FRI1_PEA
ID FRI1_PEA Reviewed; 253 AA.
AC P19975; Q43080;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ferritin-1, chloroplastic;
DE EC=1.16.3.1;
DE Flags: Precursor;
OS Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1472006; DOI=10.1042/bj2880931;
RA Lobreaux S., Yewdall S.J., Briat J.-F., Harrison P.M.;
RT "Amino-acid sequence and predicted three-dimensional structure of pea seed
RT (Pisum sativum) ferritin.";
RL Biochem. J. 288:931-939(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7826338; DOI=10.1042/bj3050253;
RA Van Wuytswinkel O., Savino G., Briat J.-F.;
RT "Purification and characterization of recombinant pea-seed ferritins
RT expressed in Escherichia coli: influence of N-terminus deletions on protein
RT solubility and core formation in vitro.";
RL Biochem. J. 305:253-261(1995).
RN [3]
RP PROTEIN SEQUENCE OF 48-82.
RC TISSUE=Seed;
RX PubMed=2536754; DOI=10.1016/s0021-9258(18)94113-x;
RA Laulhere J.-P., Laboure A.M., Briat J.-F.;
RT "Mechanism of the transition from plant ferritin to phytosiderin.";
RL J. Biol. Chem. 264:3629-3635(1989).
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 -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR EMBL; X64417; CAA45763.1; -; mRNA.
DR EMBL; X73369; CAA51786.1; -; mRNA.
DR PIR; S27358; S27358.
DR AlphaFoldDB; P19975; -.
DR SMR; P19975; -.
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; 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; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:2536754"
FT CHAIN 48..253
FT /note="Ferritin-1, chloroplastic"
FT /id="PRO_0000008862"
FT DOMAIN 81..234
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT REGION 48..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 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 46
FT /note="S -> C (in Ref. 2; CAA51786)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="A -> V (in Ref. 2; CAA51786)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="L -> M (in Ref. 2; CAA51786)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="H -> E (in Ref. 2; CAA51786)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="Y -> H (in Ref. 2; CAA51786)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 28619 MW; 9C754BCBDBC926F7 CRC64;
MALSSSKFSS FSGFSLSPVS GNGVQKPCFC DLRVGEKWGS RKFRVSATTA PLTGVIFEPF
EEVKKDYLAV PSVPLVSLAR QNFADECESV INEQINVEYN ASYVYHSLFA YFDRDNVALK
GFAKFFKESS EEHREHAEKL MKYQNTRGGR VVLHPIKDVP SEFEHVEKGD ALYAMELALS
LEKLTNEKLL NVHSVAERNN DLEMTHFIEG EYLAEQVEAI KKISEYVAQL RRVGKGHGVW
HFDQRLLHGV HGA
