Function: The stable signal peptide (SSP) is cleaved and functions as a signal peptide. In addition, it is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion
By similarity.Glycoprotein G1 mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis
By similarity.Glycoprotein G2 is a viral fusion protein. Membrane fusion is mediated by conformational changes induced upon acidification in the endosome
Potential.
Subunit structure: Glycoprotein G1 is a homotetramer; disulfide-linked
Potential. Glycoprotein G2 is a homotetramer
Potential. SSP is a homodimer; disulfide-linked. GP2 homotetramers bind through ionic interactions with GP1 homotetramers to form, with the stable signal peptide, the GP complex. The GP-C polyprotein interacts with host protease MBTPS1/SKI-1; this results in polyprotein processing
By similarity.
Subcellular location: Stable signal peptide: Virion membrane; Multi-pass membrane protein
Potential. Host endoplasmic reticulum membrane; Multi-pass membrane protein
Potential. Host Golgi apparatus membrane; Multi-pass membrane protein
Potential. Host cell membrane; Multi-pass membrane protein
Potential. Glycoprotein G1: Virion membrane; Peripheral membrane protein
Potential. Host endoplasmic reticulum membrane; Peripheral membrane protein
Potential. Host Golgi apparatus membrane; Peripheral membrane protein
Potential. Host cell membrane; Peripheral membrane protein
Potential. Glycoprotein G2: Virion membrane; Single-pass membrane protein
Potential. Host endoplasmic reticulum membrane; Single-pass membrane protein
Potential. Host Golgi apparatus membrane; Single-pass membrane protein
Potential. Host cell membrane; Single-pass membrane protein
Potential. 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
By similarity.
Domain: The cytoplasmic domain of GP2 plays a role in ER location and binds to the SSP.
Post-translational modification: The SSP remains stably associated with the GP complex following cleavage by signal peptidase and plays crucial roles in the trafficking of GP through the secretory pathway
By similarity.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.
Sequence similarities: Belongs to the arenaviridae GPC protein family.
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