# APOBEC1

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Protein-coding gene in the species Homo sapiens

APOBEC1 Identifiers Aliases APOBEC1, APOBEC-1, BEDP, CDAR1, HEPR, apolipoprotein B mRNA editing enzyme catalytic subunit 1 External IDs OMIM: 600130; MGI: 103298; HomoloGene: 1243; GeneCards: APOBEC1; OMA:APOBEC1 - orthologs Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12p13.31 Start 7,649,400 bp[1] End 7,665,908 bp[1] Gene location (Mouse) Chr. Chromosome 6 (mouse)[2] Band 6 F1|6 57.68 cM Start 122,554,751 bp[2] End 122,579,403 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa duodenum mucosa of ileum testicle mucosa of transverse colon gastric mucosa islet of Langerhans rectum gallbladder muscle tissue Top expressed in granulocyte stroma of bone marrow pyloric antrum Ileal epithelium left colon spleen jejunum duodenum blood mucous cell of stomach More reference expression data BioGPS More reference expression data Gene ontology Molecular function enzyme activator activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines protein binding mRNA binding cytidine deaminase activity RNA binding catalytic activity zinc ion binding hydrolase activity cytosine deaminase activity metal ion binding protein domain specific binding ribonucleoprotein complex binding mRNA 3'-UTR AU-rich region binding Cellular component nucleus nucleoplasm cytoplasm Biological process DNA cytosine deamination cellular response to insulin stimulus response to osmotic stress mRNA processing RNA processing response to calcium ion response to ethanol regulation of cell population proliferation response to zinc ion defense response to virus cytidine to uridine editing response to gamma radiation mRNA stabilization DNA demethylation lipoprotein metabolic process lipoprotein transport positive regulation of catalytic activity lipoprotein biosynthetic process lipid metabolism negative regulation of DNA methylation-dependent heterochromatin assembly positive regulation of mRNA modification cytidine deamination mRNA modification triglyceride metabolic process negative regulation of triglyceride metabolic process Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 339 11810 Ensembl ENSG00000111701 ENSMUSG00000040613 UniProt P41238 P51908 RefSeq (mRNA) NM_005889 NM_001304566 NM_001644 NM_001134391 NM_031159 RefSeq (protein) NP_001291495 NP_001635 NP_005880 NP_001127863 NP_112436 Location (UCSC) Chr 12: 7.65 – 7.67 Mb Chr 6: 122.55 – 122.58 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Apolipoprotein B mRNA editing enzyme, catalytic polypeptide 1** also known as **C->U-editing enzyme APOBEC-1** is a [protein](/source/Protein) that in humans is encoded by the *APOBEC1* [gene](/source/Gene).[5]

This gene encodes a member of the [APOBEC protein family](/source/APOBEC) and the [cytidine deaminase](/source/Cytidine_deaminase) enzyme family. The encoded protein forms a multiple-protein RNA editing [holoenzyme](/source/Holoenzyme) with APOBEC1 complementation factor ([A1CF](/source/A1CF)). This holoenzyme is involved in the editing of [cytosine](/source/Cytosine)-to-[uracil](/source/Uracil) (C-to-U) nucleotide bases in [apolipoprotein B](/source/Apolipoprotein_B) and [neurofibromin 1](/source/Neurofibromin_1) mRNAs.[5]

APOBEC-1 (A1) has been linked with cholesterol control, cancer development and inhibition of viral replication.[6] Its function relies on introducing a stop codon into [apolipoprotein B](/source/Apolipoprotein_B) (ApoB) [mRNA](/source/MRNA), which alters lipid metabolism in the gastrointestinal tract. The editing mechanism is highly specific. A1’s deamination of the cytosine base yields uracil, which creates a stop codon in the mRNA.

The overall deamination of cytidine to form uridine.

