Mitochondrial ferritin

FTMT
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1R03
Identifiers
Aliases	FTMT, MTF, Mitochondrial ferritin, ferritin mitochondrial
External IDs	OMIM: 608847 MGI: 1914884 HomoloGene: 110661 GeneCards: FTMT
Gene location (Human)
Chr.	Chromosome 5 (human)[1]
End	121,852,833 bp[1]
Gene location (Mouse)
Chr.	Chromosome 18 (mouse)[2]
End	52,332,996 bp[2]
Gene ontology
Molecular function	• ferric iron binding; • metal ion binding; • oxidoreductase activity; • iron ion binding; • ferroxidase activity; • ferrous iron binding; • identical protein binding;
Cellular component	• cell nucleus; • mitochondrion; • mitochondrial matrix; • cytoplasm;
Biological process	• iron ion transport; • positive regulation of succinate dehydrogenase activity; • positive regulation of aconitate hydratase activity; • positive regulation of cell proliferation; • positive regulation of lyase activity; • oxidation-reduction process; • intracellular sequestering of iron ion; • cellular iron ion homeostasis;
	Sources:Amigo / QuickGO
Orthologs
	94033
	67634
	ENSG00000181867
	ENSMUSG00000024510
	Q8N4E7
	Q9D5H4
	NM_177478
	NM_026286
	NP_803431
	NP_080562
	Wikidata
View/Edit Human	View/Edit Mouse

Mitochondrial ferritin is a ferroxidase enzyme that in humans is encoded by the FTMT gene.[5]

It is classified as a metal-binding protein which is located within the mitochondria. After the protein is taken up by the mitochondria it can be processed into a mature protein and assemble functional ferritin shells.

Structure

Its structure was determined at 1.70 Å through the use of X-ray diffraction and contains 182 residues. It is 67% helical. The Ramachandran plot shows that the structure of mitochondrial ferritin is mainly alpha helical with a low prevalence of beta sheets.

References

GRCh38: Ensembl release 89: ENSG00000181867 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000024510 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Levi S, Corsi B, Bosisio M, Invernizzi R, Volz A, Sanford D, Arosio P, Drysdale J (July 2001). "A human mitochondrial ferritin encoded by an intronless gene". J. Biol. Chem. 276 (27): 24437–40. doi:10.1074/jbc.C100141200. PMID 11323407.

