A0A2U7PVP1 · A0A2U7PVP1_9VIRU

  • Protein
    Pre-glycoprotein polyprotein GP complex
  • Gene
    GPC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

function

Glycoprotein G1

Forms the virion spikes together with glycoprotein G2. The glycoprotein spike trimers are connected to the underlying matrix. Interacts with the host receptor leading to virus endocytosis.

Glycoprotein G2

Forms the virion spikes together with glycoprotein G1. The glycoprotein spike trimers are connected to the underlying matrix. Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced by acidification.

Stable signal peptide

Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Features

Showing features for binding site, site.

Type
IDPosition(s)Description
Binding site57Zn2+ 1 (UniProtKB | ChEBI)
Site58-59Cleavage; by host signal peptidase
Site255-256Cleavage; by host MBTPS1
Binding site451Zn2+ 2 (UniProtKB | ChEBI)
Binding site453Zn2+ 2 (UniProtKB | ChEBI)
Binding site459Zn2+ 2 (UniProtKB | ChEBI)
Binding site463Zn2+ 1 (UniProtKB | ChEBI)
Binding site471Zn2+ 1 (UniProtKB | ChEBI)
Binding site473Zn2+ 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componenthost cell endoplasmic reticulum membrane
Cellular Componenthost cell Golgi membrane
Cellular Componenthost cell plasma membrane
Cellular Componentmembrane
Cellular Componentviral envelope
Cellular Componentvirion membrane
Molecular Functionmetal ion binding
Biological Processfusion of virus membrane with host endosome membrane
Biological Processreceptor-mediated endocytosis of virus by host cell
Biological Processvirion attachment to host cell

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Pre-glycoprotein polyprotein GP complex
  • Short names
    Pre-GP-C
  • Cleaved into 3 chains

Gene names

    • Name
      GPC

Organism names

  • Taxonomic identifier
  • Organism
    Apore virus
  • Strain
    • LBCE 12071
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Negarnaviricota > Polyploviricotina > Ellioviricetes > Bunyavirales > Arenaviridae > Mammarenavirus > Mammarenavirus aporeense

Accessions

  • Primary accession
    A0A2U7PVP1

Proteomes

Subcellular Location

Glycoprotein G2

Virion membrane
; Single-pass membrane protein
Host endoplasmic reticulum membrane
; Single-pass membrane protein
Host Golgi apparatus membrane
; Single-pass membrane protein
Host cell membrane
; Single-pass membrane protein
Note: Binding to the stable signal peptide masks endogenous ER localization signals in the cytoplasmic domain of G2 to ensure that only the fully assembled, tripartite GP complex is transported for virion assembly.

Glycoprotein G1

Virion membrane
; Peripheral membrane protein
Host endoplasmic reticulum membrane
; Peripheral membrane protein
Host Golgi apparatus membrane
; Peripheral membrane protein
Host cell membrane
; Peripheral membrane protein

Stable signal peptide

Virion membrane
; Single-pass type II membrane protein
Host endoplasmic reticulum membrane
; Single-pass type II membrane protein
Host Golgi apparatus membrane
; Single-pass type II membrane protein
Host cell membrane
; Single-pass type II membrane protein

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain2-17Extracellular
Topological domain34-58Cytoplasmic
Transmembrane431-448Helical
Topological domain450-489Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for initiator methionine, lipidation, chain, disulfide bond, glycosylation.

Type
IDPosition(s)Description
Initiator methionine1Removed; by host
Lipidation2N-myristoyl glycine; by host
ChainPRO_50234849992-58Stable signal peptide
ChainPRO_50234849982-489Pre-glycoprotein polyprotein GP complex
Disulfide bond85↔230
Glycosylation88N-linked (GlcNAc...) asparagine; by host
Glycosylation125N-linked (GlcNAc...) asparagine; by host
Glycosylation178N-linked (GlcNAc...) asparagine; by host
Glycosylation223N-linked (GlcNAc...) asparagine; by host
ChainPRO_5023484997256-489Glycoprotein G2
Disulfide bond275↔288
Disulfide bond297↔306
Disulfide bond360↔381
Glycosylation361N-linked (GlcNAc...) asparagine; by host
Glycosylation369N-linked (GlcNAc...) asparagine; by host
Glycosylation386N-linked (GlcNAc...) asparagine; by host
Glycosylation391N-linked (GlcNAc...) asparagine; by host

Post-translational modification

Pre-glycoprotein polyprotein GP complex

Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleavage by signal peptidase.

Keywords

Interaction

Subunit

Glycoprotein G1

Homotrimer; disulfide-linked. In pre-fusion state, G1 homotrimers bind G2 homotrimers via ionic interactions. Part of the GP complex (GP-C) together with glycoprotein G2 and the stable signal peptide. The GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions may induce virion budding.

Glycoprotein G2

Homotrimer. Interacts with the stable signal peptide. In pre-fusion state, G2 homotrimers bind G1 homotrimers via ionic interactions. Part of the GP complex (GP-C) together with glycoprotein G1 and the stable signal peptide. Acidification in the endosome triggers rearrangements, which ultimately leads to a 6 helix bundle formed by the two heptad repeat domains (HR1 and HR2) in post-fusion state. The GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions may induce virion budding.

Stable signal peptide

Interacts with glycoprotein G2. Part of the GP complex (GP-C) together with glycoprotein G1 and glycoprotein G2. The GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions may induce virion budding.

Structure

3D structure databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region254-290Fusion
Region291-359HR1
Region364-427HR2

Domain

Glycoprotein G2

Contains 1 fusion peptide at the N-terminus, 2 heptad repeats domains HR1 and HR2 and, at the C-terminus, a cytoplasmic domain that plays a role in ER location. Also contains a zinc-binding domain that allows SSP retention in the GPC complex by accepting a cysteine from SSP as the fourth ligand.

Stable signal peptide

The N-terminus is localized at the extracellular side of the GP-C, with a part embedded in the membrane probably.

Sequence similarities

Belongs to the arenaviridae GPC protein family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    489
  • Mass (Da)
    56,064
  • Last updated
    2018-09-12 v1
  • Checksum
    BEF31829B0750AEA
MGQLVSFFSEIPNIIHEAINIALITVSLIALLKGMVNLWKSGLFQLIVFLILAGKSCSFKIGRSTELQNITFNMLEVLKDHPTSCMVNQSFYYILENSNATWGLEVSVTDISLLMAEHDRPVMGNLSNCVHPSVRHGAKLTGLLEWVFRGLKYDFVNYPRPLCQKFNNTVNETRVQINMTDGVGSHGFKETIIQRLAVLFGSRLMFSNEQGNKVTKRYLLIRNVTWSGQCQGNHINSLHLMMANTGRAFGMRQLQGIFTWTITDAAGNDMPGGYCLERWMLVASDLRCFGNTALAKCNLNHDSEFCDMLKLFEFNKKAIETLNDNTKNKVNLLTHSINALISDNLLMKNRLKELLDTPYCNYTKFWYVNHTSTGTHSLPRCWMVKNNSYLNESEFRNDWILESDHLLSEMLNREYLERQGKTPITLVDLCFWSTLFFTTTLFLHLIGFPTHRHIRGESCPLPHRLNSRGGCRCGKYPDLKKPTTWHKRH

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MF317490
EMBL· GenBank· DDBJ
AUD40058.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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