Hmdb loader
Identification
HMDB Protein ID HMDBP14232
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 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.Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
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
ATP binding
serine-type peptidase activity
RNA helicase activity
double-stranded RNA binding
nucleoside-triphosphatase activity
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 187438.87
Theoretical pI Not Available
Pfam Domain Function
Signals Not Available
Transmembrane Regions
  • 446-466;473-493;916-940;947-965;990-1010;1012-1030;1038-1058;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P27914
UniProtKB/Swiss-Prot Entry Name POLG_DEN2T
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Chen WB, Maguire T: Nucleotide sequence of the envelope glycoprotein gene of a dengue-2 virus isolated during an epidemic of benign dengue fever in Tonga in 1974. Nucleic Acids Res. 1990 Oct 11;18(19):5889. doi: 10.1093/nar/18.19.5889. [PubMed:2216784 ]
  2. Zhang Y, Zhang W, Ogata S, Clements D, Strauss JH, Baker TS, Kuhn RJ, Rossmann MG: Conformational changes of the flavivirus E glycoprotein. Structure. 2004 Sep;12(9):1607-18. doi: 10.1016/j.str.2004.06.019. [PubMed:15341726 ]