Reviewed
Chlorocebus Aethiops (Green Monkey) (Cercopithecus Aethiops) [TaxID: 9534]; Homo Sapiens (Human) [TaxID: 9606]; Rousettus Aegyptiacus (Egyptian Rousette) (Egyptian Fruit Bat) [TaxID: 9407]
GP
♦Envelope glycoprotein (GP1,2) (GP) (Virion spike glycoprotein) [Cleaved into: GP1
♦ GP2]
♦ GP2]
Lake Victoria Marburgvirus (strain Ozolin-75) (MARV) (Marburg Virus (strain South Africa/Ozolin/1975))
Viruses> SsRNA Viruses> SsRNA Negative-strand Viruses> Mononegavirales> Filoviridae> Marburgvirus> Marburg Marburgvirus> Lake Victoria Marburgvirus (strain Ozolin-75) (MARV) (Marburg Virus (strain South Africa/Ozolin/1975))
9448698 ;
Various pathway(s) in which protein is involved
Not Available
Not Available
MRTTCLFISLILIQGIKTLPILEIASNDQPQNVDSVCSGTLQKTEDVHLMGFTLSGQKVADSPLEASKRWAFRTGVPPKNVEYTEGEEAKTCYNISVTDP
SGKSLLLDPPTNVRDYPKCKTIHHIQGQNPHAQGIALHLWGAFFLYDRIASTTMYRGKVFTEGNIAAMIVNKTVHKMIFSRQGQGYRHMNLTSTNKYWTS
SNGTQTNDTGCFGTLHEYNSTKNQTCAPSKTPPPPPTARPEIKPTSTPTDATRLNTTNPNSDDEDLTTSGSGSGEQELYTTSDAVTKQGLSSTMPPTPSP
QPGTPQQGGNNTNHSQDATTELDNTNTTAQPPTPSHNTTTISTNNTSKHNLSTLSAPPQNTTNPNTQSMATENEKTSAPPKATLPPTENPTTEKSTNNTK
SPTTMEPNTTNGHFTSPSSTPNSTTQHLIYFRRKRSILWREGDMFPFLDGLINAPIDFDPVPNTKTIFDESSSSGASTEEDQHASSNISLTLSYLPHTSG
NTAYSGENENDCDAELRIWSVQEDDLAAGLSWIPFFGPGIEGLYTAGLIKNQNNLVCRLRRLANQTAKSLELLLRVTTEERTFSLINRHAIDFLLTRWGG
TCKVLGPDCCIGIEDLSRNISEQIDQIKKDEQKEGTGWGLGGKWWTSDWGVLTNLGILLLLSIAVLIALSCICRIFTKYIG
SGKSLLLDPPTNVRDYPKCKTIHHIQGQNPHAQGIALHLWGAFFLYDRIASTTMYRGKVFTEGNIAAMIVNKTVHKMIFSRQGQGYRHMNLTSTNKYWTS
SNGTQTNDTGCFGTLHEYNSTKNQTCAPSKTPPPPPTARPEIKPTSTPTDATRLNTTNPNSDDEDLTTSGSGSGEQELYTTSDAVTKQGLSSTMPPTPSP
QPGTPQQGGNNTNHSQDATTELDNTNTTAQPPTPSHNTTTISTNNTSKHNLSTLSAPPQNTTNPNTQSMATENEKTSAPPKATLPPTENPTTEKSTNNTK
SPTTMEPNTTNGHFTSPSSTPNSTTQHLIYFRRKRSILWREGDMFPFLDGLINAPIDFDPVPNTKTIFDESSSSGASTEEDQHASSNISLTLSYLPHTSG
NTAYSGENENDCDAELRIWSVQEDDLAAGLSWIPFFGPGIEGLYTAGLIKNQNNLVCRLRRLANQTAKSLELLLRVTTEERTFSLINRHAIDFLLTRWGG
TCKVLGPDCCIGIEDLSRNISEQIDQIKKDEQKEGTGWGLGGKWWTSDWGVLTNLGILLLLSIAVLIALSCICRIFTKYIG
681
Not Available
Not Available
05-07-2004
Inferred from homology
| Amino Acid | Count | % Frequency | Amino Acid | Count | % Frequency |
|---|---|---|---|---|---|
| Alanine (A) | Leucine (L) | ||||
| Arginine (R) | Lysine (K) | ||||
| Asparagine (N) | Methionine (M) | ||||
| Aspartic Acid (D) | Phenylalanine (F) | ||||
| Cysteine (C) | Proline (P) | ||||
| Glutamine (Q) | Serine (S) | ||||
| Glutamic Acid (E) | Threonine (T) | ||||
| Glycine (G) | Tryptophan (W) | ||||
| Histidine (H) | Tyrosine (Y) | ||||
| Isoleucine (I) | Valine (V) |
| % Number of Residues in Helices | % Number of Residues in Strands | % Number of Residues in Coils |
|---|---|---|
♦GP1 is 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 the host cell. Binding to CD209 and CLEC4M, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses, facilitate infection of macrophages and endothelial cells. These interactions not only facilitate virus cell entry, but also allow capture of viral particles by DCs and subsequent transmission to susceptible cells without DCs infection (trans infection) (By similarity).
♦ GP2 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 (By similarity).
♦ GP2 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 (By similarity).
Not Available
♦ GP2: Virion membrane
♦ Single-pass type I membrane protein . Host cell membrane
♦ Single-pass type I membrane protein . Note=In the cell, localizes to the plasma membrane lipid rafts, which probably represent the assembly and budding site. .
♦ GP1: Virion membrane
♦ Peripheral membrane protein . Host cell membrane
♦ Peripheral membrane protein . Note=GP1 is not anchored to the viral envelope, but forms a disulfid-linked complex with the extravirion surface GP2. In the cell, both GP1 and GP2 localize to the plasma membrane lipid rafts, which probably represent the assembly and budding site. GP1 can also be shed after proteolytic processing. .
♦ Single-pass type I membrane protein . Host cell membrane
♦ Single-pass type I membrane protein . Note=In the cell, localizes to the plasma membrane lipid rafts, which probably represent the assembly and budding site. .
♦ GP1: Virion membrane
♦ Peripheral membrane protein . Host cell membrane
♦ Peripheral membrane protein . Note=GP1 is not anchored to the viral envelope, but forms a disulfid-linked complex with the extravirion surface GP2. In the cell, both GP1 and GP2 localize to the plasma membrane lipid rafts, which probably represent the assembly and budding site. GP1 can also be shed after proteolytic processing. .
Not Available
Not Available
Predicted/Modelled
Not Available
Not Available
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.
Not Available
- Million Molecules
Best 20 Hit molecules
Not Available