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- Table of Contents
Facts about MORC family CW-type zinc finger protein 3.
Recruits TP53 and SP100 to PML-NBs, thus regulating TP53 activity (PubMed:17332504). Binds RNA in vitro (PubMed:11927593).
Human | |
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Gene Name: | MORC3 |
Uniprot: | Q14149 |
Entrez: | 23515 |
Belongs to: |
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No superfamily |
KIAA0136; MORC family CW-type zinc finger 3; MORC family CW-type zinc finger protein 3; nuclear matrix protein NXP2; NXP2; ZCW5; ZCWCC3; Zinc finger CW-type coiled-coil domain protein 3; zinc finger, CW type with coiled-coil domain 3; zinc finger, CW-type with coiled-coil domain 3
Mass (kDA):
107.113 kDA
Human | |
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Location: | 21q22.12 |
Sequence: | 21; NC_000021.9 (36320189..36376646) |
Expressed in heart, placenta, skeletal muscle, brain, pancreas, lung, liver, but not kidney.
Nucleus, nucleoplasm. Nucleus matrix. Nucleus, PML body. Also found in PML-independent nuclear bodies. Localization to nuclear bodies is ATP-dependent.
The MORC3 marker is one of the most widely used polynucleotide markers for HIV immunotherapy. This marker can identify HIV immunotherapy-positive cells. It was first developed in 1993. It is highly sensitive and is used in a wide range of immunological tests. You can read on to learn about its uses. This article provides a general introduction about the MORC3 marker, and its uses.
MORC3 is a protein found in the nucleus of many cells. It is part of the MORC protein family, which also includes the divergent SMCHD1 gene. MORC3 includes three domains. These are the GHLATPase and CW-type zinc finger domains, as well as the coiled coil dimerization domain. This protein may be involved in gene silencing or regulation of chromatin structure in response to DNA damage signals. The protein Sp100 (and p53) recruit MORC3 to PML cells' nucleus.
MORC3 also has an antiviral function. MORC3 also has an antiviral function, which reduces the rate of human cytomegalovirus plaque growth. MORC3 has antiviral properties that go beyond HSV-1. For this reason, researchers have studied the MORC3 gene in mice. The MORC3 mutation causes the infection in these mice.
MORC3 has been shown to be found to interact with the ICP0 protein at the nucleus before its degradation. It is capable of detecting many types if cancer. However, it's not clear exactly how MORC3 breaks down in the body. It is known that HSV-1 causes its degradation. Despite the importance of MORC3, this marker is still a valuable tool for molecular biologists, and other researchers.
Recent research shows that MORC3 is an epigenetic controller. It may play a role in transcription regulation, chromatin modification, and DNA repair. It has been linked to many types of cancers. Although it has been demonstrated that this gene is essential for influenza replication, no antiviral function has been found. The best use of the MORC3 marker is yet to be determined for cancer research.
The MORC3 polynucleotides, which are highly expressed within influenza virus, play a role transcriptionally. This marker can help to determine the role played by NXP2/MORC3 for influenza virus replication. It is highly expressed in human and mouse lymphoid tissues, and can be used in numerous applications including diagnosis, research, and vaccine development.
One of MORC3's most exciting uses is its ability detect IAP elements in DNA. This marker has the highest affinity for IAP element. On the other hand, MORC2A targets LINE elements. These enrichments suggest that the MORCs regulate distinct repetitive elements. MORC3 is therefore an important molecular marker for the identification of ERVs.
MORC2 regulates chromatin access at heterochromatic loci that are rich in zinc finger proteins. MORC1 mutations in C.elegans cause in vivo decompactions of chromatin. MORC3 activates TheATPase and allows for efficient compactions of naked DNA, chromatin, and chromatin. It is still not clear what MORC3 does in the human body.
Infection with influenza virus affects the cellular accumulation of NXP2/MORC3 and its localization in the cell. The ability of the infectious virus to multiply can be reduced by downregulating NXP2/MORC3. This protein is essential for several important illnesses, including influenza. It is used in many areas and has been validated in numerous clinical trials. The full publication contains more information about the MORC3 polynucleotide mark.
Recent research shows that CTA1 DD enhances certain immune responses against HIV in nonhuman primates. This discovery could open the door to a clinically safe cell-mediated vaccine adjuvant or mucosal vaccine adjuvant. This marker could also be used as a way to identify HIV-positive individuals. This study will enable researchers to better understand MORC3's role in HIV immunotherapy.
The human immunodeficiency virus (HIV) is a highly contagious virus that causes acquired immune deficiency syndrome. HIV disease is a series of symptoms in HIV-infected patients that causes a loss of T cells. HIV type 1 and HIV 2 are the main strains. Related viruses are also used as animal models in research.
New compounds must be developed to prevent HIV-infected cells replication in humans. This is especially true in the context of HIV immunotherapy. These compounds contain immunogenic compositions that elicit a protective immune response against the virus. The MORC3 gene marker is a promising candidate.
Moorc3 shows an important role for HIV immunotherapy. MORC3 helps in the development of new antivirals. Researchers have been studying HIV's molecular structures and the MORC3 marker is a great candidate. A recent study published in Science Translational Medicine illustrates the potential advantages of MORC3 for HIV immunotherapy.
The HIV-1 envelope protein, gp120, contains the MORC3 protein. The V1/V2 domains include approximately 50-90 different residues. These include the gp120 positions 128-194. The V3 loop is critical for binding coreceptors. The V3 domain has residues starting with gp120, which are vital for HIV-infected cells. Its amino sequence can found in GENBANK (r), Accession No. ACF75939
The MORC3 polypeptide marker has several useful functions in virology. Its antiviral activities are essential during HSV-1 and HMV-2 infections. Additionally, its depletion causes plaque formation to increase. MORC3 may have applications in many areas, including the field of cancer research. Here are some of the most commonly used MORC3 applications.
The MORC3 polypeptide mark is a highly localized protein within the nuclear matrix. When cells become infected with the influenza virus, a fraction of MORC3 relocates to the cytoplasm. The cytoplasm also contains the viral Ribonucleoprotein Complex (RNP), which interacts with MORC3. It has antiviral property, which is demonstrated by its ability infuse infected cells with virus replication.
The study showed that MORC3 was involved in the recruitment and transfer of PML NB proteins into HSV-1 genomes. This suggests that MORC3 also plays a role in the recruitment PML NB proteins. It has also been suggested that it is a transcriptional suppressor and DNA binding proteins. Its function is still unclear. However, further research is needed. And because of its high level of conservation, MORC3 has a wide range of applications.
Research in molecular diagnosing has shown MORC3 as a useful protein to detect breast cancer. It is also associated wit resistance to antiestrogen drugs. It can regulate the activity of the tumor suppressor p53, which regulates the induction of cellular senescence in PML. It could be used as a therapeutic target. It also facilitates recruitment of polycomb suppressive complex 2 (polycomb repressive) and enhancer of zeste holog 2.
The MORC3 proteins are also known as the mTORC3. It has several uses in virology. It is an epigenetic regulator in cell division and regulation. It could play a role DNA break repair, transcription regulation and chromatin remodeling. It has been associated with a variety cancers, but it was not previously thought to be involved in the antiviral reaction to influenza.
PMID: 11927593 by Kimura Y., et al. The newly identified human nuclear protein NXP-2 possesses three distinct domains, the nuclear matrix-binding, RNA-binding, and coiled- coil domains.
PMID: 17332504 by Takahashi K., et al. Dynamic regulation of p53 subnuclear localization and senescence by MORC3.