ミトコンドリアフェリチン

FTMT
PDBに登録されている構造
PDBオルソログ検索: RCSB PDBe PDBj
PDBのIDコード一覧

1R03

識別子
記号FTMT, MTF, Mitochondrial ferritin, ferritin mitochondrial
外部IDOMIM: 608847 MGI: 1914884 HomoloGene: 110661 GeneCards: FTMT
遺伝子の位置 (ヒト)
5番染色体 (ヒト)
染色体5番染色体 (ヒト)[1]
5番染色体 (ヒト)
FTMT遺伝子の位置
FTMT遺伝子の位置
バンドデータ無し開始点121,851,882 bp[1]
終点121,852,833 bp[1]
遺伝子の位置 (マウス)
18番染色体 (マウス)
染色体18番染色体 (マウス)[2]
18番染色体 (マウス)
FTMT遺伝子の位置
FTMT遺伝子の位置
バンドデータ無し開始点52,464,621 bp[2]
終点52,466,068 bp[2]
遺伝子オントロジー
分子機能• ferric iron binding
• 金属イオン結合
• 酸化還元酵素活性
• iron ion binding
• ferroxidase activity
• ferrous iron binding
• identical protein binding
細胞の構成要素• 細胞核
• ミトコンドリア
• ミトコンドリアマトリックス
• 細胞質
生物学的プロセス• iron ion transport
• positive regulation of succinate dehydrogenase activity
• positive regulation of aconitate hydratase activity
• positive regulation of cell population proliferation
• positive regulation of lyase activity
• intracellular sequestering of iron ion
• cellular iron ion homeostasis
出典:Amigo / QuickGO
オルソログ
種ヒトマウス
Entrez

94033

67634

Ensembl

ENSG00000181867

ENSMUSG00000024510

UniProt

Q8N4E7

Q9D5H4

RefSeq
(mRNA)

NM_177478

NM_026286

RefSeq
(タンパク質)

NP_803431

NP_080562

場所
(UCSC)		Chr 5: 121.85 – 121.85 MbChr 5: 52.46 – 52.47 Mb
PubMed検索[3][4]
ウィキデータ
閲覧/編集 ヒト閲覧/編集 マウス

ミトコンドリアフェリチン（Mitochondrial ferritin）とはフェロキシダーゼの一種である。ヒトにおいてはFTMT 遺伝子にコードされている[5]。

ミトコンドリアに存在する金属結合性タンパク質である。ミトコンドリアフェリチンはタンパク質前駆体であり、ミトコンドリアに取り込まれた際にプレセシングされて成熟タンパク質となる。そして、フェリチンとなる。

構造

182個の残基から成る。主にαヘリックスから成り、βシートは少ない。構造の67%はヘリックスである[6]。

脚注

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000181867 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024510 - Ensembl, May 2017
  3. ^ Human PubMed Reference:
  4. ^ Mouse PubMed Reference:
  5. ^ “A human mitochondrial ferritin encoded by an intronless gene”. J. Biol. Chem. 276 (27): 24437–40. (July 2001). doi:10.1074/jbc.C100141200. PMID 11323407. 
  6. ^ Langlois d'Estaintot, B., Santambrogio, P., Granier, T., Gallois, B., Chevallier, J.M., Precigoux, G., Levi, S., Arosio, P. (2 July 2004). “Crystal Structure and Biochemical Properties of the Human Mitochondrial Ferritin and its Mutant Ser144Ala”. Journal of Molecular Biology 340 (2): 277-293. doi:10.1016/j.jmb.2004.04.036. PMID 15201052. http://www.rcsb.org/pdb/explore/explore.do?structureId=1R03. 

参考文献

Further reading

  • “Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala.”. J. Mol. Biol. 340 (2): 277–93. (2004). doi:10.1016/j.jmb.2004.04.036. PMID 15201052. 
  • “The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin.”. Biochim. Biophys. Acta 1782 (2): 90–8. (2008). doi:10.1016/j.bbadis.2007.11.006. PMID 18160053. 
  • “Tissue-specific expression of ferritin H regulates cellular iron homoeostasis in vivo.”. Biochem. J. 395 (3): 501–7. (2006). doi:10.1042/BJ20060063. PMC 1462685. PMID 16448386. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1462685/. 
  • “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. (2006). doi:10.1128/MCB.26.7.2845-2856.2006. PMC 1430308. PMID 16537925. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1430308/. 
  • “Ferritin contains less iron (59Fe) in cells when the protein pores are unfolded by mutation.”. J. Biol. Chem. 283 (46): 31394–400. (2008). doi:10.1074/jbc.M806025200. PMC 2581568. PMID 18805796. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2581568/. 
  • “Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia.”. Blood 101 (5): 1996–2000. (2003). doi:10.1182/blood-2002-07-2006. PMID 12406866. 
  • “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. (2006). doi:10.1016/j.gene.2006.02.034. PMID 16797877. 
  • “PIAS3 interacts with ATF1 and regulates the human ferritin H gene through an antioxidant-responsive element.”. J. Biol. Chem. 282 (31): 22335–43. (2007). doi:10.1074/jbc.M701477200. PMC 2409283. PMID 17565989. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2409283/. 
  • “Elevated intracellular calcium increases ferritin H expression through an NFAT-independent post-transcriptional mechanism involving mRNA stabilization.”. Biochem. J. 411 (1): 107–13. (2008). doi:10.1042/BJ20071544. PMC 2702759. PMID 18076382. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2702759/. 
  • “Mitochondrial ferritin: a new player in iron metabolism.”. Blood Cells Mol. Dis. 29 (3): 376–83. (2002). doi:10.1006/bcmd.2002.0577. PMID 12547228. 
  • “Ferritin: a novel mechanism for delivery of iron to the brain and other organs.”. Am. J. Physiol., Cell Physiol. 293 (2): C641–9. (2007). doi:10.1152/ajpcell.00599.2006. PMID 17459943. 
  • “Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: hypothesis for a protective role in Friedreich ataxia.”. Hum. Mol. Genet. 18 (1): 1–11. (2009). doi:10.1093/hmg/ddn308. PMC 3298861. PMID 18815198. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3298861/. 
  • “The putative "nucleation site" in human H-chain ferritin is not required for mineralization of the iron core.”. Biochemistry 43 (14): 4332–7. (2004). doi:10.1021/bi0498813. PMID 15065877. 
  • “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. (2009). doi:10.1007/s00775-009-0563-z. PMID 19585161. 
  • “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”. Genome Res. 14 (10B): 2121–7. (2004). doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC528928/. 
  • “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. (2002). doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241/. 
  • “Role and regulation of ferritin H in rotenone-mediated mitochondrial oxidative stress.”. Free Radic. Biol. Med. 44 (9): 1762–71. (2008). doi:10.1016/j.freeradbiomed.2008.01.031. PMC 2682214. PMID 18325346. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2682214/. 
  • “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. (2005). doi:10.1016/j.jmb.2005.01.007. PMID 15755449. 
  • “p53-mediated downregulation of H ferritin promoter transcriptional efficiency via NF-Y.”. Int. J. Biochem. Cell Biol. 40 (10): 2110–9. (2008). doi:10.1016/j.biocel.2008.02.010. PMID 18372207. 
  • “Mitochondrial ferritin in the substantia nigra in restless legs syndrome.”. J. Neuropathol. Exp. Neurol. 68 (11): 1193–9. (2009). doi:10.1097/NEN.0b013e3181bdc44f. PMC 3024883. PMID 19816198. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3024883/.