Langlois d'Estaintot B, Santambrogio P, Granier T, et al. (2004). "Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala". J. Mol. Biol. 340 (2): 277–93. doi:10.1016/j.jmb.2004.04.036. PMID 15201052.
Zanella I, Derosas M, Corrado M, et al. (2008). "The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin" (PDF). Biochim. Biophys. Acta. 1782 (2): 90–8. doi:10.1016/j.bbadis.2007.11.006. PMID 18160053.
Wilkinson J, Di X, Schönig K, et al. (2006). "Tissue-specific expression of ferritin H regulates cellular iron homoeostasis in vivo". Biochem. J. 395 (3): 501–7. doi:10.1042/BJ20060063. PMC 1462685. PMID 16448386.
Iwasaki K, Mackenzie EL, Hailemariam K, et al. (2006). "Hemin-mediated regulation of an antioxidant-responsive element of the human ferritin H gene and role of Ref-1 during erythroid differentiation of K562 cells". Mol. Cell. Biol. 26 (7): 2845–56. doi:10.1128/MCB.26.7.2845-2856.2006. PMC 1430308. PMID 16537925.
Hasan MR, Tosha T, Theil EC (2008). "Ferritin contains less iron (59Fe) in cells when the protein pores are unfolded by mutation". J. Biol. Chem. 283 (46): 31394–400. doi:10.1074/jbc.M806025200. PMC 2581568. PMID 18805796.
Cazzola M, Invernizzi R, Bergamaschi G, et al. (2003). "Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia". Blood. 101 (5): 1996–2000. doi:10.1182/blood-2002-07-2006. PMID 12406866.
Faniello MC, Fregola A, Nisticò A, et al. (2006). "Detection and functional analysis of an SNP in the promoter of the human ferritin H gene that modulates the gene expression". Gene. 377: 1–5. doi:10.1016/j.gene.2006.02.034. PMID 16797877.
Iwasaki K, Hailemariam K, Tsuji Y (2007). "PIAS3 interacts with ATF1 and regulates the human ferritin H gene through an antioxidant-responsive element". J. Biol. Chem. 282 (31): 22335–43. doi:10.1074/jbc.M701477200. PMC 2409283. PMID 17565989.
MacKenzie EL, Tsuji Y (2008). "Elevated intracellular calcium increases ferritin H expression through an NFAT-independent post-transcriptional mechanism involving mRNA stabilization". Biochem. J. 411 (1): 107–13. doi:10.1042/BJ20071544. PMC 2702759. PMID 18076382.
Drysdale J, Arosio P, Invernizzi R, et al. (2002). "Mitochondrial ferritin: a new player in iron metabolism". Blood Cells Mol. Dis. 29 (3): 376–83. doi:10.1006/bcmd.2002.0577. PMID 12547228.
Fisher J, Devraj K, Ingram J, et al. (2007). "Ferritin: a novel mechanism for delivery of iron to the brain and other organs". Am. J. Physiol., Cell Physiol. 293 (2): C641–9. doi:10.1152/ajpcell.00599.2006. PMID 17459943.
Campanella A, Rovelli E, Santambrogio P, et al. (2009). "Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: hypothesis for a protective role in Friedreich ataxia". Hum. Mol. Genet. 18 (1): 1–11. doi:10.1093/hmg/ddn308. PMC 3298861. PMID 18815198.
Bou-Abdallah F, Biasiotto G, Arosio P, Chasteen ND (2004). "The putative "nucleation site" in human H-chain ferritin is not required for mineralization of the iron core". Biochemistry. 43 (14): 4332–7. doi:10.1021/bi0498813. PMID 15065877.
Binning RC, Bacelo DE (2009). "Computational modeling of the dizinc-ferroxidase complex of human H ferritin: direct comparison of the density functional theory calculated and experimental structures". J. Biol. Inorg. Chem. 14 (8): 1199–208. doi:10.1007/s00775-009-0563-z. PMID 19585161. S2CID 23855417.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
MacKenzie EL, Ray PD, Tsuji Y (2008). "Role and regulation of ferritin H in rotenone-mediated mitochondrial oxidative stress". Free Radic. Biol. Med. 44 (9): 1762–71. doi:10.1016/j.freeradbiomed.2008.01.031. PMC 2682214. PMID 18325346.
Bou-Abdallah F, Santambrogio P, Levi S, et al. (2005). "Unique iron binding and oxidation properties of human mitochondrial ferritin: a comparative analysis with Human H-chain ferritin". J. Mol. Biol. 347 (3): 543–54. doi:10.1016/j.jmb.2005.01.007. PMID 15755449.
Faniello MC, Di Sanzo M, Quaresima B, et al. (2008). "p53-mediated downregulation of H ferritin promoter transcriptional efficiency via NF-Y". Int. J. Biochem. Cell Biol. 40 (10): 2110–9. doi:10.1016/j.biocel.2008.02.010. hdl:10447/35800. PMID 18372207.
Snyder AM, Wang X, Patton SM, et al. (2009). "Mitochondrial ferritin in the substantia nigra in restless legs syndrome". J. Neuropathol. Exp. Neurol. 68 (11): 1193–9. doi:10.1097/NEN.0b013e3181bdc44f. PMC 3024883. PMID 19816198.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000181867 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000024510 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid11323407-5] Levi S, Corsi B, Bosisio M, Invernizzi R, Volz A, Sanford D, Arosio P, Drysdale J (July 2001). "A human mitochondrial ferritin encoded by an intronless gene". J. Biol. Chem. 276 (27): 24437–40. doi:10.1074/jbc.C100141200. PMID 11323407.

Other oxidoreductases (EC 1.15-1.21)
1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3
1.16: Oxidizing metal ions	Ceruloplasmin (Methionine synthase) reductase
1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase
1.18: Acting on iron-sulfur proteins as donors	Nitrogenase
1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)
1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5
1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Mitochondrial ferritin

Structure

References

Further reading