P31791 · ENV_FENV1

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).
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).

Features

Showing features for site.

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TypeIDPosition(s)Description
Site470-471Cleavage; by host
Site650-651Cleavage; by viral protease

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componenthost cell plasma membrane
Cellular Componentmembrane
Cellular Componentviral envelope
Cellular Componentvirion membrane
Biological Processfusion of virus membrane with host plasma membrane
Biological Processsymbiont entry into host cell
Biological Processvirion attachment to host cell

Keywords

Names & Taxonomy

Protein names

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

Gene names

    • Name
      env

Organism names

Accessions

  • Primary accession
    P31791
  • Secondary accessions
    • Q28416

Subcellular Location

Transmembrane protein

Virion membrane
; Single-pass type I membrane protein
Host cell membrane
; Single-pass type I membrane protein

Surface protein

Virion membrane ; Peripheral membrane protein
Host cell 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. 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).

R-peptide

Host cell membrane
; Peripheral membrane protein
Note: The R-peptide is membrane-associated through its palmitate.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain23-611Extracellular
Transmembrane612-632Helical
Topological domain633-671Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, lipidation, peptide.

TypeIDPosition(s)Description
Signal1-22
ChainPRO_000004070323-470Surface protein
ChainPRO_000023955823-671Envelope glycoprotein
Disulfide bond121↔142
Disulfide bond134↔147
Glycosylation169N-linked (GlcNAc...) asparagine; by host
Glycosylation281N-linked (GlcNAc...) asparagine; by host
Glycosylation326N-linked (GlcNAc...) asparagine; by host
Glycosylation331N-linked (GlcNAc...) asparagine; by host
Glycosylation355N-linked (GlcNAc...) asparagine; by host
Glycosylation358N-linked (GlcNAc...) asparagine; by host
Glycosylation415N-linked (GlcNAc...) asparagine; by host
Glycosylation435N-linked (GlcNAc...) asparagine; by host
ChainPRO_0000040704471-650Transmembrane protein
Lipidation631S-palmitoyl cysteine; by host
PeptidePRO_0000239559651-671R-peptide

Post-translational modification

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. The R-peptide is released from the C-terminus of the cytoplasmic tail of the TM protein upon particle formation as a result of proteolytic cleavage by the viral protease. Cleavage of this peptide is required for TM to become fusogenic (By similarity).
The transmembrane protein is palmitoylated.
The R-peptide is palmitoylated.

Keywords

PTM databases

Interaction

Subunit

The mature envelope protein (Env) consists of a trimer of SU-TM heterodimers attached by noncovalent interactions or by a labile interchain disulfide bond.

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias, motif, coiled coil.

TypeIDPosition(s)Description
Region265-310Disordered
Compositional bias290-306Pro residues
Motif336-339CXXC
Region473-493Fusion peptide
Coiled coil501-550
Region539-555Immunosuppression
Motif556-564CX6CC
Coiled coil560-596
Motif656-659YXXL motif; contains endocytosis signal

Domain

The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo (By similarity).

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    671
  • Mass (Da)
    75,152
  • Last updated
    1993-07-01 v1
  • Checksum
    EA9847024EF794A0
MKPPAGMVFLWVLTSLGAGIGAKIVKEGNPHQVYTLTWQIYSQSGEVVWEVQGNHALNTWWPALTPDFCQLAAGLDTWDIPDRSPKNLETSMEGTSQQLTPQGCSKPWKRCALTERDFYVCPRDNRDRATAHRCGGYEEYFCSAWGCETTGDAYWQPTSTWDLITITRNYTKPDSCDDRVERERKTSRHWRDPLSLPLKITFTDSGKRALGWQTGYTWGLRWYLPGKDRGIILKIKLKIDTITQTVGPNLVLADQKTPVQLAIPVQPPRAPTQTPRVNPVNSTLSPSLGYPAPAPGPRPPYPTSPSRPGTGDRLLNLVQGVYLTLNLTAPNQTQDCWLCLTAKPPYYQGVAIIGNFTNHTNAPLRCSTTPRHGLTLTEVTGYGLCIGKIPPSHQNLCSQTVPSVGQGPYYLTAPNGTYWVCNTGLTPCISLQILNDTADYCILIELWPKIFYHDSEYIYGHYEPGGRFRRDPVSLTVALLLGGLTMGSLAAGIGTGTAALIETNQFKQLQIAMHSDIQALEESISALERSLISLSEVVLQNRRGLDLLFLQEGGLCAALKEECCFYADHTGIVRDSMAKLRERFKQRQKLFESQQGWFEGWYNKSPWFTTLVSSLMVPLILLLLILMFGPCILNHLLQFIRERLSVIQALVLTQQYHQLRQFDAERPDAIE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias290-306Pro residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X51929
EMBL· GenBank· DDBJ
CAB38567.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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