A1 has been linked with both positive and negative health effects. In rodents, it has wide tissue distribution where as in humans, it is only expressed in the small intestine.[7]

## Gene

*APOBEC1* lies on human chromosome 12.[8]

## Function

ApoB is essential in the assembly of very low density lipoproteins from lipids, in the liver and small intestine.[7] By editing ApoB, it forces only the smaller product, ApoB48, to be expressed, which greatly inhibits lipoprotein production. However, A1 is currently found only at extremely low levels in the human liver and intestine, while it is highly expressed in rodents. In humans, A1 is found exclusively in gastrointestinal epithelial cells.[6]

## Mechanism

A1 modifies the [cytosine](/source/Cytosine) base at position 6666 on the ApoB mRNA strand through a deamination.[9] An A1 dimer first binds to ACF, which forms the binding complex that is then able to eliminate the amine group from cytosine.

These residues (Leu-182 to Pro-191) are necessary for dimerization of APOBEC1, which is necessary to form the correct enzyme complex with ACF. During experimentation, substituted leucine and isoleucine residues significantly reduced the deamination of cytosine.

ACF binds to the mooring sequence, which puts A1 in position to edit the correct residue.[10] By converting cytosine to uracil, A1 changes the codon from CAA, which codes for glutamine during transcription, to UAA, a stop codon.[11] This stop codon yields the much shorter protein ApoB48 instead of ApoB100, as the mRNA is predisposed to transcript.[12] The editing amount, or expression, of A1 performs is correlated with the insulin concentration in the nucleus, the site of modification.[13][14] Tests involving A1 mutants with various deleted amino acid sequences have shown that editing activity is dependent on residues 14 to 35. Like all APOBEC proteins, A1 coordinates a zinc atom with two cysteine and one histidine residues that serve as a Lewis acid. Hydrolytic deamination of the cytosine amine group then occurs, catalyzed by the proton transfer from the nearby glutamic acid residue, and the enzymatic structure is conserved by a proline residue.[10]

Possible mechanism for C-to-U modification using Zinc complex with H-66, Cys-93, and Cys-96.

## Structure

The structure of A1 relies on three dimensional folds induced by a zinc complex.[15] These folds allow the enzyme to access the RNA specifically. Deletion tests with mutant strands have shown that residues 181 to 210 are integral to mRNA editing, and there is most likely a beta-turn at proline residues 190 and 191.[10] Specifically, L182, I185, and L189 are integral to the complex’s function, most likely due to their importance to dimerization.[10] Substituting these residues has no predicted impact on secondary structure, so the significant decrease in editing activity is best explained by the alteration of the side-chains, which are integral to dimer structure.[10] Amino acid replacements at these sites deactivated deamination. The C-terminal of enzyme structure is more strongly expressed in the nucleus, hence the site of modification, while the 181 to 210 residues indicate that the enzyme is in the cytoplasm. These are regulatory factors.[16]

APOBEC1 catalytic active site, residue regionResidues 59-70, 82-95Linking glycine represents residues 71-81, which are not related to activation

## Disease relevance

The low levels of A1 in humans are one reason why high lipid intake is damaging to health. ApoB48 is essential for the assembly and secretion of triglyceride-rich chylomicrons, which are necessary as a response to high-fat intake. ApoB100 are metabolized in the bloodstream to LDL cholesterol,[17] high levels of which are associated with atherosclerosis.[18] While A1 has a negligible impact on human lipid synthesis, at high concentrations it can be genotoxic. Its diffusion toward the nucleic membrane can lead it to mutate DNA sequences that are actively transcribed on the genome. In single growth assays, A1 has been found to impact HIV replications. Additionally, A1 has reduced Hepatitis B virus (HBV) DNA replication, although the mechanism is still not known. The antiviral properties of A1 extend to both DNA and RNA due to its deamination function, which can hinder DNA replication and consequently suppress further infection by HIV or HBV.[19] A pan-cancer study shows that A1 mRNA level is associated with adverse prognosis as well as higher rate of the human genomic insertions and deletions (indels), particularly in-frame ones, which proposes its endogenous mutator activity. [20] There has also been evidence that A1 also edits at NF1, related to tumors in nerve cells.[21]

## Interactions

APOBEC1 has been shown to [interact](/source/Protein-protein_interaction) with:

- [ACF](/source/ACF_(gene))[22][23]

- [BAG4](/source/BAG4),[24] and

- [SYNCRIP](/source/SYNCRIP).[25]

## See also

- [Apolipoprotein B](/source/Apolipoprotein_B)

- [Post-transcriptional modification](/source/Post-transcriptional_modification)

- [Mutation](/source/Mutation)

- [Deamination](/source/Deamination)

- [NF1](/source/Neurofibromin_1)

- [Dimer (chemistry)](/source/Dimer_(chemistry))

- [Chromosome 12 (human)](/source/Chromosome_12_(human))

## References

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1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000040613](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000040613) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

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1. **[^](#cite_ref-pmid20348446_18-0)** Chen Z, Eggerman TL, Bocharov AV, Baranova IN, Vishnyakova TG, Csako G, Patterson AP (2010). ["Hypermutation induced by APOBEC-1 overexpression can be eliminated"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2856876). *RNA*. **16** (5): 1040–52. [doi](/source/Doi_(identifier)):[10.1261/rna.1863010](https://doi.org/10.1261%2Frna.1863010). [PMC](/source/PMC_(identifier)) [2856876](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2856876). [PMID](/source/PMID_(identifier)) [20348446](https://pubmed.ncbi.nlm.nih.gov/20348446).

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1. **[^](#cite_ref-pmid11352648_25-0)** Lau PP, Chang BH, Chan L (April 2001). "Two-hybrid cloning identifies an RNA-binding protein, GRY-RBP, as a component of apobec-1 editosome". *Biochem. Biophys. Res. Commun*. **282** (4): 977–83. [Bibcode](/source/Bibcode_(identifier)):[2001BBRC..282..977L](https://ui.adsabs.harvard.edu/abs/2001BBRC..282..977L). [doi](/source/Doi_(identifier)):[10.1006/bbrc.2001.4679](https://doi.org/10.1006%2Fbbrc.2001.4679). [PMID](/source/PMID_(identifier)) [11352648](https://pubmed.ncbi.nlm.nih.gov/11352648).

## External links

- Human [*APOBEC1*](https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&singleSearch=knownCanonical&position=APOBEC1) genome location and [*APOBEC1*](https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_type=knownGene&hgg_gene=APOBEC1) gene details page in the [UCSC Genome Browser](/source/UCSC_Genome_Browser).

## Further reading

- Wedekind JE, Dance GS, Sowden MP, Smith HC (2003). "Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business". *Trends Genet*. **19** (4): 207–16. [doi](/source/Doi_(identifier)):[10.1016/S0168-9525(03)00054-4](https://doi.org/10.1016%2FS0168-9525%2803%2900054-4). [PMID](/source/PMID_(identifier)) [12683974](https://pubmed.ncbi.nlm.nih.gov/12683974).

- Harris RS, Liddament MT (2004). "Retroviral restriction by APOBEC proteins". *Nat. Rev. Immunol*. **4** (11): 868–77. [doi](/source/Doi_(identifier)):[10.1038/nri1489](https://doi.org/10.1038%2Fnri1489). [PMID](/source/PMID_(identifier)) [15516966](https://pubmed.ncbi.nlm.nih.gov/15516966). [S2CID](/source/S2CID_(identifier)) [10789405](https://api.semanticscholar.org/CorpusID:10789405).

- Espinosa R, Funahashi T, Hadjiagapiou C, Le Beau MM, Davidson NO (1994). "Assignment of the gene encoding the human apolipoprotein B mRNA editing enzyme (APOBEC1) to chromosome 12p13.1". *Genomics*. **24** (2): 414–5. [doi](/source/Doi_(identifier)):[10.1006/geno.1994.1645](https://doi.org/10.1006%2Fgeno.1994.1645). [PMID](/source/PMID_(identifier)) [7698776](https://pubmed.ncbi.nlm.nih.gov/7698776).

