National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory
Protein Information |
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| Protein Name | Non-structural protein 11 |
| Accession Code | K9N638 |
| Gene | 1a |
| Organism | Betacoronavirus England 1 (Taxonomy: 1263720) |
| Part of Reference Proteome? | No |
| Sequence (Length: 4391) |
Structure Viewer (PDB: 5HIH) |
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Description |
Position in the Nuclear Envelope |
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| Location | Location ID | Description |
| Host Perinuclear Region | SL-0382 | The host perinuclear region is the host cytoplasmic region just around the host nucleus. Note: This location is defined for viral proteins that appear in the perinuclear region of infected host cells | Membrane Topology |
| Topology | Source | Annotation Type |
| Transmembrane | UniProt | Sequence Analysis {ECO:0000255} | Assigned Ontology terms |
Description |
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|---|---|
| The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products. {By SimilarityUniProtKB:P0C6X7}. [Host translation inhibitor nsp1]: Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response. {Experimental EvidencePubMed:26311885}. [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses. {By SimilarityUniProtKB:P0C6X7}. [Papain-like proteinase]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates, together with nsp4, in the assembly of virally induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B. signaling. {By SimilarityUniProtKB:P0C6X7, ECO:0000269|PubMed:25142582}. [Non-structural protein 4]: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. {By SimilarityUniProtKB:P0C6X7}. [3C-like proteinase]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''- phosphate (ADRP). {By SimilarityUniProtKB:P0C6X7, ECO:0000255|PROSITE- ProRule:PRU00772}. [Non-structural protein 6]: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes. {By SimilarityUniProtKB:P0C6X7}. [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {By SimilarityUniProtKB:P0C6X7}. [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {By SimilarityUniProtKB:P0C6X7}. [Non-structural protein 9]: May participate in viral replication by acting as a ssRNA-binding protein. {By SimilarityUniProtKB:P0C6X7}. [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {By SimilarityUniProtKB:P0C6X7}. | Assigned Ontology terms |
Interactions with Nuclear Envelope proteins (2 interactors) |
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Interactions with other proteins (9 interactors) |
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Database | Links |
| UNIPROT | K9N638 |
| PDB | 4R3D 5DUS 5HIH 5WKJ 5WKK 5WKL 5WKM 7T3Y 7T3Z 7T40 7T41 |
| Pfam | PF16251 PF11501 PF11633 PF09401 PF19212 PF19211 PF19218 PF16348 PF19217 PF19213 PF08716 PF08717 PF08710 PF08715 PF01661 PF05409 |
| PROSITE | PS51963 PS51942 PS51941 PS51994 PS51945 PS51952 PS51962 PS51991 PS51990 PS51989 PS51992 PS51943 PS51944 PS51946 PS51949 PS51950 PS51951 PS51442 PS51154 PS51124 |
National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory