FRI1_SOYBN
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 03-AUG-2022, entry version 135.
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.GLYMA18G43650.2; -.
DR GeneID; 547824; -.
DR KEGG; gmx:547824; -.
DR eggNOG; KOG2332; Eukaryota.
DR OrthoDB; 1249457at2759; -.
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 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 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
