| IED ID | IndEnz0002018880 |
| Enzyme Type ID | protease018880 |
| Protein Name |
Envelope glycoprotein gp95 Env polyprotein Cleaved into: Surface protein SU Glycoprotein 85 gp85 ; Transmembrane protein TM Glycoprotein 37 gp37 |
| Gene Name | env |
| Organism | Rous sarcoma virus (strain Prague C) (RSV-PrC) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Orthoretrovirinae Alpharetrovirus Rous sarcoma virus Rous sarcoma virus (strain Prague C) (RSV-PrC) |
| Enzyme Sequence | MRRALFLQAFLTGYPGKTSKKDSKEKPLATSKKDPEKTPLLPTRVNYILIIGVLVLCEVTGVRADVHLLEQPGNLWITWANRTGQTDFCLSTQSATSPFQTCLIGIPSPISEGDFKGYVSDTNCSTVGTDRLVLSASITGGPDNSTTLTYRKVSCLLLKLNVSMWDEPPELQLLGSQSLPNVTNITQVSGVAGGCVYFAPRATGLFLGWSKQGLSRFLLRHPFTSTSNSTEPFTVVTADRHNLFMGSEYCGAYGYRFWEIYNCSQTRNTYRCGDVGGTGLPETWCRGKGGIWVNQSKEINETEPFSFTANCTGSNLGNVSGCCGEPITILPLGAWIDSTQGSFTKPKALPPAIFLICGDRAWQGIPSRPVGGPCYLGKLTMLAPNHTDILKILANSSRTGIRRKRSVSHLDDTCSDEVQLWGPTARIFASILAPGVAAAQALREIERLACWSVKQANLTTSLLGDLLDDVTSIRHAVLQNRAAIDFLLLAHGHGCEDVAGMCCFNLSDHSESIQKKFQLMKKHVNKIGVDSDPIGSWLRGIFGGIGEWAVHLLKGLLLGLVVILLLLVCLPCLLQFVSSSIRKMINSSINYHTEYRKMQGGAV |
| Enzyme Length | 603 |
| Uniprot Accession Number | P03396 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). {ECO:0000250}.; FUNCTION: 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). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Coiled coil (2); Glycosylation (16); Lipidation (2); Mutagenesis (2); Natural variant (9); Region (2); Sequence conflict (1); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Cleavage on pair of basic residues;Coiled coil;Disulfide bond;Fusion of virus membrane with host cell membrane;Fusion of virus membrane with host membrane;Glycoprotein;Host cell membrane;Host membrane;Host-virus interaction;Lipoprotein;Membrane;Palmitate;Signal;Transmembrane;Transmembrane helix;Viral attachment to host cell;Viral envelope protein;Viral penetration into host cytoplasm;Virion;Virus entry into host cell |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity). {ECO:0000250}.; PTM: The transmembrane protein is palmitoylated. Palmitoylation is necessary for glycoprotein function and infectivity. {ECO:0000269|PubMed:11689636}. |
| Signal Peptide | SIGNAL 1..64; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 65,661 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |