ATOX1

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Antioxidant 1 copper chaperone
Protein ATOX1 PDB 1fe0.png
PDB rendering based on 1fe0.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ATOX1 ; ATX1; HAH1
External IDs OMIM602270 MGI1333855 HomoloGene2984 GeneCards: ATOX1 Gene
EC number 6.2.1.2
RNA expression pattern
PBB GE ATOX1 203454 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 475 11927
Ensembl ENSG00000177556 ENSMUSG00000018585
UniProt O00244 O08997
RefSeq (mRNA) NM_004045 NM_009720
RefSeq (protein) NP_004036 NP_033850
Location (UCSC) Chr 5:
151.12 – 151.15 Mb
Chr 11:
55.45 – 55.46 Mb
PubMed search [1] [2]

Copper transport protein ATOX1 is a protein that in humans is encoded by the ATOX1 gene.[1][2]

Function[edit]

This gene encodes a copper chaperone that plays a role in copper homeostasis by binding and transporting cytosolic copper to ATPase proteins in the trans-Golgi network for later incorporation to the ceruloplasmin. This protein also functions as an antioxidant against superoxide and hydrogen peroxide, and therefore, may play a significant role in cancer carcinogenesis. Because of its cytogenetic location, this gene represents a candidate gene for 5q-syndrome.[2]

In melanocytic cells ATOX1 gene expression may be regulated by MITF.[3]

Interactions[edit]

ATOX1 has been shown to interact with Wilson disease protein[4][5] and ATP7A.[4]

References[edit]

  1. ^ Klomp LW, Lin SJ, Yuan DS, Klausner RD, Culotta VC, Gitlin JD (May 1997). "Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis". J Biol Chem 272 (14): 9221–6. doi:10.1074/jbc.272.14.9221. PMID 9083055. 
  2. ^ a b "Entrez Gene: ATOX1 ATX1 antioxidant protein 1 homolog (yeast)". 
  3. ^ Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971. 
  4. ^ a b Larin D, Mekios C, Das K, Ross B, Yang AS, Gilliam TC (October 1999). "Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone, HAH1p". J. Biol. Chem. 274 (40): 28497–504. doi:10.1074/jbc.274.40.28497. PMID 10497213. 
  5. ^ Hamza I, Schaefer M, Klomp LW, Gitlin JD (November 1999). "Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis". Proc. Natl. Acad. Sci. U.S.A. 96 (23): 13363–8. doi:10.1073/pnas.96.23.13363. PMC 23953. PMID 10557326. 


Further reading[edit]

  • Hung IH, Casareno RL, Labesse G, Mathews FS, Gitlin JD (1998). "HAH1 is a copper-binding protein with distinct amino acid residues mediating copper homeostasis and antioxidant defense.". J. Biol. Chem. 273 (3): 1749–54. doi:10.1074/jbc.273.3.1749. PMID 9430722. 
  • Larin D, Mekios C, Das K, Ross B, Yang AS, Gilliam TC (1999). "Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone, HAH1p.". J. Biol. Chem. 274 (40): 28497–504. doi:10.1074/jbc.274.40.28497. PMID 10497213. 
  • Hamza I, Schaefer M, Klomp LW, Gitlin JD (1999). "Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis.". Proc. Natl. Acad. Sci. U.S.A. 96 (23): 13363–8. doi:10.1073/pnas.96.23.13363. PMC 23953. PMID 10557326. 
  • Wernimont AK, Huffman DL, Lamb AL, O'Halloran TV, Rosenzweig AC (2000). "Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins.". Nat. Struct. Biol. 7 (9): 766–71. doi:10.1038/78999. PMID 10966647. 
  • Boultwood J, Strickson AJ, Jabs EW, Cheng JF, Fidler C, Wainscoat JS (2000). "Physical mapping of the human ATX1 homologue (HAH1) to the critical region of the 5q- syndrome within 5q32, and immediately adjacent to the SPARC gene.". Hum. Genet. 106 (1): 127–9. doi:10.1007/s004390051020. PMID 10982193. 
  • Walker JM, Tsivkovskii R, Lutsenko S (2002). "Metallochaperone Atox1 transfers copper to the NH2-terminal domain of the Wilson's disease protein and regulates its catalytic activity.". J. Biol. Chem. 277 (31): 27953–9. doi:10.1074/jbc.M203845200. PMID 12029094. 
  • Moore SD, Helmle KE, Prat LM, Cox DW (2003). "Tissue localization of the copper chaperone ATOX1 and its potential role in disease.". Mamm. Genome 13 (10): 563–8. doi:10.1007/s00335-002-2172-9. PMID 12420134. 
  • Liu PC, Koeller DM, Kaler SG (2004). "Genomic organization of ATOX1, a human copper chaperone.". BMC Genet. 4: 4. doi:10.1186/1471-2156-4-4. PMC 150598. PMID 12594858. 
  • Strausak D, Howie MK, Firth SD, Schlicksupp A, Pipkorn R, Multhaup G et al. (2003). "Kinetic analysis of the interaction of the copper chaperone Atox1 with the metal binding sites of the Menkes protein.". J. Biol. Chem. 278 (23): 20821–7. doi:10.1074/jbc.M212437200. PMID 12679332. 
  • Ralle M, Lutsenko S, Blackburn NJ (2003). "X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines.". J. Biol. Chem. 278 (25): 23163–70. doi:10.1074/jbc.M303474200. PMID 12686548. 
  • Lutsenko S, Tsivkovskii R, Walker JM (2003). "Functional properties of the human copper-transporting ATPase ATP7B (the Wilson's disease protein) and regulation by metallochaperone Atox1.". Ann. N. Y. Acad. Sci. 986: 204–11. doi:10.1111/j.1749-6632.2003.tb07161.x. PMID 12763797. 
  • Wernimont AK, Yatsunyk LA, Rosenzweig AC (2004). "Binding of copper(I) by the Wilson disease protein and its copper chaperone.". J. Biol. Chem. 279 (13): 12269–76. doi:10.1074/jbc.M311213200. PMID 14709553. 
  • Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation.". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. 
  • Anastassopoulou I, Banci L, Bertini I, Cantini F, Katsari E, Rosato A (2004). "Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1.". Biochemistry 43 (41): 13046–53. doi:10.1021/bi0487591. PMID 15476398. 
  • Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A (2005). "An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.". FEBS J. 272 (3): 865–71. doi:10.1111/j.1742-4658.2004.04526.x. PMID 15670166. 
  • Jeney V, Itoh S, Wendt M, Gradek Q, Ushio-Fukai M, Harrison DG et al. (2005). "Role of antioxidant-1 in extracellular superoxide dismutase function and expression.". Circ. Res. 96 (7): 723–9. doi:10.1161/01.RES.0000162001.57896.66. PMID 15761197.