ID FRI2_SOYBN Reviewed; 257 AA. AC Q94IC4; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 110. DE RecName: Full=Ferritin-2, chloroplastic; DE EC=1.16.3.1; DE AltName: Full=SFerH-2; DE Flags: Precursor; OS Glycine max (Soybean) (Glycine hispida). 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; indigoferoid/millettioid clade; Phaseoleae; Glycine; OC Glycine subgen. Soja. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11278898; DOI=10.1074/jbc.m011399200; RA Masuda T., Goto F., Yoshihara T.; RT "A novel plant ferritin subunit from soybean that is related to a mechanism RT in iron release."; RL J. Biol. Chem. 276:19575-19579(2001). 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+) + 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. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. 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; AB062754; BAB60683.1; -; mRNA. DR PDB; 6J4J; X-ray; 2.10 A; A/B/C/D/E/H=49-257. DR PDB; 6J4M; X-ray; 2.60 A; A/H=49-257. DR PDBsum; 6J4J; -. DR PDBsum; 6J4M; -. DR SMR; Q94IC4; -. DR STRING; 3847.Q94IC4; -. DR PaxDb; 3847-GLYMA01G31300-1; -. DR eggNOG; KOG2332; Eukaryota. DR InParanoid; Q94IC4; -. DR Proteomes; UP000008827; Unplaced. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0008199; F:ferric iron binding; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central. DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central. DR GO; GO:0006826; P:iron ion transport; IEA:InterPro. DR CDD; cd01056; Euk_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; IPR008331; Ferritin_DPS_dom. DR PANTHER; PTHR11431; FERRITIN; 1. DR PANTHER; PTHR11431:SF101; FERRITIN-1, CHLOROPLASTIC; 1. DR Pfam; PF00210; Ferritin; 1. DR SUPFAM; SSF47240; Ferritin-like; 1. DR PROSITE; PS00204; FERRITIN_2; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Chloroplast; Iron; Iron storage; Metal-binding; KW Oxidoreductase; Plastid; Reference proteome; Transit peptide. FT TRANSIT 1..51 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 52..257 FT /note="Ferritin-2, chloroplastic" FT /id="PRO_0000008865" FT DOMAIN 85..238 FT /note="Ferritin-like diiron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT REGION 52..84 FT /note="Extension peptide (EP)" FT BINDING 102 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 137 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 137 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 140 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 186 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 220 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT HELIX 89..116 FT /evidence="ECO:0007829|PDB:6J4J" FT TURN 119..121 FT /evidence="ECO:0007829|PDB:6J4J" FT HELIX 124..151 FT /evidence="ECO:0007829|PDB:6J4J" FT TURN 170..172 FT /evidence="ECO:0007829|PDB:6J4J" FT HELIX 174..202 FT /evidence="ECO:0007829|PDB:6J4J" FT HELIX 206..215 FT /evidence="ECO:0007829|PDB:6J4J" FT HELIX 217..237 FT /evidence="ECO:0007829|PDB:6J4J" FT HELIX 241..251 FT /evidence="ECO:0007829|PDB:6J4J" SQ SEQUENCE 257 AA; 28734 MW; 9BACC4531D853EB9 CRC64; MALSCSKVLS FYLSPVVGGG DVPKKLTFSS FLGLSKGVGG SRSSRVCAAS NAPAPLAGVI FEPFQELKKD YLAVPIAHNV XLARQNYADD SESAINEQIN VEYNVSYVYH ALFAYFDRDN IALKGLAKFF KESSEEEREH AEQLIKYQNI RGGRVVLHPI TSPPSEFEHS EKGDALYAME LALSLEKLTN EKLLHVHSVA ERNNDPQXAD FIESEFLYEQ VKSIKKIAEY VAQLRLVGKG HGVWHFDQKL LHDEDHV //