P27399 · ENV_SFV3L

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.

TypeIDPosition(s)Description
Site126-127Cleavage; by host
Site566-567Cleavage; by host

GO annotations

AspectTerm
Cellular Componenthost cell endoplasmic reticulum membrane
Cellular Componentmembrane
Cellular Componentviral envelope
Cellular Componentvirion membrane

Names & Taxonomy

Protein names

  • Recommended name
    Envelope glycoprotein gp130
  • Alternative names
    • Env polyprotein
  • Cleaved into 3 chains

Gene names

    • Name
      env

Organism names

Accessions

  • Primary accession
    P27399

Proteomes

Subcellular Location

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.

TypeIDPosition(s)Description
Topological domain1-65Cytoplasmic
Transmembrane66-88Helical; Signal-anchor for type III membrane protein
Topological domain89-954Lumenal
Transmembrane955-975Helical
Topological domain976-982Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain, cross-link, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00002454341-126Leader peptide
ChainPRO_00001254701-982Envelope glycoprotein gp130
Cross-link14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Glycosylation109N-linked (GlcNAc...) asparagine; by host
ChainPRO_0000245435127-566Surface protein
Glycosylation141N-linked (GlcNAc...) asparagine; by host
Glycosylation183N-linked (GlcNAc...) asparagine; by host
Glycosylation309N-linked (GlcNAc...) asparagine; by host
Glycosylation346N-linked (GlcNAc...) asparagine; by host
Glycosylation390N-linked (GlcNAc...) asparagine; by host
Glycosylation404N-linked (GlcNAc...) asparagine; by host
Glycosylation412N-linked (GlcNAc...) asparagine; by host
Glycosylation484N-linked (GlcNAc...) asparagine; by host
Glycosylation522N-linked (GlcNAc...) asparagine; by host
Glycosylation551N-linked (GlcNAc...) asparagine; by host
ChainPRO_0000245436567-982Transmembrane protein
Glycosylation776N-linked (GlcNAc...) asparagine; by host
Glycosylation802N-linked (GlcNAc...) asparagine; by host
Glycosylation827N-linked (GlcNAc...) asparagine; by host

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 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).

Structure

3D structure databases

Family & Domains

Features

Showing features for region, motif.

TypeIDPosition(s)Description
Region1-15Involved in virion budding
Region570-592Fusion peptide
Motif978-980Endoplasmic reticulum retention signal

Domain

The ER retention signal plays an important role in establishing the intracellular site of budding.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    982
  • Mass (Da)
    113,314
  • Last updated
    1992-08-01 v1
  • Checksum
    721F2F8929D604FF
MAPPMNLQQWLLWKKMNETHLALENISSLTEEQKQQVIIEIQQEEVIPTRMDRVKYLAYACCATSTRVMCWLFLICVLLIIVFVSCFVTVARIQWNRDINVFGPVIDWNVTHQATYQQLKAARLTRSLKVEHPHISYISINMSSIPQGVMYTPHPEPIILKERVLGISQVLMINSENIANVANLSQETKVLLTDMINEELQDLSNQMIDFELPLGDPRDQDQYIHHKCYQEFAHCYLVKYKKPSPWISEGIIVDQCPLPRIHDPNYYKYQPIWDYYLKIQNIRPQGWTSKSYYGTARMGSFYIPTFLRNNTVSHVLFCSDQLYGKWYNIENNIQENEQLLKTKLYNLTTYSKLKARALPKEWNNQGNARLFRSFNPLDVCNRPEAVLLLNTTYFTYSLWEGDCNYTTALIQNLTECRQPDRLKLKHPYACRFWRYKEGQEEVKCLGNEKKKCLYYSEYSSPEAQFDFGFLSYLNAFPGLKYIENQTVREPEYEVYSLYMECMNSAEKYGIDSVLFALKTFLNFTGTPVNEMSTARAFVGLTDPKFPPTYPNITKEQKRCNNLKRRKRSTNIEKLRSMGYSLTGAVQTLSQISDINDERLQQGVSLLRDHVVTLMEAALHDITIMEGMLAIQHVHTHLNHLKTILLMRKIDWTFIKSNWIKEQLQKTEDEMKIIRRTAKSLVYYVTQTSSSTTATSWEIGIYYEITIPKHIYLNNWQVINIGHLVESAGHLTLIRVKHPYEVINKECTYEQYLHLEDCISQDYVICDTVQIVSPCGNSTTTSDCPVTAEKVKEPYVQVSALKNGSYLVLTSRTDCSIPAYVPSIVTVNETVKCFGVEFHKPLYSESKVSFEPQVPHLKLRLPHLVGIIANLQNLEIEVTSTQESIKDQIERAKSQLLRLDIHEGDFPAWIQQLASATRDVWPAAARALQGIGNVLSNTAQGIFGTTVSILSYAKPILIGIGVILLIAFLFKIVSWLPGKKKRN

Sequence caution

The sequence AAA47798.1 differs from that shown. Reason: Erroneous initiation

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M74895
EMBL· GenBank· DDBJ
AAA47798.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation

Genome annotation databases

Similar Proteins

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