| Type |
Details |
Score |
| Publication |
| First Author: |
Xu X |
| Year: |
2021 |
| Journal: |
Front Neurosci |
| Title: |
Bone Marrow Stromal Cell Antigen 2: Is a Potential Neuroinflammation Biomarker of SOD1(G93A) Mouse Model of Amyotrophic Lateral Sclerosis in Pre-symptomatic Stage. |
| Volume: |
15 |
|
| Pages: |
788730 |
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•
•
•
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| Publication |
| First Author: |
Manouchehri N |
| Year: |
2021 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
CD11c+CD88+CD317+ myeloid cells are critical mediators of persistent CNS autoimmunity. |
| Volume: |
118 |
| Issue: |
14 |
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•
•
•
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| Publication |
| First Author: |
Yamamoto A |
| Year: |
2021 |
| Journal: |
FASEB J |
| Title: |
Transcription factor old astrocyte specifically induced substance is a novel regulator of kidney fibrosis. |
| Volume: |
35 |
| Issue: |
2 |
| Pages: |
e21158 |
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| Protein Domain |
| Type: |
Family |
| Description: |
SARS-CoV contains a number of open reading frames that code for a total of eight accessory proteins, namely ORFs 3a, 3b, 6, 7a, 7b, 8a, 8b, and 9b. These ORFs are specific for SARS-CoV and do not show significant homology to accessory proteins of other coronaviruses. This entry represents the structural accessory protein ORF7a, also called NS7a, of Severe Acute Respiratory Syndrome Coronaviruses (SARS-CoV) from betacoronavirus subgenera Sarbecovirus (lineage B), including SARS-CoV-2. ORF7a/NS7a from betacoronavirus in the subgenera Sarbecovirus (B lineage) are not related to NS7a proteins from other coronavirus lineages.Structurally, ORF7a possesses a distinctive immunoglobulin (Ig)-like domain which is related to extracellular metazoan Ig domains that are involved in adhesion, such as ICAM; it also contains a 15-aa signal peptide sequence at its N terminus, an 81-aa luminal domain, a 21-aa transmembrane domain, and a short C-terminal tail. Coexpression of SARS-CoV ORF7a with S, M, N, and E proteins resulted in production of virus-like particles (VLPs) carrying ORF7a protein, indicating that ORF7a is a viral structural protein. Expression studies of ORF7a have shown that biological functions include induction of apoptosis through a caspase-dependent pathway, activation of the p38 mitogen-activated protein kinase signaling pathway, inhibition of host protein translation, and suppression of cell growth progression. These results collectively suggested that ORF7a protein may be involved in virus-host interactions []. Studies in SARS-CoV-2 revealed that ORF7a plays a role as antagonist of host tetherin (BST2), disrupting its antiviral effect. ORF7a binds to BST2 and sequesters it to the perinuclear region, thereby preventing its antiviral function at cell membrane []. |
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| Protein Domain |
| Type: |
Domain |
| Description: |
This entry includes the structural accessory protein ORF7a, also called NS7a, X4 and U122, of Severe Acute Respiratory Syndrome Coronaviruses (SARS-CoV) from betacoronavirus subgenera Sarbecovirus (lineage B), including SARS-CoV-2. ORF7a/NS7a from betacoronavirus in the subgenera Sarbecovirus (B lineage) are not related to NS7a proteins from other coronavirus lineages. The structure of the structural accessory protein ORF7a, shows similarities to the immunoglobulin-like fold with some features resembling those of the Dl domain of ICAM-1 and suggests a binding activity to integrin I domains []. In SARS-CoV-infected cells, ORF7a is expressed and retained intracellularly within the Golgi network []. ORF7a is thought to play an important role during the SARS-CoV replication cycle []. Expression studies of ORF7a have shown that biological functions include induction of apoptosis through a caspase-dependent pathway, activation of the p38 mitogen-activated protein kinase signaling pathway, inhibition of host protein translation, and suppression of cell growth progression. These results collectively suggested that ORF7a protein may be involved in virus-host interactions []. Studies in SARS-CoV-2 revealed that ORF7a plays a role as antagonist of host tetherin (BST2), disrupting its antiviral effect. ORF7a binds to BST2 and sequesters it to the perinuclear region, thereby preventing its antiviral function at cell membrane [].This entry represents the X4 ectodomain from ORF7a (X4e), which forms a well defined β-sandwich fold. It is built up from seven β-strands, four strands form one β-sheet and the other three strands form a second sheet. The sheets are closely packed or 'sandwiched' against each other. Each sheet is amphipathic with the hydrophobic side facing inward. Two disulfide bonds link both sheets on opposite edges therefore stabilizing the β-sandwich structure [, ]. |
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| Publication |
| First Author: |
Nelson CA |
| Year: |
2005 |
| Journal: |
Structure |
| Title: |
Structure and intracellular targeting of the SARS-coronavirus Orf7a accessory protein. |
| Volume: |
13 |
| Issue: |
1 |
| Pages: |
75-85 |
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•
•
•
•
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| Publication |
| First Author: |
Hänel K |
| Year: |
2006 |
| Journal: |
J Biomed Sci |
| Title: |
Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains. |
| Volume: |
13 |
| Issue: |
3 |
| Pages: |
281-93 |
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•
•
•
•
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| Publication |
| First Author: |
Akerström S |
| Year: |
2007 |
| Journal: |
Antiviral Res |
| Title: |
Inhibition of SARS-CoV replication cycle by small interference RNAs silencing specific SARS proteins, 7a/7b, 3a/3b and S. |
| Volume: |
73 |
| Issue: |
3 |
| Pages: |
219-27 |
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