APOBEC3A
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Official Full Name
apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3A
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Overview
This gene is a member of the cytidine 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 protein encoded by this gene lacks the zinc binding activity of other family members. The protein plays a role in immunity, by restricting transmission of foreign DNA such as viruses. One mechanism of foreign DNA restriction is deamination of foreign double-stranded DNA cytidines to uridines, which leads to DNA degradation. However, other mechanisms are also thought to be involved, as anti-viral effect is not dependent on deaminase activity. One allele of this gene results from the deletion of approximately 29.5 kb of sequence between this gene, APOBEC3A, and the adjacent gene APOBEC3B. The breakpoints of the deletion are within the two genes, so the deletion allele is predicted to have the promoter and coding region of APOBEC3A, but the 3 UTR of APOBEC3B. -
Synonyms
APOBEC3A; apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3A; ARP3; phorbolin I; PHRBN;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Human
- Rhesus Macaque
- E.coli
- HEK293
- Mamanlian cells
- Mammalian Cell
- Flag
- GST
- His
- His (Fc)
- Avi
- His|SUMO
- Myc|DDK
- N/A
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
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Human | APOBEC3A-9753H | Recombinant Human APOBEC3A, GST-tagged | E.coli | GST | 1-61a.a. | |
Human | APOBEC3A-15H | Recombinant Human APOBEC3A protein, MYC/DDK-tagged | HEK293 | Myc/DDK | ||
Human | APOBEC3A-30HCL | Recombinant Human APOBEC3A lysate | HEK293 | N/A | ||
Human | APOBEC3A-5726HFL | Recombinant Full Length Human APOBEC3A protein, Flag-tagged | Mamanlian cells | Flag | ||
Human | APOBEC3A-1784H | Recombinant Human APOBEC3A Protein (1-199 aa), His-SUMO-tagged | E.coli | His/SUMO | 1-199 aa | |
Rhesus Macaque | APOBEC3A-360R | Recombinant Rhesus monkey APOBEC3A Protein, His-tagged | Mammalian Cell | His | ||
Rhesus Macaque | APOBEC3A-189R-B | Recombinant Rhesus Macaque APOBEC3A Protein Pre-coupled Magnetic Beads | HEK293 | |||
Rhesus Macaque | APOBEC3A-189R | Recombinant Rhesus Macaque APOBEC3A Protein, His (Fc)-Avi-tagged | HEK293 | His (Fc)-Avi |
- APOBEC3A Related Articles
APOBEC3A involved in several pathways and played different roles in them. We selected most pathways APOBEC3A participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with APOBEC3A were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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APOBEC3A has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by APOBEC3A itself. We selected most functions APOBEC3A had, and list some proteins which have the same functions with APOBEC3A. You can find most of the proteins on our site.
Function | Related Protein |
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APOBEC3A has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with APOBEC3A here. Most of them are supplied by our site. Hope this information will be useful for your research of APOBEC3A.
- Q&As
- Reviews
Q&As (18)
Ask a questionYes, genetic variants and polymorphisms of the APOBEC3A gene have been identified. These variations can affect the protein's activity or expression levels, potentially influencing its role in antiviral defense and mutagenesis.
Yes, our APOBEC3A proteins can be used in Western Blot.
Although APOBEC3A is primarily recognized for its antiviral activities, recent studies suggest it may play additional roles. It has been implicated in DNA repair processes, regulation of immune responses, and potential contributions to autoimmune disorders.
Given the anti-viral activity of APOBEC3A, there is interest in developing inhibitors that can block its function to limit viral replication. However, the development of specific and potent inhibitors is complex due to the structural similarities and overlapping functions of other APOBEC3 proteins.
While dysregulation of APOBEC3A activity has been implicated in cancer development, there is currently limited evidence linking alterations or mutations in the APOBEC3A gene to specific genetic disorders or diseases.
Several cellular factors, such as APOBEC3B, have been shown to interact with APOBEC3A and regulate its activity. Additionally, post-translational modifications, such as phosphorylation, may also modulate its function.
Several viruses have evolved strategies to counteract or evade the antiviral activity of APOBEC3A. For example, human immunodeficiency virus type 1 (HIV-1) encodes the protein Vif, which targets APOBEC3A (and other APOBEC3 proteins) for degradation.
APOBEC3A-induced DNA mutations can have diverse outcomes. On one hand, they can inhibit viral replication by introducing hypermutations that lead to non-functional viral genomes. On the other hand, excessive APOBEC3A activity or dysregulated expression can contribute to genomic instability and promote cancer development.
APOBEC3A has been reported to interact with several cellular proteins involved in DNA repair, immune responses, and viral pathogenesis. These interactions contribute to the regulation of its activity, but the full extent and functional consequences of these interactions are still being explored.
Yes, APOBEC3A-induced hypermutation can accelerate the evolution of various viruses, particularly RNA viruses. By introducing errors in viral genomes during replication, APOBEC3A can drive the emergence of viral variants that can potentially escape host immune responses or develop drug resistance.
APOBEC3A expression can vary among different cell types and tissues. It is predominantly expressed in tissues exposed to viral infections, such as the gastrointestinal tract, reproductive organs, and lymphoid tissues.
APOBEC3A belongs to a family of seven APOBEC3 proteins in humans, including APOBEC3B, APOBEC3C, APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H. These proteins share similar structural features and exhibit overlapping antiviral functions.
The antiviral and mutagenic activities of APOBEC3A make it an attractive target for therapeutic interventions. However, due to its potential for causing DNA mutations and genomic instability, careful consideration is needed to balance the benefits and potential risks in therapeutic applications.
No, APOBEC3A is primarily known for its activity on DNA molecules. It catalyzes the deamination of cytosines in single-stranded DNA, which can lead to the generation of uracil and subsequent DNA mutations.
There is evidence suggesting that certain environmental factors, such as chronic viral infections or exposure to genotoxic agents like cigarette smoke, can stimulate APOBEC3A expression and activity. These factors may contribute to increased DNA damage and mutagenesis.
While direct targeting of APOBEC3A for cancer treatment is challenging due to its mutagenic properties, there are ongoing efforts to develop therapeutic approaches that modulate its expression or activity to balance its antiviral effects while minimizing genomic instability.
The increased expression and mutational activity of APOBEC3A in certain cancers have led to investigations into its potential diagnostic and prognostic value. However, further research is needed to establish its utility as a clinical marker.
Dysregulation of APOBEC3A has been implicated in cancer development, specifically in various types of malignancies, including breast, cervical, and head and neck cancers. Elevated APOBEC3A expression and activity have been associated with increased mutagenesis and tumor evolution.
Customer Reviews (4)
Write a reviewthe APOBEC3A protein has proven to be invaluable in protein electron microscopy structure analysis.
I must applaud the APOBEC3A protein for its outstanding performance in Western blotting experiments.
I highly recommend the APOBEC3A protein for a variety of experimental applications.
The remarkable quality and reliability of the APOBEC3A protein have significantly contributed to the success of my structural investigations.
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