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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Envelope glycoprotein

UniprotKB/SwissProt ID: Q27ID8 (Q27ID8)

Gene Name: env

Organism: Xenotropic MuLV-related virus (isolate VP62) (XMRV)

Function: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction activates a thiol in a CXXC motif of the C-terminal domain, where the other Cys residue participates in the formation of the intersubunit disulfide. The activated thiol will attack the disulfide and cause its isomerization into a disulfide isomer within the motif. This leads to SU displacement and TM refolding, and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity) The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Virion membrane. Host cell membrane. Virion membrane. Host cell membrane. Host cell membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR008981 FMuLV_rcpt-bd
IPR018154 TLV/ENV_coat_polyprotein