ACO1

ACO1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesACO1, ACONS, HEL60, IREB1, IREBP, IREBP1, IRP1, aconitase 1
External IDsMGI: 87879 HomoloGene: 1657 GeneCards: ACO1
Gene location (Human)
Chr.Chromosome 9 (human)[1]
Band9p21.1Start32,384,603 bp[1]
End32,454,769 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

48

11428

Ensembl

ENSG00000122729

ENSMUSG00000028405

UniProt

P21399

P28271

RefSeq (mRNA)

NM_001278352
NM_002197
NM_001362840

NM_007386

RefSeq (protein)

NP_001265281
NP_002188
NP_001349769

NP_031412

Location (UCSC)Chr 9: 32.38 – 32.45 MbChr 4: 40.14 – 40.2 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Aconitase 1, soluble is a protein that in humans is encoded by the ACO1 gene.[5]

Function

The protein encoded by this gene is a bifunctional, cytosolic protein that functions as an essential enzyme in the TCA cycle and interacts with mRNA to control the levels of iron inside cells. When cellular iron levels are high, this protein binds to a 4Fe-4S cluster and functions as an aconitase. Aconitases are iron-sulfur proteins that function to catalyze the conversion of citrate to isocitrate. When cellular iron levels are low, the protein binds to iron-responsive elements (IREs), which are stem-loop structures found in the 5' UTR of ferritin mRNA, and in the 3' UTR of transferrin receptor mRNA. When the protein binds to IRE, it results in repression of translation of ferritin mRNA, and inhibition of degradation of the otherwise rapidly degraded transferrin receptor mRNA. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Alternative splicing results in multiple transcript variants.[5]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000122729 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028405 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. 1 2 "Entrez Gene: Aconitase 1, soluble".

Further reading

  • Wang W, Di X, D'Agostino RB, Torti SV, Torti FM (Aug 2007). "Excess capacity of the iron regulatory protein system". The Journal of Biological Chemistry. 282 (34): 24650–9. doi:10.1074/jbc.M703167200. PMID 17604281.
  • Martelli A, Salin B, Dycke C, Louwagie M, Andrieu JP, Richaud P, Moulis JM (Feb 2007). "Folding and turnover of human iron regulatory protein 1 depend on its subcellular localization". The FEBS Journal. 274 (4): 1083–92. doi:10.1111/j.1742-4658.2007.05657.x. PMID 17244191.
  • Hu J, Connor JR (Aug 1996). "Demonstration and characterization of the iron regulatory protein in human brain". Journal of Neurochemistry. 67 (2): 838–44. doi:10.1046/j.1471-4159.1996.67020838.x. PMID 8764614.
  • Popovic Z, Templeton DM (Jun 2007). "Inhibition of an iron-responsive element/iron regulatory protein-1 complex by ATP binding and hydrolysis". The FEBS Journal. 274 (12): 3108–19. doi:10.1111/j.1742-4658.2007.05843.x. PMID 17521334.
  • Wang J, Fillebeen C, Chen G, Biederbick A, Lill R, Pantopoulos K (Apr 2007). "Iron-dependent degradation of apo-IRP1 by the ubiquitin-proteasome pathway". Molecular and Cellular Biology. 27 (7): 2423–30. doi:10.1128/MCB.01111-06. PMC 1899896. PMID 17242182.
  • Liu CY, Liu YF, Zeng L, Zhang SG, Xu H (Apr 2007). "[The expression of TfR1 mRNA and IRP1 mRNA in the placenta from different maternal iron status]". Zhonghua Xue Ye Xue Za Zhi = Zhonghua Xueyexue Zazhi. 28 (4): 255–8. PMID 17877204.
  • Zimmer M, Lamb J, Ebert BL, Lynch M, Neil C, Schmidt E, Golub TR, Iliopoulos O (Apr 2010). "The connectivity map links iron regulatory protein-1-mediated inhibition of hypoxia-inducible factor-2a translation to the anti-inflammatory 15-deoxy-delta12,14-prostaglandin J2". Cancer Research. 70 (8): 3071–9. doi:10.1158/0008-5472.CAN-09-2877. PMC 2861799. PMID 20354189.
  • Gu JM, Lim SO, Oh SJ, Yoon SM, Seong JK, Jung G (May 2008). "HBx modulates iron regulatory protein 1-mediated iron metabolism via reactive oxygen species". Virus Research. 133 (2): 167–77. doi:10.1016/j.virusres.2007.12.014. PMID 18262302.
  • Popovic Z, Templeton DM (Oct 2004). "Iron accumulation and iron-regulatory protein activity in human hepatoma (HepG2) cells". Molecular and Cellular Biochemistry. 265 (1–2): 37–45. doi:10.1023/b:mcbi.0000044313.19574.c6. PMID 15543932.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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