P27399 · ENV_SFV3L
- ProteinEnvelope glycoprotein gp130
- Geneenv
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids982 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 TM and is thought to activate its fusogenic potential by unmasking its fusion peptide (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).
The leader peptide is a component of released, infectious virions and is required for particle budding.
Miscellaneous
Foamy viruses are distinct from other retroviruses in many respects. Their protease is active as an uncleaved Pro-Pol protein. Mature particles do not include the usual processed retroviral structural protein (MA, CA and NC), but instead contain two large Gag proteins. Their functional nucleic acid appears to be either RNA or dsDNA (up to 20% of extracellular particles), because they probably proceed either to an early (before integration) or late reverse transcription (after assembly). Foamy viruses have the ability to retrotranspose intracellularly with high efficiency. They bud predominantly into the endoplasmic reticulum (ER) and occasionally at the plasma membrane. Budding requires the presence of Env proteins. Most viral particles probably remain within the infected cell.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 126-127 | Cleavage; by host | ||||
Sequence: RS | ||||||
Site | 566-567 | Cleavage; by host | ||||
Sequence: KR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Cellular Component | viral envelope | |
Cellular Component | virion membrane |
Names & Taxonomy
Protein names
- Recommended nameEnvelope glycoprotein gp130
- Alternative names
- Cleaved into 3 chains
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Pararnavirae > Artverviricota > Revtraviricetes > Ortervirales > Retroviridae > Spumaretrovirinae > Spumavirus > African green monkey simian foamy virus
- Virus hosts
Accessions
- Primary accessionP27399
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Envelope glycoprotein gp130
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).
Leader peptide
Virion membrane ; Single-pass type II membrane protein
Host endoplasmic reticulum membrane ; Single-pass type II membrane protein
Note: Its N-terminus is located inside the viral particle.
Transmembrane protein
Virion membrane ; Single-pass type I membrane protein
Host endoplasmic reticulum membrane ; Single-pass type I membrane protein
Surface protein
Virion membrane ; Peripheral membrane protein
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.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-65 | Cytoplasmic | ||||
Sequence: MAPPMNLQQWLLWKKMNETHLALENISSLTEEQKQQVIIEIQQEEVIPTRMDRVKYLAYACCATS | ||||||
Transmembrane | 66-88 | Helical; Signal-anchor for type III membrane protein | ||||
Sequence: TRVMCWLFLICVLLIIVFVSCFV | ||||||
Topological domain | 89-954 | Lumenal | ||||
Sequence: TVARIQWNRDINVFGPVIDWNVTHQATYQQLKAARLTRSLKVEHPHISYISINMSSIPQGVMYTPHPEPIILKERVLGISQVLMINSENIANVANLSQETKVLLTDMINEELQDLSNQMIDFELPLGDPRDQDQYIHHKCYQEFAHCYLVKYKKPSPWISEGIIVDQCPLPRIHDPNYYKYQPIWDYYLKIQNIRPQGWTSKSYYGTARMGSFYIPTFLRNNTVSHVLFCSDQLYGKWYNIENNIQENEQLLKTKLYNLTTYSKLKARALPKEWNNQGNARLFRSFNPLDVCNRPEAVLLLNTTYFTYSLWEGDCNYTTALIQNLTECRQPDRLKLKHPYACRFWRYKEGQEEVKCLGNEKKKCLYYSEYSSPEAQFDFGFLSYLNAFPGLKYIENQTVREPEYEVYSLYMECMNSAEKYGIDSVLFALKTFLNFTGTPVNEMSTARAFVGLTDPKFPPTYPNITKEQKRCNNLKRRKRSTNIEKLRSMGYSLTGAVQTLSQISDINDERLQQGVSLLRDHVVTLMEAALHDITIMEGMLAIQHVHTHLNHLKTILLMRKIDWTFIKSNWIKEQLQKTEDEMKIIRRTAKSLVYYVTQTSSSTTATSWEIGIYYEITIPKHIYLNNWQVINIGHLVESAGHLTLIRVKHPYEVINKECTYEQYLHLEDCISQDYVICDTVQIVSPCGNSTTTSDCPVTAEKVKEPYVQVSALKNGSYLVLTSRTDCSIPAYVPSIVTVNETVKCFGVEFHKPLYSESKVSFEPQVPHLKLRLPHLVGIIANLQNLEIEVTSTQESIKDQIERAKSQLLRLDIHEGDFPAWIQQLASATRDVWPAAARALQGIGNVLSNTAQGIFGTTVSILSYAKP | ||||||
Transmembrane | 955-975 | Helical | ||||
Sequence: ILIGIGVILLIAFLFKIVSWL | ||||||
Topological domain | 976-982 | Cytoplasmic | ||||
Sequence: PGKKKRN |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, cross-link, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000245434 | 1-126 | Leader peptide | |||
Sequence: MAPPMNLQQWLLWKKMNETHLALENISSLTEEQKQQVIIEIQQEEVIPTRMDRVKYLAYACCATSTRVMCWLFLICVLLIIVFVSCFVTVARIQWNRDINVFGPVIDWNVTHQATYQQLKAARLTR | ||||||
Chain | PRO_0000125470 | 1-982 | Envelope glycoprotein gp130 | |||
