| Identification |
|---|
| HMDB Protein ID
| HMDBP14233 |
| Secondary Accession Numbers
| None |
| Name
| Genome polyprotein |
| Synonyms
|
Not Available
|
| Gene Name
| Not Available |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers.Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is the only viral peptide matured by host furin in the trans-Golgi network probably to avoid catastrophic activation of the viral fusion activity in acidic Golgi compartment prior to virion release. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.May play a role in virus budding. Exerts cytotoxic effects by activating a mitochondrial apoptotic pathway through M ectodomain. May display a viroporin activity.Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease. |
| Pathways
|
Not Available
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| fusion of virus membrane with host endosome membrane |
| clathrin-dependent endocytosis of virus by host cell |
| virion attachment to host cell |
| Cellular Component |
| integral to membrane |
| extracellular region |
| viral envelope |
| host cell endoplasmic reticulum membrane |
| virion membrane |
| viral nucleocapsid |
| Molecular Function |
| protein dimerization activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| Not Available |
| Molecular Weight
| 74931.37 |
| Theoretical pI
| Not Available |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
- 2-22;139-159;166-180;626-646;653-673;
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| P18356 |
| UniProtKB/Swiss-Prot Entry Name
| POLG_DEN2U |
| PDB IDs
|
|
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Gruenberg A, Woo WS, Biedrzycka A, Wright PJ: Partial nucleotide sequence and deduced amino acid sequence of the structural proteins of dengue virus type 2, New Guinea C and PUO-218 strains. J Gen Virol. 1988 Jun;69 ( Pt 6):1391-8. doi: 10.1099/0022-1317-69-6-1391. [PubMed:3385407 ]
- Huang KC, Lee MC, Wu CW, Huang KJ, Lei HY, Cheng JW: Solution structure and neutralizing antibody binding studies of domain III of the dengue-2 virus envelope protein. Proteins. 2008 Feb 15;70(3):1116-9. doi: 10.1002/prot.21806. [PubMed:18004779 ]
- Lok SM, Kostyuchenko V, Nybakken GE, Holdaway HA, Battisti AJ, Sukupolvi-Petty S, Sedlak D, Fremont DH, Chipman PR, Roehrig JT, Diamond MS, Kuhn RJ, Rossmann MG: Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins. Nat Struct Mol Biol. 2008 Mar;15(3):312-7. doi: 10.1038/nsmb.1382. Epub 2008 Feb 10. [PubMed:18264114 ]
- Yu IM, Holdaway HA, Chipman PR, Kuhn RJ, Rossmann MG, Chen J: Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion. J Virol. 2009 Dec;83(23):12101-7. doi: 10.1128/JVI.01637-09. Epub 2009 Sep 16. [PubMed:19759134 ]
|
