Genome Polyprotein Langat Virus Recombinant Protein

Function: Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA

By similarity.prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated

By similarity.Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes

By similarity.

Subcellular location: Capsid protein C: Virion

Potential. Peptide pr: Secreted

By similarity. Small envelope protein M: Virion membrane; Multi-pass membrane protein

By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein

By similarity. Envelope protein E: Virion membrane; Multi-pass membrane protein

By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein

By similarity.

Post-translational modification: Specific enzymatic cleavages in vivo yield mature proteins Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site

By similarity.