Sequence: MAPPMNLQQWLLWKKMNETHLALENISSLTEEQKQQVIIEIQQEEVIPTRMDRVKYLAYACCATSTRVMCWLFLICVLLIIVFVSCFVTVARIQWNRDINVFGPVIDWNVTHQATYQQLKAARLTRSLKVEHPHISYISINMSSIPQGVMYTPHPEPIILKERVLGISQVLMINSENIANVANLSQETKVLLTDMINEELQDLSNQMIDFELPLGDPRDQDQYIHHKCYQEFAHCYLVKYKKPSPWISEGIIVDQCPLPRIHDPNYYKYQPIWDYYLKIQNIRPQGWTSKSYYGTARMGSFYIPTFLRNNTVSHVLFCSDQLYGKWYNIENNIQENEQLLKTKLYNLTTYSKLKARALPKEWNNQGNARLFRSFNPLDVCNRPEAVLLLNTTYFTYSLWEGDCNYTTALIQNLTECRQPDRLKLKHPYACRFWRYKEGQEEVKCLGNEKKKCLYYSEYSSPEAQFDFGFLSYLNAFPGLKYIENQTVREPEYEVYSLYMECMNSAEKYGIDSVLFALKTFLNFTGTPVNEMSTARAFVGLTDPKFPPTYPNITKEQKRCNNLKRRKRSTNIEKLRSMGYSLTGAVQTLSQISDINDERLQQGVSLLRDHVVTLMEAALHDITIMEGMLAIQHVHTHLNHLKTILLMRKIDWTFIKSNWIKEQLQKTEDEMKIIRRTAKSLVYYVTQTSSSTTATSWEIGIYYEITIPKHIYLNNWQVINIGHLVESAGHLTLIRVKHPYEVINKECTYEQYLHLEDCISQDYVICDTVQIVSPCGNSTTTSDCPVTAEKVKEPYVQVSALKNGSYLVLTSRTDCSIPAYVPSIVTVNETVKCFGVEFHKPLYSESKVSFEPQVPHLKLRLPHLVGIIANLQNLEIEVTSTQESIKDQIERAKSQLLRLDIHEGDFPAWIQQLASATRDVWPAAARALQGIGNVLSNTAQGIFGTTVSILSYAKPILIGIGVILLIAFLFKIVSWLPGKKKRN | ||||||
Cross-link | 14 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 15 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Cross-link | 34 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Glycosylation | 109 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Chain | PRO_0000245435 | 127-566 | Surface protein | |||
Sequence: SLKVEHPHISYISINMSSIPQGVMYTPHPEPIILKERVLGISQVLMINSENIANVANLSQETKVLLTDMINEELQDLSNQMIDFELPLGDPRDQDQYIHHKCYQEFAHCYLVKYKKPSPWISEGIIVDQCPLPRIHDPNYYKYQPIWDYYLKIQNIRPQGWTSKSYYGTARMGSFYIPTFLRNNTVSHVLFCSDQLYGKWYNIENNIQENEQLLKTKLYNLTTYSKLKARALPKEWNNQGNARLFRSFNPLDVCNRPEAVLLLNTTYFTYSLWEGDCNYTTALIQNLTECRQPDRLKLKHPYACRFWRYKEGQEEVKCLGNEKKKCLYYSEYSSPEAQFDFGFLSYLNAFPGLKYIENQTVREPEYEVYSLYMECMNSAEKYGIDSVLFALKTFLNFTGTPVNEMSTARAFVGLTDPKFPPTYPNITKEQKRCNNLKRRK | ||||||
Glycosylation | 141 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 183 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 309 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 346 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 390 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 404 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 412 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 484 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 522 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 551 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Chain | PRO_0000245436 | 567-982 | Transmembrane protein | |||
Sequence: RSTNIEKLRSMGYSLTGAVQTLSQISDINDERLQQGVSLLRDHVVTLMEAALHDITIMEGMLAIQHVHTHLNHLKTILLMRKIDWTFIKSNWIKEQLQKTEDEMKIIRRTAKSLVYYVTQTSSSTTATSWEIGIYYEITIPKHIYLNNWQVINIGHLVESAGHLTLIRVKHPYEVINKECTYEQYLHLEDCISQDYVICDTVQIVSPCGNSTTTSDCPVTAEKVKEPYVQVSALKNGSYLVLTSRTDCSIPAYVPSIVTVNETVKCFGVEFHKPLYSESKVSFEPQVPHLKLRLPHLVGIIANLQNLEIEVTSTQESIKDQIERAKSQLLRLDIHEGDFPAWIQQLASATRDVWPAAARALQGIGNVLSNTAQGIFGTTVSILSYAKPILIGIGVILLIAFLFKIVSWLPGKKKRN | ||||||
Glycosylation | 776 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 802 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Glycosylation | 827 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N |
Post-translational modification
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.
The transmembrane protein and the surface protein are N-glycosylated.
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).
Keywords
- PTM
PTM databases
Interaction
Subunit
The mature envelope protein consists of a trimer of SU-TM heterodimers. The N-terminus of leader peptide specifically interacts with Gag protein. This specific interaction between Gag protein and Env glycoprotein may allow particle egress (By similarity).
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-15 | Involved in virion budding | ||||
Sequence: MAPPMNLQQWLLWKK | ||||||
Region | 570-592 | Fusion peptide | ||||
Sequence: NIEKLRSMGYSLTGAVQTLSQIS | ||||||
Motif | 978-980 | Endoplasmic reticulum retention signal | ||||
Sequence: KKK |
Domain
The ER retention signal plays an important role in establishing the intracellular site of budding.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length982
- Mass (Da)113,314
- Last updated1992-08-01 v1
- Checksum721F2F8929D604FF
Sequence caution
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M74895 EMBL· GenBank· DDBJ | AAA47798.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |