Detail Information for IndEnz0002001999
IED ID IndEnz0002001999
Enzyme Type ID protease001999
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 Human spumaretrovirus (SFVcpz(hu)) (Human foamy virus)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Ortervirales Retroviridae Spumaretrovirinae Spumavirus Simian foamy virus Human spumaretrovirus (SFVcpz(hu)) (Human foamy virus)
Enzyme Sequence MAPPMTLQQWIIWKKMNKAHEALQNTTTVTEQQKEQIILDIQNEEVQPTRRDKFRYLLYTCCATSSRVLAWMFLVCILLIIVLVSCFVTISRIQWNKDIQVLGPVIDWNVTQRAVYQPLQTRRIARSLRMQHPVPKYVEVNMTSIPQGVYYEPHPEPIVVKERVLGLSQILMINSENIANNANLTQEVKKLLTEMVNEEMQSLSDVMIDFEIPLGDPRDQEQYIHRKCYQEFANCYLVKYKEPKPWPKEGLIADQCPLPGYHAGLTYNRQSIWDYYIKVESIRPANWTTKSKYGQARLGSFYIPSSLRQINVSHVLFCSDQLYSKWYNIENTIEQNERFLLNKLNNLTSGTSVLKKRALPKDWSSQGKNALFREINVLDICSKPESVILLNTSYYSFSLWEGDCNFTKDMISQLVPECDGFYNNSKWMHMHPYACRFWRSKKNEKEETKCRDGETKRCLYYPLWDSPESTYDFGYLAYQKNFPSPICIEQQKIRDQDYEVYSLYQERKIASKAYGIDTVLFSLKNFLNYTGTPVNEMPNARAFVGLIDPKFPPSYPNVTREHYTSCNNRKRRSVDNNYAKLRSMGYALTGAVQTLSQISDINDENLQQGIYLLRDHVITLMEATLHDISVMEGMFAVQHLHTHLNHLKTMLLERRIDWTYMSSTWLQQQLQKSDDEMKVIKRIARSLVYYVKQTHSSPTATAWEIGLYYELVIPKHIYLNNWNVVNIGHLVKSAGQLTHVTIAHPYEIINKECVETIYLHLEDCTRQDYVICDVVKIVQPCGNSSDTSDCPVWAEAVKEPFVQVNPLKNGSYLVLASSTDCQIPPYVPSIVTVNETTSCFGLDFKRPLVAEERLSFEPRLPNLQLRLPHLVGIIAKIKGIKIEVTSSGESIKEQIERAKAELLRLDIHEGDTPAWIQQLAAATKDVWPAAASALQGIGNFLSGTAQGIFGTAFSLLGYLKPILIGVGVILLVILIFKIVSWIPTKKKNQ
Enzyme Length 989
Uniprot Accession Number P14351
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 (5); Erroneous initiation (2); Glycosylation (14); Motif (1); Mutagenesis (11); Region (2); Site (3); Topological domain (3); Transmembrane (2)
Keywords Cleavage on pair of basic residues;Direct protein sequencing;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. 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 {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; 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 protease to yield a functional hetero-oligomeric complex. {ECO:0000250}.; PTM: The transmembrane protein and the surface protein are N-glycosylated. {ECO:0000250}.; 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 (By similarity). {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 985..987; /note=Endoplasmic reticulum retention signal
Gene Encoded By
Mass 113,891
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda