APOBEC3A

Apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3A, also known as APOBEC3A, is a gene of the APOBEC3 family found in humans, non-human primates, and some other mammals.^[1] It is a DNA cytidine deaminase with antiviral effects. While other members of the family such as APOBEC3G are believed to act by editing ssDNA by removing an amino group from cytosine in DNA, introducing a cytosine to uracil change which can ultimately lead to a cytosine to thymine mutation, one study suggests that APOBEC3A can inhibit parvoviruses by another mechanism.^[2] The cellular function of APOBEC3A is likely to be the destruction of foreign DNA through extensive deamination of cytosine.^[3]

This gene is a member of the polynucleotide cytosine deaminase gene family. It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22. Members of the cluster encode proteins that are structurally and functionally related to the C to U RNA-editing cytidine deaminase APOBEC1. The APOBEC3 family of DNA editing enzymes are thought to be part of the innate immune system by restricting retroviruses, mobile genetic elements like retrotransposons and endogenous retroviruses. APOBEC3A is highly expressed in monocytes and macrophages upon stimulation with interferon.^[3]

References

↑ "Entrez Gene: APOBEC3A apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3A".
↑ Iñigo Narvaiza, Daniel C. Linfesty, Benjamin N. Greener, Yoshiyuki Hakata, David J. Pintel, Eric Logue, Nathaniel R. Landau, Matthew D. Weitzman (2009). Jung, Jae U., ed. "Deaminase-Independent Inhibition of Parvoviruses by the APOBEC3A Cytidine Deaminase". PLoS Pathogens 5 (5): e1000439. doi:10.1371/journal.ppat.1000439. PMC 2678267. PMID 19461882.
1 2 Mark D. Stenglein, Michael B. Burns, Michael B. Burns, Joy Lengyel, Reuben S. Harris (2010). "APOBEC3 proteins mediate the clearance of foreign DNA from human cells". Nature Structural & Molecular Biology 17 (2): 222–229. doi:10.1038/nsmb.1744. PMC 2921484. PMID 20062055.

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:10.1016/S0168-9525(03)00054-4. PMID 12683974.
Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667.
Madsen P, Anant S, Rasmussen HH, et al. (1999). "Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1". J. Invest. Dermatol. 113 (2): 162–9. doi:10.1046/j.1523-1747.1999.00682.x. PMID 10469298.
Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
Jarmuz A, Chester A, Bayliss J, et al. (2002). "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22". Genomics 79 (3): 285–96. doi:10.1006/geno.2002.6718. PMID 11863358.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Izmailova E, Bertley FM, Huang Q, et al. (2003). "HIV-1 Tat reprograms immature dendritic cells to express chemoattractants for activated T cells and macrophages". Nature Medicine 9 (2): 191–7. doi:10.1038/nm822. PMID 12539042.
Mariani R, Chen D, Schröfelbauer B, et al. (2003). "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif". Cell 114 (1): 21–31. doi:10.1016/S0092-8674(03)00515-4. PMID 12859895.
Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Bogerd HP, Wiegand HL, Doehle BP, et al. (2006). "APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells". Nucleic Acids Res. 34 (1): 89–95. doi:10.1093/nar/gkj416. PMC 1326241. PMID 16407327.
Goila-Gaur R, Khan MA, Miyagi E, et al. (2007). "Targeting APOBEC3A to the viral nucleoprotein complex confers antiviral activity". Retrovirology 4: 61. doi:10.1186/1742-4690-4-61. PMC 2018723. PMID 17727729.

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase

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

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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APOBEC3A

References

Further reading