| IED ID | IndEnz0002019306 |
| Enzyme Type ID | protease019306 |
| Protein Name |
Envelope glycoprotein gp130 Env polyprotein Cleaved into: Leader peptide LP Env leader protein Elp gp18LP ; Surface protein SU Glycoprotein 80 gp80 ; Transmembrane protein TM Glycoprotein 48 gp48 |
| Gene Name | env |
| Organism | Simian foamy virus (isolate chimpanzee) (SFVcpz) |
| Taxonomic Lineage | Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Spumaretrovirinae Spumavirus Simian foamy virus Simian foamy virus (isolate chimpanzee) (SFVcpz) |
| Enzyme Sequence | MAPPMTLQQWIIWNKMNKAHEALQNSTTVTDQQKEQIILEIQNEEVRPTRKDKIRYLLYTCCATSSRVLAWMLLVCVLLIVVLVSCFLTISRIQWNRDIQVLGPVIDWNVTQRAVYQPLQTRRIARSLRMQHPVPKYIEVNMTSIPQGVYYEPHPEPIVVTERVLGLSQVLMINSENIANNANLTQEVKKLLAEVVNEEMQSLSDVMIDFEIPLGDPRDQEQYIHRKCYQEFAHCYLVKYKTPKSWPTEGLIADQCPLPGYHAGLSYKPQSIWDYYIKVEITRPANWSSQAVYGQARLGSFYVPKGIRQNNYSHVLFCSDQLYSKWYNIENSIEQNEKFLLNKLDNLTTGSSLLKKRALPKEWSSQGKNALFKEINVLDVCSKPELVILLNTSYYSFSLWEGDCNFTKNMISQLVPECEGFYNNSKWMHMHPYACRFWRSKNEKEETKCRPGEKEKCLYYPYQDSLESTYDFGFLAYQKNFPAPICIEQQEIRDKDYEVYSLYQECKLASKVHGIDTVLFSLKNFLNHTGRPVNEMPNARAFVGLVDPKFPPSYPNVTREHYTSCNNRKRRSTDNNYAKLKSMGYALTGAVQTLSQISDINDENLQQGIYLLRDHVITLMEATLHDISVMEGMFAVQHLHTHLNHLKTMLLERRIDWTYMSSAWLQQQLQKSDDEMKVIKRIAKSLVYYVKQTYNSPTATAWEIGLYYELTIPKHVYLNNWNVVNIGHLVQSAGQLTHVTIAHPYEIINKECTETKYLHLKDCRRQDYVICDVVEIVQPCGNSTDTSDCPVWAEAVKEPFVQVNPLKNGSYLVLASSTDCQIPPYVPSIVTVNETTSCYGLNFKKPLVAEERLGFEPRLPNLQLRLPHLVGIIAKIKGLKIEVTSSGESIKDQIERAKAELLRLDIHEGDTPAWIQQLAAATKDVWPAAASALQGIGNFLSGAAHGIFGTAFSLLGYLKPILIGVGVILLIILIFKIVSWIPTKKKSQ |
| Enzyme Length | 988 |
| Uniprot Accession Number | Q87041 |
| 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 the cell receptor. This interaction triggers the refolding of transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide (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}.; FUNCTION: The leader peptide is a component of released, infectious virions and is required for particle budding. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (4); Cross-link (4); Glycosylation (14); Motif (1); Mutagenesis (2); Region (2); Site (3); Topological domain (3); Transmembrane (2) |
| Keywords | Cleavage on pair of basic residues;Glycoprotein;Host endoplasmic reticulum;Host membrane;Isopeptide bond;Membrane;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Ubl conjugation;Viral envelope protein;Virion |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Envelope glycoprotein gp130]: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:23132852}. Note=The polyprotein has a highly unusual biosynthesis for a retroviral glycoprotein. It is translated as a full-length precursor protein into the rough endoplasmic reticulum and initially has a type III protein configuration with both its N and C-termini located intracytoplasmically (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Leader peptide]: Virion membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Its N-terminus is located inside the viral particle. {ECO:0000250}.; SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endoplasmic reticulum membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host endoplasmic reticulum membrane; Peripheral membrane protein. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Envelope glycoproteins are synthesized as an inactive precursor that is processed by host furin or a furin-like proprotein convertase (PC)-mediated cleavage proteolysis to yield a functional heterooligomeric complex (By similarity). Further proteolytically processed through regulated intramembrane proteolysis either by SPPL2A and SPPL2B or by SPPL3 in a PC-mediated cleavage-dependent or -independent manner, respectively (PubMed:23132852). {ECO:0000250, ECO:0000269|PubMed:23132852}.; PTM: The transmembrane protein and the surface protein are N-glycosylated.; PTM: Mono- and polyubiquitinated leader peptide are found in viral particles. Ubiquitination may be involved in regulating the balance between viral and subviral particles release. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 984..986; /note=Endoplasmic reticulum retention signal; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 113,353 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |