ID   FRI2_VIGUN              Reviewed;         250 AA.
AC   Q41709;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Ferritin-2, chloroplastic;
DE            EC=1.16.3.1;
DE   Flags: Precursor;
GN   Name=PFE2;
OS   Vigna unguiculata (Cowpea).
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; Vigna.
OX   NCBI_TaxID=3917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. N41; TISSUE=Leaf;
RX   PubMed=9895297; DOI=10.1042/bj3370523;
RA   Wardrop A.J., Wicks R.E., Entsch B.;
RT   "Occurrence and expression of members of the ferritin gene family in
RT   cowpeas.";
RL   Biochem. J. 337:523-530(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 53-123.
RC   STRAIN=cv. N41; TISSUE=Leaf;
RX   PubMed=8484787; DOI=10.1006/bbrc.1993.1487;
RA   Wicks R.E., Entsch B.;
RT   "Functional genes found for three different plant ferritin subunits in the
RT   legume, Vigna unguiculata.";
RL   Biochem. Biophys. Res. Commun. 192:813-819(1993).
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.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR   EMBL; AF052058; AAC06027.1; -; mRNA.
DR   EMBL; X67755; CAA47983.1; -; Genomic_DNA.
DR   PIR; PQ0614; PQ0614.
DR   PIR; T08124; T08124.
DR   AlphaFoldDB; Q41709; -.
DR   SMR; Q41709; -.
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; 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..43
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..250
FT                   /note="Ferritin-2, chloroplastic"
FT                   /id="PRO_0000008870"
FT   DOMAIN          77..230
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   REGION          44..76
FT                   /note="Extension peptide (EP)"
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
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         129
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         132
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         178
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         212
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
SQ   SEQUENCE   250 AA;  28041 MW;  7A5E7AE5024B0656 CRC64;
     MLLRTAAASS LSLFNPNAEP SRSVPVLANN ASRLVVRAAK GSTNHRALTG VIFEPFEEVK
     KELDLVPTVP QASLARQKYV DESEAAVNEQ INVEYNVSYV YHALFAYFDR DNVALRGLAK
     FFKESSEEER EHAEKLMEYQ NRRGGKVKLQ SIVMPLSEFD HADKGDALHA MELALSLEKL
     TNEKLLHLHS VATKNGDVQL ADFVESEFLG EQVESIKRIS EYVAQLRRVG KGHGVWHFDQ
     MLLHEGGHLA