ID FRI1_PEA Reviewed; 253 AA. AC P19975; Q43080; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 2. DT 10-JUN-2026, entry version 113. DE RecName: Full=Ferritin-1, chloroplastic; DE EC=1.16.3.1; DE Flags: Precursor; 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; Lathyrus. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1472006; DOI=10.1042/bj2880931; RA Lobreaux S., Yewdall S.J., Briat J.-F., Harrison P.M.; RT "Amino-acid sequence and predicted three-dimensional structure of pea seed RT (Pisum sativum) ferritin."; RL Biochem. J. 288:931-939(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7826338; DOI=10.1042/bj3050253; RA Van Wuytswinkel O., Savino G., Briat J.-F.; RT "Purification and characterization of recombinant pea-seed ferritins RT expressed in Escherichia coli: influence of N-terminus deletions on protein RT solubility and core formation in vitro."; RL Biochem. J. 305:253-261(1995). RN [3] RP PROTEIN SEQUENCE OF 48-82. RC TISSUE=Seed; RX PubMed=2536754; DOI=10.1016/s0021-9258(18)94113-x; RA Laulhere J.-P., Laboure A.M., Briat J.-F.; RT "Mechanism of the transition from plant ferritin to phytosiderin."; RL J. Biol. Chem. 264:3629-3635(1989). 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. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(2+) + O2 + 4 H(+) = 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. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid. 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 EMBL; X64417; CAA45763.1; -; mRNA. DR EMBL; X73369; CAA51786.1; -; mRNA. DR PIR; S27358; S27358. DR AlphaFoldDB; P19975; -. DR SMR; P19975; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro. DR GO; GO:0008198; F:ferrous iron binding; IEA:TreeGrafter. DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006879; P:intracellular iron ion homeostasis; IEA:InterPro. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IEA:UniProtKB-ARBA. DR CDD; cd01056; Euk_Ferritin; 1. DR FunFam; 1.20.1260.10:FF:000006; Ferritin; 1. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR001519; Ferritin. DR InterPro; IPR012347; Ferritin-like. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR014034; Ferritin_CS. DR InterPro; IPR008331; Ferritin_DPS_dom. DR PANTHER; PTHR11431; FERRITIN; 1. DR PANTHER; PTHR11431:SF90; FERRITIN-1, CHLOROPLASTIC; 1. DR Pfam; PF00210; Ferritin; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00540; FERRITIN_1; 1. DR PROSITE; PS00204; FERRITIN_2; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 1: Evidence at protein level; KW Chloroplast; Direct protein sequencing; Iron; Iron storage; Metal-binding; KW Oxidoreductase; Plastid; Transit peptide. FT TRANSIT 1..47 FT /note="Chloroplast" FT /evidence="ECO:0000269|PubMed:2536754" FT CHAIN 48..253 FT /note="Ferritin-1, chloroplastic" FT /id="PRO_0000008862" FT DOMAIN 81..234 FT /note="Ferritin-like diiron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT REGION 48..80 FT /note="Extension peptide (EP)" FT BINDING 98 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 136 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 182 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 216 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT CONFLICT 46 FT /note="S -> C (in Ref. 2; CAA51786)" FT /evidence="ECO:0000305" FT CONFLICT 101 FT /note="A -> V (in Ref. 2; CAA51786)" FT /evidence="ECO:0000305" FT CONFLICT 108 FT /note="L -> M (in Ref. 2; CAA51786)" FT /evidence="ECO:0000305" FT CONFLICT 133 FT /note="H -> E (in Ref. 2; CAA51786)" FT /evidence="ECO:0000305" FT CONFLICT 173 FT /note="Y -> H (in Ref. 2; CAA51786)" FT /evidence="ECO:0000305" SQ SEQUENCE 253 AA; 28619 MW; 9C754BCBDBC926F7 CRC64; MALSSSKFSS FSGFSLSPVS GNGVQKPCFC DLRVGEKWGS RKFRVSATTA PLTGVIFEPF EEVKKDYLAV PSVPLVSLAR QNFADECESV INEQINVEYN ASYVYHSLFA YFDRDNVALK GFAKFFKESS EEHREHAEKL MKYQNTRGGR VVLHPIKDVP SEFEHVEKGD ALYAMELALS LEKLTNEKLL NVHSVAERNN DLEMTHFIEG EYLAEQVEAI KKISEYVAQL RRVGKGHGVW HFDQRLLHGV HGA //