FTMT_HUMAN
ID FTMT_HUMAN Reviewed; 242 AA.
AC Q8N4E7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ferritin, mitochondrial {ECO:0000305};
DE EC=1.16.3.1 {ECO:0000269|PubMed:15201052};
DE Flags: Precursor;
GN Name=FTMT {ECO:0000312|HGNC:HGNC:17345};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11323407; DOI=10.1074/jbc.c100141200;
RA Levi S., Corsi B., Bosisio M., Invernizzi R., Volz A., Sanford D.,
RA Arosio P., Drysdale J.;
RT "A human mitochondrial ferritin encoded by an intronless gene.";
RL J. Biol. Chem. 276:24437-24440(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 61-242, FUNCTION, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF SER-204, AND SUBUNIT.
RX PubMed=15201052; DOI=10.1016/j.jmb.2004.04.036;
RA Langlois d'Estaintot B., Santambrogio P., Granier T., Gallois B.,
RA Chevalier J.M., Precigoux G., Levi S., Arosio P.;
RT "Crystal structure and biochemical properties of the human mitochondrial
RT ferritin and its mutant Ser144Ala.";
RL J. Mol. Biol. 340:277-293(2004).
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 (PubMed:11323407, PubMed:15201052). Important for iron homeostasis
CC (PubMed:11323407, PubMed:15201052). Iron is taken up in the ferrous
CC form and deposited as ferric hydroxides after oxidation
CC (PubMed:11323407, PubMed:15201052). {ECO:0000269|PubMed:11323407,
CC ECO:0000269|PubMed:15201052}.
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:0000269|PubMed:11323407, ECO:0000269|PubMed:15201052};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11149;
CC Evidence={ECO:0000305|PubMed:11323407, ECO:0000305|PubMed:15201052};
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.
CC {ECO:0000269|PubMed:15201052}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11323407}.
CC -!- TISSUE SPECIFICITY: Detected in testis and erythroleukemia. Expression
CC is very low or not detectable in brain, colon, heart, kidney, liver,
CC lung, muscle, placental, spleen and small intestine.
CC {ECO:0000269|PubMed:11323407}.
CC -!- SIMILARITY: Belongs to the ferritin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ferritin entry;
CC URL="https://en.wikipedia.org/wiki/Ferritin";
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DR EMBL; BC034419; AAH34419.1; -; mRNA.
DR CCDS; CCDS4128.1; -.
DR RefSeq; NP_803431.1; NM_177478.1.
DR PDB; 1R03; X-ray; 1.70 A; A=61-242.
DR PDB; 5Z8J; X-ray; 2.30 A; A=61-242.
DR PDB; 5Z8S; X-ray; 1.97 A; A=61-242.
DR PDB; 5Z8U; X-ray; 1.90 A; A/B=61-242.
DR PDB; 5Z91; X-ray; 3.00 A; A=61-242.
DR PDB; 7O63; X-ray; 1.16 A; A=61-242.
DR PDB; 7O64; X-ray; 1.96 A; A=61-242.
DR PDB; 7O65; X-ray; 1.70 A; A=61-242.
DR PDB; 7O66; X-ray; 1.60 A; A=61-242.
DR PDB; 7O67; X-ray; 1.86 A; A=61-242.
DR PDB; 7O68; X-ray; 1.68 A; A=61-242.
DR PDB; 7O69; X-ray; 1.35 A; A=61-242.
DR PDB; 7O6A; X-ray; 1.40 A; A=61-242.
DR PDB; 7O6C; X-ray; 1.20 A; A=61-242.
DR PDB; 7O6D; X-ray; 1.47 A; A=61-242.
DR PDB; 7OWY; X-ray; 1.55 A; A=61-242.
DR PDBsum; 1R03; -.
DR PDBsum; 5Z8J; -.
DR PDBsum; 5Z8S; -.
DR PDBsum; 5Z8U; -.
DR PDBsum; 5Z91; -.
DR PDBsum; 7O63; -.
DR PDBsum; 7O64; -.
DR PDBsum; 7O65; -.
DR PDBsum; 7O66; -.
DR PDBsum; 7O67; -.
DR PDBsum; 7O68; -.
DR PDBsum; 7O69; -.
DR PDBsum; 7O6A; -.
