P16899 · ENV_OMVVS

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.

1990100200300400500600700800900
TypeIDPosition(s)Description
Site662-663Cleavage; by host

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 Processsymbiont entry into host cell
Biological Processvirion attachment to host cell

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Envelope glycoprotein gp160
  • Alternative names
    • Env polyprotein
  • Cleaved into 2 chains

Gene names

    • Name
      env

Organism names

Accessions

  • Primary accession
    P16899

Subcellular Location

Transmembrane protein

Virion membrane
; Single-pass type I membrane protein
Host cell membrane
; Single-pass type I membrane protein
Note: It is probably 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.

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. It is probably 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).

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain108-838Extracellular
Transmembrane839-859Helical
Topological domain860-990Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, lipidation.

TypeIDPosition(s)Description
Signal1-107
ChainPRO_0000038732108-662Surface protein
ChainPRO_0000239539108-990Envelope glycoprotein gp160
Glycosylation141N-linked (GlcNAc...) asparagine; by host
Glycosylation162N-linked (GlcNAc...) asparagine; by host
Glycosylation207N-linked (GlcNAc...) asparagine; by host
Glycosylation259N-linked (GlcNAc...) asparagine; by host
Glycosylation299N-linked (GlcNAc...) asparagine; by host
Glycosylation363N-linked (GlcNAc...) asparagine; by host
Glycosylation386N-linked (GlcNAc...) asparagine; by host
Glycosylation402N-linked (GlcNAc...) asparagine; by host
Glycosylation413N-linked (GlcNAc...) asparagine; by host
Glycosylation434N-linked (GlcNAc...) asparagine; by host
Glycosylation438N-linked (GlcNAc...) asparagine; by host
Glycosylation469N-linked (GlcNAc...) asparagine; by host
Glycosylation474N-linked (GlcNAc...) asparagine; by host
Glycosylation480N-linked (GlcNAc...) asparagine; by host
Glycosylation490N-linked (GlcNAc...) asparagine; by host
Glycosylation500N-linked (GlcNAc...) asparagine; by host
Glycosylation514N-linked (GlcNAc...) asparagine; by host
Glycosylation526N-linked (GlcNAc...) asparagine; by host
Glycosylation536N-linked (GlcNAc...) asparagine; by host
Glycosylation542N-linked (GlcNAc...) asparagine; by host
Glycosylation550N-linked (GlcNAc...) asparagine; by host
Glycosylation560N-linked (GlcNAc...) asparagine; by host
Glycosylation567N-linked (GlcNAc...) asparagine; by host
ChainPRO_0000038733663-990Transmembrane protein
Glycosylation703N-linked (GlcNAc...) asparagine; by host
Glycosylation771N-linked (GlcNAc...) asparagine; by host
Glycosylation778N-linked (GlcNAc...) asparagine; by host
Glycosylation794N-linked (GlcNAc...) asparagine; by host
Lipidation862S-palmitoyl cysteine; by host

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 (By similarity).
The transmembrane protein 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.

Family & Domains

Features

Showing features for region, coiled coil.

TypeIDPosition(s)Description
Region663-683Fusion peptide
Coiled coil695-745
Region729-745Immunosuppression
Coiled coil786-821
Region890-909Disordered

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    990
  • Mass (Da)
    114,498
  • Last updated
    1990-08-01 v1
  • Checksum
    279B816BE55614F3
MASSKNMPSRITQKSMEPPLRETWQQVVQEMVMRKQRDEEEKQNLVTGKEKSWVSIDLLGTKQEGKRQKVNIWGPWEKWGIKIVWVMLWVIQLMLWGCLIWEMGKKHSCNAEEVIALVDDPGGFQKVKYVESVPVTCMTKNFTQWGCQPEGAYPDPDLEYRNISQDILEQVYKQEWPWNTYHWPLWQMENMRQWMKENEKEYTSRNNKTKEDIDALLAGKIRGRFCVPYPFALLKCEEWCWYPANINQETGHAQQIKINCTKAKAVSCTEQMPLAAVQRVYWEKEDEEGMKFMNIQACNESQLRCKTSPGGCVQGYPIPVGAEIIPESMKYLRGKKSPYGGIKDKNGELKLPLSVRVWVRMANLSGWVNGTPPYWSARIKGSTGINGTRWYGIGTLHHLGYNISSNPEKGLCNFTKELWIGGDRFQYQYKPSWNCSQNWTGYPVWHVFRYLDMTEHMTSRCVQRPLRHNITVGNGTITGNCSVTDWEGCNCTRSGNYLYNSTTGGLLVIICRQNSTITGIMGTNTNWTTMWGIYKNCSECKNSTLDRTDNGTLGTVNNINCSLPHYNESNKWTCAARNSKKKRDSLYIAGRDFWGRVKALYSCESNLGGLDGMMHQQMVLQKYQVIKVRAYTYGVVDMPKAYREKNMRNKRSTEISRPRKKRGIGLVIVLAIMAIIAAAGAGLGVANAVQQSYTRTAVQSLANATAAQQNVLEATYAMVQHVAKGVRILEARVARVEAIVDRMMLYHELDCWHYQHYCVTSTRTEVAQYVNWTRYKDNCTWQQWEEEIEQHEANLSLLLKEAALQVQIAQRDAQRIPDVWKALQEAFDWSGWFSWLKYIPWIVVCIVGVICFRLLMCVITMCLQAYRQVREIRYTRVTVVIEAPVDLEEKQREERDGSSGSENLEHEKRTSPRSFIQIWRATVQAWKTSPWGKGWKKILYMTLLPLLTLQIWMEETGWNGDKRCKKKKERVDCQDRESMPAIENEYVELS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M34193
EMBL· GenBank· DDBJ
AAA46783.1
EMBL· GenBank· DDBJ
Genomic DNA
M31646
EMBL· GenBank· DDBJ
AAA66817.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

Disclaimer

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