plastids. CC -!- TISSUE SPECIFICITY: Leaves. {ECO:0000269|Ref.1, ECO:0000305}. CC -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: CC 4.74, its MW is: 25.7 kDa. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Chloroplast; Direct protein sequencing; Iron; Iron storage; Membrane; KW Metal-binding; Oxidoreductase; Plastid; Plastid inner membrane. FT CHAIN 1..>13 FT /note="Ferritin-2, chloroplastic" FT /id="PRO_0000201084" FT NON_TER 13 FT /evidence="ECO:0000305" SQ SEQUENCE 13 AA; 1246 MW; 26C9DC25F334ADC7 CRC64; ATTDSPATLT GVI //