ID   FTMT_BOVIN              Reviewed;         242 AA.
AC   Q2YDI9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   08-NOV-2023, entry version 94.
DE   RecName: Full=Ferritin, mitochondrial {ECO:0000250|UniProtKB:Q8N4E7};
DE            EC=1.16.3.1 {ECO:0000250|UniProtKB:Q8N4E7};
DE   Flags: Precursor;
GN   Name=FTMT {ECO:0000250|UniProtKB:Q8N4E7};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of ferrous iron(II) to ferric
CC       iron(III) and stores iron in a soluble, non-toxic, readily available
CC       form. Important for iron homeostasis. Iron is taken up in the ferrous
CC       form and deposited as ferric hydroxides after oxidation.
CC       {ECO:0000250|UniProtKB:Q8N4E7}.
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:0000250|UniProtKB:Q8N4E7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11149;
CC         Evidence={ECO:0000250|UniProtKB:Q8N4E7};
CC   -!- SUBUNIT: Homooligomer of 24 subunits. The functional molecule is
CC       roughly spherical and contains a central cavity into which the
CC       polymeric mineral iron core is deposited (By similarity).
CC       {ECO:0000250|UniProtKB:Q8N4E7}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8N4E7}.
CC   -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
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DR   EMBL; BC110199; AAI10200.1; -; mRNA.
DR   RefSeq; NP_001069658.1; NM_001076190.1.
DR   AlphaFoldDB; Q2YDI9; -.
DR   SMR; Q2YDI9; -.
DR   STRING; 9913.ENSBTAP00000041498; -.
DR   PaxDb; 9913-ENSBTAP00000041498; -.
DR   GeneID; 539838; -.
DR   KEGG; bta:539838; -.
DR   CTD; 94033; -.
DR   eggNOG; KOG2332; Eukaryota.
DR   InParanoid; Q2YDI9; -.
DR   OrthoDB; 4611704at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; ISS:UniProtKB.
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:SF30; FERRITIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   SUPFAM; SSF47240; Ferritin-like; 1.
DR   PROSITE; PS00204; FERRITIN_2; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Iron; Iron storage; Metal-binding; Mitochondrion; Oxidoreductase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..242
FT                   /note="Ferritin, mitochondrial"
FT                   /id="PRO_0000252366"
FT   DOMAIN          70..219
FT                   /note="Ferritin-like diiron"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT   BINDING         87
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4E7"
FT   BINDING         122
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4E7"
FT   BINDING         122
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4E7"
FT   BINDING         125
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4E7"
FT   BINDING         167
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4E7"
FT   BINDING         201
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4E7"
SQ   SEQUENCE   242 AA;  27366 MW;  B2B73D45C936A669 CRC64;
     MLPCSLFLPK HISTSLVFLR SARHGFALLP RWVPRLSSDY PPAAPIRLLA AAASSRRPAD
     GAGAPSRVRQ NFHPDSEAAI NRQINLELYA SYVYLSMAYY FSRDDVALHN FARYFLRLSR
     EEAEHAEKLM RLQNQRGGLI CLQDIKKPDQ NDWKSGLNAM ECALLLEKNV NQSLLELHTL
     ASDKGDPHLC DFLETHYLNE QVKSIKELGD HVNNLVKMGA PESGLAEYLF DKHTLGNENN
     HN
//