ID FRI4_SOYBN Reviewed; 247 AA. AC Q948P5; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 2. DT 27-MAR-2024, entry version 119. DE RecName: Full=Ferritin-4, chloroplastic; DE EC=1.16.3.1; DE AltName: Full=SFerH-4; 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=17904862; DOI=10.1016/j.pep.2007.07.011; RA Masuda T., Goto F., Yoshihara T., Ezure T., Suzuki T., Kobayashi S., RA Shikata M., Utsumi S.; RT "Construction of homo- and heteropolymers of plant ferritin subunits using RT an in vitro protein expression system."; RL Protein Expr. Purif. 56:237-246(2007). 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 {ECO:0000250}. 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; AB062756; BAB64537.2; -; mRNA. DR RefSeq; NP_001237049.1; NM_001250120.1. DR PDB; 3A68; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=36-247. DR PDB; 3A9Q; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=36-247. DR PDBsum; 3A68; -. DR PDBsum; 3A9Q; -. DR AlphaFoldDB; Q948P5; -. DR SMR; Q948P5; -. DR STRING; 3847.Q948P5; -. DR PaxDb; 3847-GLYMA14G06160-1; -. DR EnsemblPlants; KRH14913; KRH14913; GLYMA_14G056800. DR GeneID; 547477; -. DR Gramene; KRH14913; KRH14913; GLYMA_14G056800. DR KEGG; gmx:547477; -. DR eggNOG; KOG2332; Eukaryota. DR HOGENOM; CLU_065681_0_0_1; -. DR InParanoid; Q948P5; -. DR OMA; LKEMGGY; -. DR OrthoDB; 4611704at2759; -. DR EvolutionaryTrace; Q948P5; -. DR Proteomes; UP000008827; Chromosome 14. 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; IPR014034; Ferritin_CS. DR InterPro; IPR008331; Ferritin_DPS_dom. DR PANTHER; PTHR11431; FERRITIN; 1. DR PANTHER; PTHR11431:SF128; FERRITIN-3, 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. DR Genevisible; Q948P5; GM. 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..40 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 41..247 FT /note="Ferritin-4, chloroplastic" FT /id="PRO_0000008867" FT DOMAIN 74..227 FT /note="Ferritin-like diiron" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT REGION 41..73 FT /note="Extension peptide (EP)" FT BINDING 91 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 126 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 126 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 129 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 175 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT BINDING 209 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085" FT HELIX 52..56 FT /evidence="ECO:0007829|PDB:3A68" FT TURN 57..62 FT /evidence="ECO:0007829|PDB:3A68" FT HELIX 78..105 FT /evidence="ECO:0007829|PDB:3A68" FT TURN 108..110 FT /evidence="ECO:0007829|PDB:3A68" FT HELIX 113..140 FT /evidence="ECO:0007829|PDB:3A68" FT TURN 159..161 FT /evidence="ECO:0007829|PDB:3A68" FT HELIX 163..191 FT /evidence="ECO:0007829|PDB:3A68" FT HELIX 195..204 FT /evidence="ECO:0007829|PDB:3A68" FT HELIX 206..226 FT /evidence="ECO:0007829|PDB:3A68" FT HELIX 230..240 FT /evidence="ECO:0007829|PDB:3A68" SQ SEQUENCE 247 AA; 27559 MW; 9A643DDFB5DDEDE3 CRC64; MLLRTAAASA SSLSLFSPNA EPPRSVPARG LVVRAAKGST NHRALTGVIF EPFEEVKKEL DLVPTVPQAS LARQKYVDES ESAVNEQINV EYNVSYVYHA MFAYFDRDNV ALRGLAKFFK ESSEEEREHA EKLMEYQNKR GGKVKLQSIV MPLSDFDHAD KGDALHAMEL ALSLEKLTNE KLLNLHSVAT KNGDVQLADF VETEYLGEQV EAIKRISEYV AQLRRVGKGH GVWHFDQMLL HEGGDAA //