ID   FRI1_SOYBN              Reviewed;         250 AA.
AC   P19976;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 4.
DT   24-JAN-2024, entry version 140.
DE   RecName: Full=Ferritin-1, chloroplastic;
DE            EC=1.16.3.1;
DE   AltName: Full=SFerH-1;
DE   AltName: Full=SOF-35;
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=1896472; DOI=10.1073/pnas.88.18.8222;
RA   Lescure A.-M., Proudhon D., Pesey H., Ragland M., Theil E.C., Briat J.-F.;
RT   "Ferritin gene transcription is regulated by iron in soybean cell
RT   cultures.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:8222-8226(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-189.
RC   TISSUE=Hypocotyl;
RX   PubMed=2211706; DOI=10.1016/s0021-9258(17)44757-0;
RA   Ragland M., Briat J.-F., Gagnon J., Laulhere J.-P., Massenet O.,
RA   Theil E.C.;
RT   "Evidence for conservation of ferritin sequences among plants and animals
RT   and for a transit peptide in soybean.";
RL   J. Biol. Chem. 265:18339-18344(1990).
RN   [3]
RP   PROTEIN SEQUENCE OF 50-63.
RC   STRAIN=cv. Mandarin; TISSUE=Seed;
RX   PubMed=2264818; DOI=10.1042/bj2720147;
RA   Lescure A.-M., Massenet O., Briat J.-F.;
RT   "Purification and characterization of an iron-induced ferritin from soybean
RT   (Glycine max) cell suspensions.";
RL   Biochem. J. 272:147-150(1990).
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. Plastid.
CC   -!- TISSUE SPECIFICITY: Leaf > hypocotyl.
CC   -!- MISCELLANEOUS: Multiple cleavage sites may occur in the extension
CC       peptide yielding several smaller (26.5 kDa) ferritins subunits.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA33958.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Vector contamination.; Evidence={ECO:0000305};
CC       Sequence=AAA34016.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Vector contamination.; Evidence={ECO:0000305};
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DR   EMBL; M58336; AAA33958.1; ALT_SEQ; mRNA.
DR   EMBL; M72894; AAA34016.1; ALT_SEQ; mRNA.
DR   EMBL; M64337; AAA33959.1; -; mRNA.
DR   PIR; A40992; A40992.
DR   RefSeq; NP_001238501.1; NM_001251572.1.
DR   AlphaFoldDB; P19976; -.
DR   SMR; P19976; -.
DR   STRING; 3847.P19976; -.
DR   PaxDb; 3847-GLYMA18G43650-2; -.
DR   GeneID; 547824; -.
DR   KEGG; gmx:547824; -.
DR   eggNOG; KOG2332; Eukaryota.
DR   InParanoid; P19976; -.
DR   OrthoDB; 4611704at2759; -.
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; IPR014034; Ferritin_CS.
DR   InterPro; IPR008331; Ferritin_DPS_dom.
DR   PANTHER; PTHR11431; FERRITIN; 1.
DR   PANTHER; PTHR11431:SF90; FERRITIN-1, CHLOROPLASTIC; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00540; FERRITIN_1; 1.
DR   PROSITE; PS00204; FERRITIN_2; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW   Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:2264818"
FT   CHAIN           50..250
FT                   /note="Ferritin-1, chloroplastic"
FT                   /id="PRO_0000008864"
FT   DOMAIN          83..236
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   REGION          50..82
FT                   /note="Extension peptide (EP)"
FT   BINDING         100
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         135
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         135
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         138
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         184
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         218
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   CONFLICT        161
FT                   /note="A -> V (in Ref. 2; AAA33958/AAA34016)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   250 AA;  28051 MW;  3A48F00B33D7CBA9 CRC64;
     MALAPSKVST FSGFSPKPSV GGAQKNPTCS VSLSFLNEKL GSRNLRVCAS TVPLTGVIFE
     PFEEVKKSEL AVPTAPQVSL ARQNYADECE SAINEQINVE YNASYVYHSL FAYFDRDNVA
     LKGFAKFFKE SSEEEREHAE KLMKYQNTRG GRVVLHPIKN APSEFEHVEK GDALYAMELA
     LSLEKLVNEK LLNVHSVADR NNDPQMADFI ESEFLSEQVE SIKKISEYVA QLRRVGKGHG
     VWHFDQRLLD
//