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ACO1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2B3X, 2B3Y

Identifiers

Aliases

ACO1, ACONS, HEL60, IREB1, IREBP, IREBP1, IRP1, aconitase 1

External IDs

OMIM: 100880 MGI: 87879 HomoloGene: 1657 GeneCards: ACO1

Gene location (Human)

Chr.	Chromosome 9 (human)^[1]

Band	9p21.1	Start	32,384,603 bp^[1]
Band	9p21.1	End	32,454,769 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 4 (mouse)^[2]

Band	4 A5\|4 20.24 cM	Start	40,143,081 bp^[2]
Band	4 A5\|4 20.24 cM	End	40,198,338 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

right lobe of liver

stromal cell of endometrium

right adrenal gland

adipose tissue

left adrenal gland

kidney tubule

subcutaneous adipose tissue

duodenum

jejunal mucosa

pericardium

Top expressed in

external carotid artery

internal carotid artery

dermis

carotid body

submandibular gland

proximal tubule

vas deferens

molar

intercostal muscle

kidney

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	iron-sulfur cluster binding metal ion binding protein binding lyase activity RNA binding aconitate hydratase activity iron-responsive element binding 3 iron, 4 sulfur cluster binding 4 iron, 4 sulfur cluster binding
Cellular component	Golgi apparatus endoplasmic reticulum mitochondrion extracellular exosome cytoplasm cytosol
Biological process	response to iron(II) ion tricarboxylic acid cycle post-embryonic development regulation of gene expression intestinal absorption metabolism regulation of translation citrate metabolic process cellular iron ion homeostasis
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

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 Mb

Chr 4: 40.14 – 40.2 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

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

YouTube Encyclopedic

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Transcription

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000122729 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028405 – 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.
^ ^a ^b "Entrez Gene: Aconitase 1, soluble".

External links

Human ACO1 genome location and ACO1 gene details page in the UCSC Genome Browser.

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. S2CID 8412580.
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. S2CID 35872879.
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. S2CID 22629034.
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. S2CID 19363206.

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

v t e Carbon–oxygen lyases (EC 4.2) (primarily dehydratases)
4.2.1: Hydro-Lyases	Carbonic anhydrase Fumarase Aconitase Enolase Alpha Enolase 2 Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase Methylglutaconyl-CoA hydratase Tryptophan synthase Cystathionine beta synthase Porphobilinogen synthase 3-Isopropylmalate dehydratase Urocanase Uroporphyrinogen III synthase Nitrile hydratase
4.2.2: Acting on polysaccharides	Hyaluronate lyase Pectin lyase
4.2.3: Acting on phosphates	Threonine synthase
4.2.99: Other	Carboxymethyloxysuccinate lyase Hydroperoxide lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme 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)

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This page was last edited on 12 July 2022, at 09:50