FRI2_MAIZE
ID FRI2_MAIZE Reviewed; 252 AA.
AC P29390; Q43259;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ferritin-2, chloroplastic;
DE EC=1.16.3.1;
DE AltName: Full=ZmFer2;
DE Flags: Precursor;
GN Name=FER2;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 44-72.
RC STRAIN=cv. Missouri 17; TISSUE=Root, and Seed;
RX PubMed=1627771; DOI=10.1007/bf00026783;
RA Lobreaux S., Massenet O., Briat J.-F.;
RT "Iron induces ferritin synthesis in maize plantlets.";
RL Plant Mol. Biol. 19:563-575(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. B73; TISSUE=Seedling;
RX PubMed=7649160; DOI=10.1111/j.1432-1033.1995.tb20739.x;
RA Fobis-Loisy I., Loridon K., Lobreaux S., Lebrun M., Briat J.-F.;
RT "Structure and differential expression of two maize ferritin genes in
RT response to iron and abscisic acid.";
RL Eur. J. Biochem. 231:609-619(1995).
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: Ferritins accumulate in seed during maturation.
CC Then, they are degraded during the first days of germination. Present
CC in roots and leaves after iron treatment.
CC -!- INDUCTION: By iron.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA43664.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X61392; CAA43664.1; ALT_INIT; mRNA.
DR EMBL; X83077; CAA58147.1; -; Genomic_DNA.
DR PIR; S24057; S24057.
DR AlphaFoldDB; P29390; -.
DR SMR; P29390; -.
DR PRIDE; P29390; -.
DR MaizeGDB; 25278; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P29390; baseline and differential.
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; 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..43
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:1627771"
FT CHAIN 44..252
FT /note="Ferritin-2, chloroplastic"
FT /id="PRO_0000008860"
FT DOMAIN 81..234
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT REGION 44..80
FT /note="Extension peptide (EP)"
FT BINDING 98
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 136
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 216
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT CONFLICT 217
FT /note="G -> V (in Ref. 2; CAA58147)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="A -> G (in Ref. 2; CAA58147)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 252 AA; 27749 MW; D181B4A8A86ADED0 CRC64;
MMLRVSSSPA AAVANHLSGG AAATTAPARV TAQRSGVSLS AAAAAGKGKE VLSGVVFQPF
EEIKGELALV PQSPDRSLAR HKFVDDCEAA INEQINVEYN ASYAYHSLFA YFDRDNVALK
GFAKFFKESS DEEREHAEKL MEYQNKRGGR VRLQSIVAPL TEFDHPEKGD ALYAMELTLA
LEKLVNEKLH SLHGVATRCN DPQLIDFIES EFLEEQGEAI NKVSKYVAQL RRVGNKGHGV
WHFDQMLLQE AA