- Navaratnam N, Bhattacharya S, Fujino T, Patel D, Jarmuz AL, Scott J (1995). ["Evolutionary origins of apoB mRNA editing: catalysis by a cytidine deaminase that has acquired a novel RNA-binding motif at its active site"](https://doi.org/10.1016%2F0092-8674%2895%2990328-3). *Cell*. **81** (2): 187–95. [doi](/source/Doi_(identifier)):[10.1016/0092-8674(95)90328-3](https://doi.org/10.1016%2F0092-8674%2895%2990328-3). [PMID](/source/PMID_(identifier)) [7736571](https://pubmed.ncbi.nlm.nih.gov/7736571).

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- Lau PP, Zhu HJ, Nakamuta M, Chan L (1997). ["Cloning of an Apobec-1-binding protein that also interacts with apolipoprotein B mRNA and evidence for its involvement in RNA editing"](https://doi.org/10.1074%2Fjbc.272.3.1452). *J. Biol. Chem*. **272** (3): 1452–5. [doi](/source/Doi_(identifier)):[10.1074/jbc.272.3.1452](https://doi.org/10.1074%2Fjbc.272.3.1452). [PMID](/source/PMID_(identifier)) [8999813](https://pubmed.ncbi.nlm.nih.gov/8999813).

- Oka K, Kobayashi K, Sullivan M, Martinez J, Teng BB, Ishimura-Oka K, Chan L (1997). ["Tissue-specific inhibition of apolipoprotein B mRNA editing in the liver by adenovirus-mediated transfer of a dominant negative mutant APOBEC-1 leads to increased low density lipoprotein in mice"](https://doi.org/10.1074%2Fjbc.272.3.1456). *J. Biol. Chem*. **272** (3): 1456–60. [doi](/source/Doi_(identifier)):[10.1074/jbc.272.3.1456](https://doi.org/10.1074%2Fjbc.272.3.1456). [PMID](/source/PMID_(identifier)) [8999814](https://pubmed.ncbi.nlm.nih.gov/8999814).

- Hirano K, Min J, Funahashi T, Baunoch DA, Davidson NO (1997). ["Characterization of the human apobec-1 gene: expression in gastrointestinal tissues determined by alternative splicing with production of a novel truncated peptide"](https://doi.org/10.1016%2FS0022-2275%2820%2937210-2). *J. Lipid Res*. **38** (5): 847–59. [doi](/source/Doi_(identifier)):[10.1016/S0022-2275(20)37210-2](https://doi.org/10.1016%2FS0022-2275%2820%2937210-2). [PMID](/source/PMID_(identifier)) [9186903](https://pubmed.ncbi.nlm.nih.gov/9186903).

- Fujino T, Navaratnam N, Scott J (1998). "Human apolipoprotein B RNA editing deaminase gene (APOBEC1)". *Genomics*. **47** (2): 266–75. [doi](/source/Doi_(identifier)):[10.1006/geno.1997.5110](https://doi.org/10.1006%2Fgeno.1997.5110). [PMID](/source/PMID_(identifier)) [9479499](https://pubmed.ncbi.nlm.nih.gov/9479499).

- Mehta A, Kinter MT, Sherman NE, Driscoll DM (2000). ["Molecular cloning of apobec-1 complementation factor, a novel RNA-binding protein involved in the editing of apolipoprotein B mRNA"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC85365). *Mol. Cell. Biol*. **20** (5): 1846–54. [doi](/source/Doi_(identifier)):[10.1128/MCB.20.5.1846-1854.2000](https://doi.org/10.1128%2FMCB.20.5.1846-1854.2000). [PMC](/source/PMC_(identifier)) [85365](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC85365). [PMID](/source/PMID_(identifier)) [10669759](https://pubmed.ncbi.nlm.nih.gov/10669759).