DR PDBsum; 7O6C; -.
DR PDBsum; 7O6D; -.
DR PDBsum; 7OWY; -.
DR AlphaFoldDB; Q8N4E7; -.
DR SMR; Q8N4E7; -.
DR BioGRID; 125101; 1.
DR STRING; 9606.ENSP00000313691; -.
DR BioMuta; FTMT; -.
DR DMDM; 62900307; -.
DR jPOST; Q8N4E7; -.
DR MassIVE; Q8N4E7; -.
DR PaxDb; Q8N4E7; -.
DR PeptideAtlas; Q8N4E7; -.
DR PRIDE; Q8N4E7; -.
DR ProteomicsDB; 71925; -.
DR Antibodypedia; 52782; 67 antibodies from 19 providers.
DR DNASU; 94033; -.
DR Ensembl; ENST00000321339.3; ENSP00000313691.1; ENSG00000181867.3.
DR GeneID; 94033; -.
DR KEGG; hsa:94033; -.
DR MANE-Select; ENST00000321339.3; ENSP00000313691.1; NM_177478.2; NP_803431.1.
DR UCSC; uc003kss.4; human.
DR CTD; 94033; -.
DR DisGeNET; 94033; -.
DR GeneCards; FTMT; -.
DR HGNC; HGNC:17345; FTMT.
DR HPA; ENSG00000181867; Tissue enriched (testis).
DR MIM; 608847; gene.
DR neXtProt; NX_Q8N4E7; -.
DR OpenTargets; ENSG00000181867; -.
DR PharmGKB; PA134941146; -.
DR VEuPathDB; HostDB:ENSG00000181867; -.
DR eggNOG; KOG2332; Eukaryota.
DR GeneTree; ENSGT00940000163120; -.
DR HOGENOM; CLU_065681_4_0_1; -.
DR InParanoid; Q8N4E7; -.
DR OMA; QNYHSEV; -.
DR OrthoDB; 1249457at2759; -.
DR PhylomeDB; Q8N4E7; -.
DR TreeFam; TF313885; -.
DR PathwayCommons; Q8N4E7; -.
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR SignaLink; Q8N4E7; -.
DR BioGRID-ORCS; 94033; 21 hits in 1073 CRISPR screens.
DR EvolutionaryTrace; Q8N4E7; -.
DR GeneWiki; Mitochondrial_ferritin; -.
DR GenomeRNAi; 94033; -.
DR Pharos; Q8N4E7; Tbio.
DR PRO; PR:Q8N4E7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8N4E7; protein.
DR Bgee; ENSG00000181867; Expressed in left testis and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA: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; IDA:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IDA: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 GO; GO:1904234; P:positive regulation of aconitate hydratase activity; IGI:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0051349; P:positive regulation of lyase activity; IDA:BHF-UCL.
DR GO; GO:1904231; P:positive regulation of succinate dehydrogenase activity; IGI:BHF-UCL.
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; PS00204; FERRITIN_2; 1.
DR PROSITE; PS50905; FERRITIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Iron; Iron storage; Metal-binding; Mitochondrion;
KW Oxidoreductase; 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_0000008850"
FT DOMAIN 70..219
FT /note="Ferritin-like diiron"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00085"
FT REGION 47..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15201052,
FT ECO:0007744|PDB:1R03"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15201052,
FT ECO:0007744|PDB:1R03"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15201052,
FT ECO:0007744|PDB:1R03"
FT BINDING 125
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15201052,
FT ECO:0007744|PDB:1R03"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15201052,
FT ECO:0007744|PDB:1R03"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15201052,
FT ECO:0007744|PDB:1R03"
FT MUTAGEN 204
FT /note="S->A: Increases ferroxidase activity and iron
FT binding."
FT /evidence="ECO:0000269|PubMed:15201052"
FT HELIX 74..100
FT /evidence="ECO:0007829|PDB:7O63"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:7O63"
FT HELIX 109..136
FT /evidence="ECO:0007829|PDB:7O63"
FT HELIX 156..183
FT /evidence="ECO:0007829|PDB:7O63"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:7O63"
FT HELIX 198..218
FT /evidence="ECO:0007829|PDB:7O63"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:7O63"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:7O63"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:7O63"
SQ 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
