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SFVgp2 Structural polyprotein [ Semliki Forest virus ]

Gene ID: 922351, updated on 18-Jul-2024
Gene symbol
SFVgp2
Gene description
Structural polyprotein
Locus tag
SFVgp2
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Semliki Forest virus
Lineage
Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes; Martellivirales; Togaviridae; Alphavirus
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Sequence:
NC_003215.1 (7420..11181)

NC_003215.1Genomic Context describing neighboring genes Neighboring gene Nonstructural polyprotein Neighboring gene truncated structural polyprotein

Genomic Sequence:
NC_003215.1

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Ability of the Encephalitic Arbovirus Semliki Forest Virus To Cross the Blood-Brain Barrier Is Determined by the Charge of the E2 Glycoprotein. Ferguson MC, et al. J Virol, 2015 Aug. PMID 25972559, Free PMC Article
  2. Semliki Forest virus produced in the absence of the 6K protein has an altered spike structure as revealed by decreased membrane fusion capacity. McInerney GM, et al. Virology, 2004 Aug 1. PMID 15246260
  3. Mutations that promote furin-independent growth of Semliki Forest virus affect p62-E1 interactions and membrane fusion. Zhang X, et al. Virology, 2004 Oct 1. PMID 15351216
  4. A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion. Chanel-Vos C, et al. J Virol, 2004 Dec. PMID 15564465, Free PMC Article
  5. Reversible acid-induced inactivation of the membrane fusion protein of Semliki Forest virus. Waarts BL, et al. J Virol, 2005 Jun. PMID 15919953, Free PMC Article

See all (22) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. results suggest that the E2 D-loop interacts with the E1 protein to promote Alphavirus budding
    Title: An Alphavirus E2 Membrane-Proximal Domain Promotes Envelope Protein Lateral Interactions and Virus Budding.
  2. Lysine or glutamic acid residues at position 162 or 247 in the SFV E2 glycoprotein affects the level of viremia and the efficiency of neuroinvasion.
    Title: Ability of the Encephalitic Arbovirus Semliki Forest Virus To Cross the Blood-Brain Barrier Is Determined by the Charge of the E2 Glycoprotein.
  3. Thus, E3 mediates pH protection of E1 during virus biogenesis via interactions strongly dependent on Y47 at the E3-E2 interface.
    Title: The role of E3 in pH protection during alphavirus assembly and exit.
  4. Our results suggest a critical and previously unidentified role for the DI-DIII linker region during the low-pH-dependent refolding of E1 that drives membrane fusion.
    Title: The domain I-domain III linker plays an important role in the fusogenic conformational change of the alphavirus membrane fusion protein.
  5. The results suggest that furin-cleaved E3 continues to protect the spike from premature activation in acidic compartments of the cell and that its release in the neutral extracellular space primes the spike for low-pH activation.
    Title: Activation of the alphavirus spike protein is suppressed by bound E3.
  6. D188K mutation of E1 blocks E1 trimerization and inhibits virus entry and infection.
    Title: Pseudorevertants of a Semliki forest virus fusion-blocking mutation reveal a critical interchain interaction in the core trimer.
  7. Results indicate that the D188K mutation of Semliki Forest virus E1 protein block SFV fusion and infection.
    Title: E1 mutants identify a critical region in the trimer interface of the Semliki forest virus fusion protein.
  8. findings showed the E1 H3A mutation produced impaired virus growth & a more acidic pH requirement for virus-membrane fusion; results & location of H3 suggest this residue acts to regulate the low-pH-dependent refolding of E1 during membrane fusion
    Title: Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein.
  9. SFV E1 is the first virus fusion protein demonstrated to directly bind cholesterol.
    Title: Differential cholesterol binding by class II fusion proteins determines membrane fusion properties.
  10. Cells expressing low pH-triggered class II viral fusion protein E1 of SFV were fused to target cells. It is proposed that the trans-negative voltage across the endosomal membrane facilitates fusion after low-pH-induced conformational changes of SFV E1.
    Title: Fusion induced by a class II viral fusion protein, semliki forest virus E1, is dependent on the voltage of the target cell.
Submit: New GeneRIF Correction See all GeneRIFs (15)
Products Interactant Other Gene Complex Source Pubs Description
Preferred Names
Structural polyprotein
Names
C protein
E3 protein
E2 protein
6K protein
E1 protein

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_003215.1 Reference assembly

    Range
    7420..11181
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_463458.1 Structural polyprotein [Semliki Forest virus]

    See identical proteins and their annotated locations for NP_463458.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    B3TP01, P03315, Q809B6, Q8JMP5
    UniProtKB/TrEMBL
    Q3LRQ2

  2. NP_819004.1 C protein

    UniProtKB/TrEMBL
    Q87048

  3. NP_819005.1 E3 protein

    UniProtKB/TrEMBL
    Q87051

  4. NP_819006.1 E2 protein

    UniProtKB/TrEMBL
    Q87050

  5. NP_819007.1 6K protein

    UniProtKB/TrEMBL
    Q87045

  6. NP_819008.1 E1 protein

    UniProtKB/TrEMBL
    Q87046
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P03315.1

Gene LinkOut

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