- Lellek H, Kirsten R, Diehl I, Apostel F, Buck F, Greeve J (2000). ["Purification and molecular cloning of a novel essential component of the apolipoprotein B mRNA editing enzyme-complex"](https://doi.org/10.1074%2Fjbc.M001786200). *J. Biol. Chem*. **275** (26): 19848–56. [doi](/source/Doi_(identifier)):[10.1074/jbc.M001786200](https://doi.org/10.1074%2Fjbc.M001786200). [PMID](/source/PMID_(identifier)) [10781591](https://pubmed.ncbi.nlm.nih.gov/10781591).

- Blanc V, Navaratnam N, Henderson JO, Anant S, Kennedy S, Jarmuz A, Scott J, Davidson NO (2001). ["Identification of GRY-RBP as an apolipoprotein B RNA-binding protein that interacts with both apobec-1 and apobec-1 complementation factor to modulate C to U editing"](https://doi.org/10.1074%2Fjbc.M006435200). *J. Biol. Chem*. **276** (13): 10272–83. [doi](/source/Doi_(identifier)):[10.1074/jbc.M006435200](https://doi.org/10.1074%2Fjbc.M006435200). [PMID](/source/PMID_(identifier)) [11134005](https://pubmed.ncbi.nlm.nih.gov/11134005).

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- Lau PP, Villanueva H, Kobayashi K, Nakamuta M, Chang BH, Chan L (2001). ["A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B mRNA editing"](https://doi.org/10.1074%2Fjbc.M109215200). *J. Biol. Chem*. **276** (49): 46445–52. [doi](/source/Doi_(identifier)):[10.1074/jbc.M109215200](https://doi.org/10.1074%2Fjbc.M109215200). [PMID](/source/PMID_(identifier)) [11584023](https://pubmed.ncbi.nlm.nih.gov/11584023).

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- Mukhopadhyay D, Anant S, Lee RM, Kennedy S, Viskochil D, Davidson NO (2002). ["C-->U editing of neurofibromatosis 1 mRNA occurs in tumors that express both the type II transcript and apobec-1, the catalytic subunit of the apolipoprotein B mRNA-editing enzyme"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC384902). *Am. J. Hum. Genet*. **70** (1): 38–50. [doi](/source/Doi_(identifier)):[10.1086/337952](https://doi.org/10.1086%2F337952). [PMC](/source/PMC_(identifier)) [384902](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC384902). [PMID](/source/PMID_(identifier)) [11727199](https://pubmed.ncbi.nlm.nih.gov/11727199).

- Dance GS, Sowden MP, Cartegni L, Cooper E, Krainer AR, Smith HC (2002). ["Two proteins essential for apolipoprotein B mRNA editing are expressed from a single gene through alternative splicing"](https://doi.org/10.1074%2Fjbc.M111337200). *J. Biol. Chem*. **277** (15): 12703–9. [doi](/source/Doi_(identifier)):[10.1074/jbc.M111337200](https://doi.org/10.1074%2Fjbc.M111337200). [PMID](/source/PMID_(identifier)) [11815617](https://pubmed.ncbi.nlm.nih.gov/11815617).

v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5) 3.5.1: Linear amides / Amidohydrolases Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin 3.5.2: Cyclic amides/ Amidohydrolases Barbiturase Beta-lactamase Dihydroorotase 3.5.3: Linear amidines/ Ureohydrolases Arginase Agmatinase Protein-arginine deiminase 3.5.4: Cyclic amidines/ Aminohydrolases Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase 3.5.5: Nitriles/ Aminohydrolases Nitrilase 3.5.99: Other Riboflavinase Thiaminase II

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)

[Portal](https://en.wikipedia.org/wiki/Wikipedia:Contents/Portals):
- [Biology](https://en.wikipedia.org/wiki/Portal:Biology)

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Adapted from the Wikipedia article [APOBEC1](https://en.wikipedia.org/wiki/APOBEC1) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/APOBEC1?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.