ID K3ZJM0_SETIT Unreviewed; 253 AA.
AC K3ZJM0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Ferritin {ECO:0000256|RuleBase:RU361145};
DE EC=1.16.3.1 {ECO:0000256|RuleBase:RU361145};
GN Name=101778084 {ECO:0000313|EnsemblPlants:KQK93438};
GN ORFNames=SETIT_8G019400v2 {ECO:0000313|EMBL:RCV36909.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV36909.1};
RN [1] {ECO:0000313|EMBL:RCV36909.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK93438,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV36909.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV36909.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV36909.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK93438}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK93438};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
RN [4] {ECO:0007829|PDB:7XZ4}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 46-253 IN COMPLEX WITH FE(3+).
RX PubMed=36576327; DOI=10.1021/acs.jafc.2c07595;
RA Wang W., Wang Y., Xi H., Song Z., Zhang W., Xie L., Ma D., Qin N., Wang H.;
RT "Extension Peptide of Plant Ferritin from <i>Setaria italica</i> Presents a
RT Novel Fold.";
RL J. Agric. Food Chem. 71:934-943(2023).
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. {ECO:0000256|ARBA:ARBA00025111}.
CC -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available form.
CC Important for iron homeostasis. Iron is taken up in the ferrous form
CC and deposited as ferric hydroxides after oxidation.
CC {ECO:0000256|RuleBase:RU361145}.
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 Evidence={ECO:0000256|ARBA:ARBA00001830,
CC ECO:0000256|RuleBase:RU361145};
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. {ECO:0000256|ARBA:ARBA00026060}.
CC -!- SIMILARITY: Belongs to the ferritin family.
CC {ECO:0000256|ARBA:ARBA00007513, ECO:0000256|RuleBase:RU361145}.
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DR EMBL; AGNK02004608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003535; RCV36909.1; -; Genomic_DNA.
DR RefSeq; XP_004978583.1; XM_004978526.3.
DR PDB; 7XZ4; X-ray; 2.20 A; A=46-253.
DR STRING; 4555.K3ZJM0; -.
DR EnsemblPlants; KQK93438; KQK93438; SETIT_026773mg.
DR GeneID; 101778084; -.
DR Gramene; KQK93438; KQK93438; SETIT_026773mg.
DR KEGG; sita:101778084; -.
DR eggNOG; KOG2332; Eukaryota.
DR OMA; QKYSDEC; -.
DR OrthoDB; 4611704at2759; -.
DR Proteomes; UP000004995; Chromosome VIII.
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:SF125; 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 3D-structure {ECO:0007829|PDB:7XZ4};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361145};
KW Iron storage {ECO:0000256|ARBA:ARBA00022434,
KW ECO:0000256|RuleBase:RU361145};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361145};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361145};
KW Reference proteome {ECO:0000313|Proteomes:UP000004995}.
FT DOMAIN 83..236
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000259|PROSITE:PS50905"
FT BINDING 202
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7XZ4"
FT BINDING 208
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7XZ4"
FT BINDING 251
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="3"
FT /evidence="ECO:0007829|PDB:7XZ4"
SQ SEQUENCE 253 AA; 28002 MW; DF2A97AC12EBC6F4 CRC64;
MMLRVSPSPA AAAAAASHPS APAAAPASVR VAAPRVSPPF GTACRAAGKG KEVLSGVVFQ
PFEEIKGELS LVPQTPDKSL ARQKFVDECE AAINEQINVE YNASYAYHSL FAYFDRDNVA
LKGFAKFFKE SSDEEREHAE KLMKYQNTRG GRVRLQSIVT PLTEFDHPEK GDALYAMELA
LALEKLVNEK LHNLHAVATR CNDPQLTDFI ESEFLADQVE DIKKISEYVA QLRRVGKGHG
VWHFDQKLLE EEA
//
