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Ferritin, mitochondrial (EC 1.16.3.1)

 FTMT_HUMAN              Reviewed;         242 AA.
Q8N4E7;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
22-NOV-2017, entry version 122.
RecName: Full=Ferritin, mitochondrial;
EC=1.16.3.1;
Flags: Precursor;
Name=FTMT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11323407; DOI=10.1074/jbc.C100141200;
Levi S., Corsi B., Bosisio M., Invernizzi R., Volz A., Sanford D.,
Arosio P., Drysdale J.;
"A human mitochondrial ferritin encoded by an intronless gene.";
J. Biol. Chem. 276:24437-24440(2001).
[3]
X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 61-242, FUNCTION, AND
MUTAGENESIS OF SER-204.
PubMed=15201052; DOI=10.1016/j.jmb.2004.04.036;
Langlois d'Estaintot B., Santambrogio P., Granier T., Gallois B.,
Chevalier J.M., Precigoux G., Levi S., Arosio P.;
"Crystal structure and biochemical properties of the human
mitochondrial ferritin and its mutant Ser144Ala.";
J. Mol. Biol. 340:277-293(2004).
-!- FUNCTION: Stores iron in a soluble, non-toxic, readily available
form. Important for iron homeostasis. Has ferroxidase activity.
Iron is taken up in the ferrous form and deposited as ferric
hydroxides after oxidation. {ECO:0000269|PubMed:11323407,
ECO:0000269|PubMed:15201052}.
-!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
-!- SUBUNIT: Homooligomer of 24 subunits. The functional molecule is
roughly spherical and contains a central cavity into which the
polymeric mineral iron core is deposited.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11323407}.
-!- TISSUE SPECIFICITY: Detected in testis and erythroleukemia.
Expression is very low or not detectable in brain, colon, heart,
kidney, liver, lung, muscle, placental, spleen and small
intestine. {ECO:0000269|PubMed:11323407}.
-!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Ferritin entry;
URL="https://en.wikipedia.org/wiki/Ferritin";
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EMBL; BC034419; AAH34419.1; -; mRNA.
CCDS; CCDS4128.1; -.
RefSeq; NP_803431.1; NM_177478.1.
UniGene; Hs.105324; -.
PDB; 1R03; X-ray; 1.70 A; A=61-242.
PDBsum; 1R03; -.
ProteinModelPortal; Q8N4E7; -.
SMR; Q8N4E7; -.
STRING; 9606.ENSP00000313691; -.
BioMuta; FTMT; -.
DMDM; 62900307; -.
PaxDb; Q8N4E7; -.
PeptideAtlas; Q8N4E7; -.
PRIDE; Q8N4E7; -.
DNASU; 94033; -.
Ensembl; ENST00000321339; ENSP00000313691; ENSG00000181867.
GeneID; 94033; -.
KEGG; hsa:94033; -.
UCSC; uc003kss.4; human.
CTD; 94033; -.
DisGeNET; 94033; -.
EuPathDB; HostDB:ENSG00000181867.2; -.
GeneCards; FTMT; -.
HGNC; HGNC:17345; FTMT.
MIM; 608847; gene.
neXtProt; NX_Q8N4E7; -.
OpenTargets; ENSG00000181867; -.
PharmGKB; PA134941146; -.
eggNOG; KOG2332; Eukaryota.
eggNOG; COG1528; LUCA.
GeneTree; ENSGT00760000119129; -.
HOGENOM; HOG000223383; -.
HOVERGEN; HBG000410; -.
InParanoid; Q8N4E7; -.
KO; K18495; -.
OMA; NFHEECE; -.
OrthoDB; EOG091G0J20; -.
PhylomeDB; Q8N4E7; -.
TreeFam; TF313885; -.
Reactome; R-HSA-917937; Iron uptake and transport.
EvolutionaryTrace; Q8N4E7; -.
GeneWiki; Mitochondrial_ferritin; -.
GenomeRNAi; 94033; -.
PRO; PR:Q8N4E7; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000181867; -.
CleanEx; HS_FTMT; -.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
GO; GO:0004322; F:ferroxidase activity; TAS:Reactome.
GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
GO; GO:0006879; P:cellular iron ion homeostasis; IDA:BHF-UCL.
GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central.
GO; GO:0006826; P:iron ion transport; IEA:InterPro.
GO; GO:1904234; P:positive regulation of aconitate hydratase activity; IGI:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0051349; P:positive regulation of lyase activity; IDA:BHF-UCL.
GO; GO:1904231; P:positive regulation of succinate dehydrogenase activity; IGI:BHF-UCL.
Gene3D; 1.20.1260.10; -; 1.
InterPro; IPR001519; Ferritin.
InterPro; IPR012347; Ferritin-like.
InterPro; IPR009040; Ferritin-like_diiron.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR014034; Ferritin_CS.
InterPro; IPR008331; Ferritin_DPS_dom.
PANTHER; PTHR11431; PTHR11431; 1.
Pfam; PF00210; Ferritin; 1.
SUPFAM; SSF47240; SSF47240; 1.
PROSITE; PS00204; FERRITIN_2; 1.
PROSITE; PS50905; FERRITIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Iron; Iron storage; Metal-binding;
Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
TRANSIT 1 49 Mitochondrion. {ECO:0000255}.
CHAIN 50 242 Ferritin, mitochondrial.
/FTId=PRO_0000008850.
DOMAIN 70 219 Ferritin-like diiron.
{ECO:0000255|PROSITE-ProRule:PRU00085}.
METAL 87 87 Iron 1.
METAL 122 122 Iron 1.
METAL 122 122 Iron 2.
METAL 125 125 Iron 1.
METAL 167 167 Iron 2.
METAL 201 201 Iron 2. {ECO:0000255|PROSITE-
ProRule:PRU00085}.
MUTAGEN 204 204 S->A: Increases ferroxidase activity and
iron binding.
{ECO:0000269|PubMed:15201052}.
HELIX 74 100 {ECO:0000244|PDB:1R03}.
TURN 104 106 {ECO:0000244|PDB:1R03}.
HELIX 109 136 {ECO:0000244|PDB:1R03}.
HELIX 156 183 {ECO:0000244|PDB:1R03}.
HELIX 187 196 {ECO:0000244|PDB:1R03}.
HELIX 198 218 {ECO:0000244|PDB:1R03}.
TURN 219 222 {ECO:0000244|PDB:1R03}.
HELIX 226 233 {ECO:0000244|PDB:1R03}.
SEQUENCE 242 AA; 27538 MW; 29E4B41616A74A3F CRC64;
MLSCFRLLSR HISPSLASLR PVRCCFALPL RWAPGRPLDP RQIAPRRPLA AAASSRDPTG
PAAGPSRVRQ NFHPDSEAAI NRQINLELYA SYVYLSMAYY FSRDDVALNN FSRYFLHQSR
EETEHAEKLM RLQNQRGGRI RLQDIKKPEQ DDWESGLHAM ECALLLEKNV NQSLLELHAL
ASDKGDPHLC DFLETYYLNE QVKSIKELGD HVHNLVKMGA PDAGLAEYLF DTHTLGNENK
QN


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