FRI2_SOYBN
ID FRI2_SOYBN Reviewed; 257 AA.
AC Q94IC4;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ferritin-2, chloroplastic;
DE EC=1.16.3.1;
DE AltName: Full=SFerH-2;
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=11278898; DOI=10.1074/jbc.m011399200;
RA Masuda T., Goto F., Yoshihara T.;
RT "A novel plant ferritin subunit from soybean that is related to a mechanism
RT in iron release.";
RL J. Biol. Chem. 276:19575-19579(2001).
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.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB062754; BAB60683.1; -; mRNA.
DR PDB; 6J4J; X-ray; 2.10 A; A/B/C/D/E/H=49-257.
DR PDB; 6J4M; X-ray; 2.60 A; A/H=49-257.
DR PDBsum; 6J4J; -.
DR PDBsum; 6J4M; -.
DR SMR; Q94IC4; -.
DR STRING; 3847.GLYMA01G31300.1; -.
DR eggNOG; KOG2332; Eukaryota.
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; 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 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Iron; Iron storage; Metal-binding;
KW Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..257
FT /note="Ferritin-2, chloroplastic"
FT /id="PRO_0000008865"
FT DOMAIN 85..238
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT REGION 52..84
FT /note="Extension peptide (EP)"
FT BINDING 102
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
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 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT BINDING 220
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT HELIX 89..116
FT /evidence="ECO:0007829|PDB:6J4J"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:6J4J"
FT HELIX 124..151
FT /evidence="ECO:0007829|PDB:6J4J"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:6J4J"
FT HELIX 174..202
FT /evidence="ECO:0007829|PDB:6J4J"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:6J4J"
FT HELIX 217..237
FT /evidence="ECO:0007829|PDB:6J4J"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:6J4J"
SQ SEQUENCE 257 AA; 28734 MW; 9BACC4531D853EB9 CRC64;
MALSCSKVLS FYLSPVVGGG DVPKKLTFSS FLGLSKGVGG SRSSRVCAAS NAPAPLAGVI
FEPFQELKKD YLAVPIAHNV XLARQNYADD SESAINEQIN VEYNVSYVYH ALFAYFDRDN
IALKGLAKFF KESSEEEREH AEQLIKYQNI RGGRVVLHPI TSPPSEFEHS EKGDALYAME
LALSLEKLTN EKLLHVHSVA ERNNDPQXAD FIESEFLYEQ VKSIKKIAEY VAQLRLVGKG
HGVWHFDQKL LHDEDHV
