Trimeric GP1,2 complexes form the virion surface spikes and mediate the viral entry processes, with GP1 acting as the receptor-binding subunit and GP2 as the membrane fusion subunit. At later times of infection, down-regulates the expression of various host cell surface molecules that are essential for immune surveillance and cell adhesion (PubMed:11836430). Down-modulates several integrins including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1 (PubMed:11112476). This decrease in cell adhesion molecules may lead to cell detachment, contributing to the disruption of blood vessel integrity and hemorrhages developed during infection (cytotoxicity) (Probable). Interacts with host TLR4 and thereby stimulates the differentiation and activation of monocytes leading to bystander death of T-lymphocytes (PubMed:28542576). Down-regulates as well the function of host natural killer cells (PubMed:30013549). Counteracts the antiviral effect of host BST2/tetherin that restricts release of progeny virions from infected cells (PubMed:26516900, PubMed:27707924, PubMed:29669839). However, cooperates with VP40 and host BST2 to activate canonical NF-kappa-B pathway in a manner dependent on neddylation (PubMed:28878074). Functions as a decoy for anti-GP1,2 antibodies thereby contributing to viral immune evasion. Interacts and activates host macrophages and dendritic cells inducing up-regulation of cytokine transcription. This effect is mediated throught activation of host TLR4. Responsible for binding to the receptor(s) on target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as cofactors for virus entry into dendritic cells (DCs) and endothelial cells (PubMed:16051836). Binding to the macrophage specific lectin CLEC10A also seems to enhance virus infectivity (By similarity). Interaction with FOLR1/folate receptor alpha may be a cofactor for virus entry in some cell types, although results are contradictory. Members of the Tyro3 receptor tyrosine kinase family also seem to be cell entry factors in filovirus infection (By similarity). Once attached, the virions are internalized through clathrin-dependent endocytosis and/or macropinocytosis. After internalization of the virus into the endosomes of the host cell, proteolysis of GP1 by two cysteine proteases, CTSB/cathepsin B and CTSL/cathepsin L removes the glycan cap and allows GP1 binding to the host entry receptor NPC1 (PubMed:21866103, PubMed:32040508). NPC1-binding, Ca(2+) and acidic pH induce a conformational change of GP2, which unmasks its fusion peptide and permit membranes fusion (PubMed:21866103, PubMed:22031933, PubMed:32040508). 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. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in GP2, releasing the fusion hydrophobic peptide. Homotrimer; each monomer consists of a GP1 and a GP2 subunit linked by disulfide bonds. The resulting peplomers (GP1,2) protrude from the virus surface as spikes. Interacts with host integrin alpha-V/ITGAV (PubMed:15596847). Interacts with host CLEC10A (PubMed:14990712). Binds also to host CD209 and CLEC4M/DC-SIGN(R) (PubMed:12050398, PubMed:12504546). Interacts with host FOLR1 (PubMed:11461707). Interacts with BST2; this interaction inhibits the antiviral effect of BST2 and this allows viral release from infected cells (PubMed:27707924). Interacts with host FCN1; this interaction enhances viral entry (PubMed:26984723). Interacts with host TLR4; this interaction induces T-lymphocyte death (PubMed:28542576). Interacts with host entry receptor NPC1. GP1 and GP2delta are part of GP1,2delta soluble complexes released by ectodomain shedding. In the cell, localizes to the plasma membrane lipid rafts, which probably represent the assembly and budding site. GP1 is not anchored to the viral envelope, but forms a disulfid-linked complex with the extravirion surface GP2 (PubMed:9576958). In the cell, both GP1 and GP2 localize to the plasma membrane lipid rafts, which probably represent the assembly and budding site (PubMed:11877482). GP1 can also be shed after proteolytic processing. GP2-delta bound to GP1 (GP1,2-delta) is produced by proteolytic cleavage of GP1,2 by host ADAM17 and shed by the virus. The mucin-like region seems to be involved in the cytotoxic function. This region is also involved in binding to human CLEC10A. The coiled coil regions play a role in oligomerization and fusion activity. The signal peptide region modulates GP's high mannose glycosylation, thereby determining the efficiency of the interactions with DC-SIGN(R). N-glycosylated. Glycosylated; glycosylation is essential for the activation of dendritic cells and macrophages. O-glycosylated in the mucin-like region. Palmitoylation is not required for its function. Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into GP1 and GP2 by host cell furin in the trans Golgi, and maybe by other host proteases, to yield the mature GP1 and GP2 proteins (PubMed:9576958, PubMed:9614872) (PubMed:9882347). The cleavage site corresponds to the furin optimal cleavage sequence [KR]-X-[KR]-R (PubMed:9576958). This cleavage does not seem to be required for function (PubMed:9576958). After the internalization of the virus into cell endosomes, GP1 C-terminus is removed by the endosomal proteases cathepsin B, cathepsin L, or both, leaving a 19-kDa N-terminal fragment which is further digested by cathepsin B (PubMed:16571833). This cleaved 19-kDa GP1 can then bind to the host entry receptor NPC1 (PubMed:21866103). Proteolytic processing of GP1,2 by host ADAM17 can remove the transmembrane anchor of GP2 and leads to shedding of complexes consisting in GP1 and truncated GP2 (GP1,2delta) (PubMed:15103332). Partially edited. RNA editing at this position consists of an insertion of one or two adenine nucleotides. The sequence displayed here is the full-length transmembrane glycoprotein GP, derived from the +1A edited RNA. The unedited RNA gives rise to the small secreted glycoprotein sGP (AC P60170), the +2A edited RNA gives rise to the super small secreted glycoprotein ssGP (AC Q9YMG2). Filoviruses entry requires functional lipid rafts at the host cell surface. Essential for infectivity, as it is the sole viral protein expressed at the virion surface. Belongs to the filoviruses glycoprotein family.