FRI4_SOYBN
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 03-AUG-2022, entry version 112.
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}.
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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.GLYMA14G06160.1; -.
DR PRIDE; Q948P5; -.
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; CESAINQ; -.
DR OrthoDB; 1249457at2759; -.
DR EvolutionaryTrace; Q948P5; -.
DR Proteomes; UP000008827; Chromosome 14.
DR Genevisible; Q948P5; GM.
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 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; PTHR11431; 1.
DR Pfam; PF00210; Ferritin; 1.
DR SUPFAM; SSF47240; SSF47240; 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..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
