ID   FRI_PHAVU               Reviewed;         254 AA.
AC   P25699;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Ferritin, chloroplastic;
DE            EC=1.16.3.1;
DE   Flags: Precursor;
GN   Name=PFE;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Tendergreen; TISSUE=Seed;
RX   PubMed=1884000; DOI=10.1007/bf00040644;
RA   Spence M.J., Henzl M.T., Lammers P.J.;
RT   "The structure of a Phaseolus vulgaris cDNA encoding the iron storage
RT   protein ferritin.";
RL   Plant Mol. Biol. 17:499-504(1991).
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. Plastid.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR   EMBL; X58274; CAA41213.1; ALT_SEQ; mRNA.
DR   PIR; S17426; FRFBH.
DR   RefSeq; XP_007140214.1; XM_007140152.1.
DR   AlphaFoldDB; P25699; -.
DR   SMR; P25699; -.
DR   STRING; 3885.XP_007140214.1; -.
DR   ProMEX; P25699; -.
DR   EnsemblPlants; ESW12208; ESW12208; PHAVU_008G093700g.
DR   GeneID; 18622338; -.
DR   Gramene; ESW12208; ESW12208; PHAVU_008G093700g.
DR   KEGG; pvu:PHAVU_008G093700g; -.
DR   eggNOG; KOG2332; Eukaryota.
DR   OMA; QNYHSEV; -.
DR   OrthoDB; 1249457at2759; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
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; PS00540; FERRITIN_1; 1.
DR   PROSITE; PS00204; FERRITIN_2; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Iron; Iron storage; Metal-binding; Oxidoreductase; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..48
FT                   /note="Chloroplast"
FT   CHAIN           49..254
FT                   /note="Ferritin, chloroplastic"
FT                   /id="PRO_0000008863"
FT   DOMAIN          82..235
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   REGION          49..81
FT                   /note="Extension peptide (EP)"
FT   BINDING         99
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         134
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         134
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
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         183
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         217
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ   SEQUENCE   254 AA;  28304 MW;  60B0E974D3F4435F CRC64;
     MALAPSKVSP FSGFSLSDGV GAVRNPTCSV SLSFLNKKVG SRNLGVSAST VPLTGVIFEP
     FEEVKKEELA VPTAGQVSLA RQYYADECES AINEQINVEY NASYVYHSLF AYFDRDNVAL
     KGFARFFKES SEEEREHAEK LMKYQNTRGG RVVLHPIKNV PSEFEHVEKG DALYAMELAL
     SLEKLVNEKL RSVHSVADRN KDPQLADFIE SEFLSEQVEA IKKISEYVAQ LRMVGKGHGV
     WHFDQSLLHD GHAA