Reviewed
Homo Sapiens (Human) [TaxID: 9606]
Env
♦Envelope glycoprotein (Env polyprotein) [Cleaved into: Surface protein (SU)
♦ Transmembrane protein (TM)
♦ R-peptide]
♦ Transmembrane protein (TM)
♦ R-peptide]
Xenotropic MuLV-related Virus (isolate VP35) (XMRV)
Viruses> Retro-transcribing Viruses> Retroviridae> Orthoretrovirinae> Gammaretrovirus> Unclassified Gammaretrovirus> Murine Leukemia-related Retroviruses> XMRV-related Viruses> Xenotropic MuLV-related Virus> Xenotropic MuLV-related Virus (isolate VP35) (XMRV)
Not Available
Various pathway(s) in which protein is involved
Not Available
Not Available
MESPAFSKPLKDKINPWGPLIIMGILVRAGASVQRDSPHQVFNVTWKITNLMTGQTANATSLLGTMTDTFPKLYFDLCDLVGDNWDDPEPDIGDGCRSPG
GRKRTRLYDFYVCPGHTVLTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKGQGPCFDSSVGSGSIQGATPGGRCNPLVLEFTDAGKRAS
WDAPKTWGLRLYRSTGADPVTLFSLTRQVLNVGPRVPIGPNPVITEQLPPSQPVQIMLPRPPRPPPSGAASMVPGAPPPSQQPGTGDRLLNLVEGAYQAL
NLTSPDKTQECWLCLVSGPPYYEGVAVLGTYSNHTSAPANCSVTSQHKLTLSEVTGQGLCIGAVPKTHQALCNTTQKTSDGSYYLASPAGTIWACSTGLT
PCLSTTVLNLTTDYCVLVELWPKVTYHSPNYVYGQFGKKTKYKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATKQFEQLQAAIHTDLGALEKSVSA
LEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKKECCFYADHTGVVRDSMAKLRERLNQRQKLFESGQGWFEGLFNRSPWFTTLISTIMGPLIVLLLIL
LFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKSIDPEEVESRE
GRKRTRLYDFYVCPGHTVLTGCGGPREGYCGKWGCETTGQAYWKPSSSWDLISLKRGNTPKGQGPCFDSSVGSGSIQGATPGGRCNPLVLEFTDAGKRAS
WDAPKTWGLRLYRSTGADPVTLFSLTRQVLNVGPRVPIGPNPVITEQLPPSQPVQIMLPRPPRPPPSGAASMVPGAPPPSQQPGTGDRLLNLVEGAYQAL
NLTSPDKTQECWLCLVSGPPYYEGVAVLGTYSNHTSAPANCSVTSQHKLTLSEVTGQGLCIGAVPKTHQALCNTTQKTSDGSYYLASPAGTIWACSTGLT
PCLSTTVLNLTTDYCVLVELWPKVTYHSPNYVYGQFGKKTKYKREPVSLTLALLLGGLTMGGIAAGVGTGTTALVATKQFEQLQAAIHTDLGALEKSVSA
LEKSLTSLSEVVLQNRRGLDLLFLKEGGLCAALKKECCFYADHTGVVRDSMAKLRERLNQRQKLFESGQGWFEGLFNRSPWFTTLISTIMGPLIVLLLIL
LFGPCILNRLVQFVKDRISVVQALVLTQQYHQLKSIDPEEVESRE
645
Not Available
Not Available
21-03-2006
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 |
|---|---|---|
♦The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction activates a thiol in a CXXC motif of the C-terminal domain, where the other Cys residue participates in the formation of the intersubunit disulfide. The activated thiol will attack the disulfide and cause its isomerization into a disulfide isomer within the motif. This leads to SU displacement and TM refolding, and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).
♦ The transmembrane protein (TM) 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. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
♦ The transmembrane protein (TM) 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. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
Not Available
♦ Transmembrane protein: Virion membrane
♦ Single-pass type I membrane protein . Host cell membrane
♦ Single-pass type I membrane protein .
♦ Surface protein: Virion membrane
♦ Peripheral membrane protein. Host cell membrane
♦ Peripheral membrane protein . Note=The surface protein is not anchored to the viral envelope, but associates with the virion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). .
♦ R-peptide: Host cell membrane
♦ Peripheral membrane protein. Note=The R-peptide is membrane-associated through its palmitate. .
♦ Single-pass type I membrane protein . Host cell membrane
♦ Single-pass type I membrane protein .
♦ Surface protein: Virion membrane
♦ Peripheral membrane protein. Host cell membrane
♦ Peripheral membrane protein . Note=The surface protein is not anchored to the viral envelope, but associates with the virion surface through its binding to TM. Both proteins are thought to be concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). .
♦ R-peptide: Host cell membrane
♦ Peripheral membrane protein. Note=The R-peptide is membrane-associated through its palmitate. .
Not Available
MOTIF 311 314 CXXC. ; MOTIF 530 538 CX6CC. ; MOTIF 630 633 YXXL motif; contains endocytosis signal.
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