NP_694870.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Related Accession #
NCBI Official Full Name
glycoprotein
NCBI Protein Information
glycoprotein
UniProt Protein Name
Pre-glycoprotein polyprotein GP complex
UniProt Synonym Gene Names
UniProt Entry Name
GLYC_LASSJ
UniProt Comments for LASVsSgp2
Function: Stable signal peptide (SSP) is cleaved but is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational cleavage of GP1 and GP2, glycoprotein transport to the cell plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion. Ref.6 Ref.8Glycoprotein G1 mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis. Ref.6 Ref.8Glycoprotein G2 is a 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 irreversable conformational changes induced upon acidification in the endosome
By similarity. Ref.6 Ref.8
Subunit structure: Glycoprotein G1 is a homotrimer; disulfide-linked. Glycoprotein G2 is a homotrimer. GP2 homotrimers bind with GP1 homotrimers to form, with the stable signal peptide, the GP-complex. Interacts with host DAG1. In infected cell, this interaction reduces the expression of functional host DAG1. GP-complex interacts with protein Z, which interacts with ribonucleocapsid; these interactions supposely induce virion budding. Ref.4 Ref.6
Subcellular location: Stable signal peptide: Virion membrane; Multi-pass membrane protein
Potential. Host cell membrane; Multi-pass membrane protein
Potential. Glycoprotein G2: Virion 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 binds to the SSP.
Post-translational modification: Cleavage by signal peptidase releases the stable signal peptide, which stays associated to the glycoprotein complex through interaction with glycoprotein G2.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
By similarity. Ref.3
Sequence similarities: Belongs to the arenaviridae GPC protein family.
Research Articles on LASVsSgp2
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