Q6WB98 · FUS_HMPVC
- ProteinFusion glycoprotein F0
- GeneF
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids539 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Fusion glycoprotein F0
Inactive precursor that is cleaved to give rise to the mature F1 and F2 fusion glycoproteins.
Fusion glycoprotein F1
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 plasma cell membrane fusion, the coiled coil regions 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 cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs at the plasma or endosomal membrane. The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate.
Fusion glycoprotein F2
Major determinant of the species specificity of RSV infection (By similarity).
The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate (PubMed:22238303).
The trimer of F1-F2 (F protein) also facilitates the attachment to host cell by binding to host heparan sulfate (PubMed:22238303).
Miscellaneous
The cleavage peptide sequence for the hMPV F protein (RQSR) varies from the one described for other pneumoviruses, and differs from the furin protease motif (R/K-X-R/K-R).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell plasma membrane | |
Cellular Component | membrane | |
Cellular Component | viral envelope | |
Cellular Component | virion membrane | |
Biological Process | fusion of virus membrane with host plasma membrane | |
Biological Process | symbiont entry into host cell |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameFusion glycoprotein F0
- Short namesProtein F
- Cleaved into 2 chains
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Haploviricotina > Monjiviricetes > Mononegavirales > Pneumoviridae > Metapneumovirus > Metapneumovirus hominis
- Virus hosts
Accessions
- Primary accessionQ6WB98
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Virion membrane ; Single-pass type I membrane protein
Host cell membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 492-512 | Helical | ||||
Sequence: IIVIILIAVLGSSMILVSIFI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MSWKVVIIFSLLITPQHG | ||||||
Chain | PRO_0000394806 | 19-539 | Fusion glycoprotein F0 | |||
Sequence: LKESYLEESCSTITEGYLSVLRTGWYTNVFTLEVGDVENLTCSDGPSLIKTELDLTKSALRELKTVSADQLAREEQIENPRQSRFVLGAIALGVATAAAVTAGVAIAKTIRLESEVTAIKNALKTTNEAVSTLGNGVRVLATAVRELKDFVSKNLTRAINKNKCDIDDLKMAVSFSQFNRRFLNVVRQFSDNAGITPAISLDLMTDAELARAVSNMPTSAGQIKLMLENRAMVRRKGFGILIGVYGSSVIYMVQLPIFGVIDTPCWIVKAAPSCSGKKGNYACLLREDQGWYCQNAGSTVYYPNEKDCETRGDHVFCDTAAGINVAEQSKECNINISTTNYPCKVSTGRHPISMVALSPLGALVACYKGVSCSIGSNRVGIIKQLNKGCSYITNQDADTVTIDNTVYQLSKVEGEQHVIKGRPVSSSFDPIKFPEDQFNVALDQVFENIENSQALVDQSNRILSSAEKGNTGFIIVIILIAVLGSSMILVSIFIIIKKTKKPTGAPPELSGVTNNGFIPHS | ||||||
Chain | PRO_0000394807 | 20-102 | Fusion glycoprotein F2 | |||
Sequence: KESYLEESCSTITEGYLSVLRTGWYTNVFTLEVGDVENLTCSDGPSLIKTELDLTKSALRELKTVSADQLAREEQIENPRQSR | ||||||
Disulfide bond | 28↔407 | Interchain (between F2 and F1 chains) | ||||
Sequence: CSTITEGYLSVLRTGWYTNVFTLEVGDVENLTCSDGPSLIKTELDLTKSALRELKTVSADQLAREEQIENPRQSRFVLGAIALGVATAAAVTAGVAIAKTIRLESEVTAIKNALKTTNEAVSTLGNGVRVLATAVRELKDFVSKNLTRAINKNKCDIDDLKMAVSFSQFNRRFLNVVRQFSDNAGITPAISLDLMTDAELARAVSNMPTSAGQIKLMLENRAMVRRKGFGILIGVYGSSVIYMVQLPIFGVIDTPCWIVKAAPSCSGKKGNYACLLREDQGWYCQNAGSTVYYPNEKDCETRGDHVFCDTAAGINVAEQSKECNINISTTNYPCKVSTGRHPISMVALSPLGALVACYKGVSCSIGSNRVGIIKQLNKGC | ||||||
Glycosylation | 57 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 60↔182 | Interchain (between F2 and F1 chains) | ||||
Sequence: CSDGPSLIKTELDLTKSALRELKTVSADQLAREEQIENPRQSRFVLGAIALGVATAAAVTAGVAIAKTIRLESEVTAIKNALKTTNEAVSTLGNGVRVLATAVRELKDFVSKNLTRAINKNKC | ||||||
Chain | PRO_0000394808 | 103-539 | Fusion glycoprotein F1 | |||
Sequence: FVLGAIALGVATAAAVTAGVAIAKTIRLESEVTAIKNALKTTNEAVSTLGNGVRVLATAVRELKDFVSKNLTRAINKNKCDIDDLKMAVSFSQFNRRFLNVVRQFSDNAGITPAISLDLMTDAELARAVSNMPTSAGQIKLMLENRAMVRRKGFGILIGVYGSSVIYMVQLPIFGVIDTPCWIVKAAPSCSGKKGNYACLLREDQGWYCQNAGSTVYYPNEKDCETRGDHVFCDTAAGINVAEQSKECNINISTTNYPCKVSTGRHPISMVALSPLGALVACYKGVSCSIGSNRVGIIKQLNKGCSYITNQDADTVTIDNTVYQLSKVEGEQHVIKGRPVSSSFDPIKFPEDQFNVALDQVFENIENSQALVDQSNRILSSAEKGNTGFIIVIILIAVLGSSMILVSIFIIIKKTKKPTGAPPELSGVTNNGFIPHS | ||||||
Glycosylation | 172 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 283↔311 | |||||
Sequence: CWIVKAAPSCSGKKGNYACLLREDQGWYC | ||||||
Disulfide bond | 292↔301 | |||||
Sequence: CSGKKGNYAC | ||||||
Disulfide bond | 326↔335 | |||||
Sequence: CETRGDHVFC | ||||||
Disulfide bond | 350↔361 | |||||
Sequence: CNINISTTNYPC | ||||||
Glycosylation | 353 | N-linked (GlcNAc...) asparagine; by host | ||||
Sequence: N | ||||||
Disulfide bond | 384↔390 | |||||
Sequence: CYKGVSC |
Post-translational modification
Fusion glycoprotein F0
The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed.
Keywords
- PTM
PTM databases
Interaction
Subunit
Fusion glycoprotein F1
Homotrimer. Heterodimer with fusion protein F2; disulfide-linked. As a heterodimer with F2, interacts with host heparan sulfate (PubMed:22238303).
As a heterodimer with F2, interacts with host integrin ITGAV/ITGB1 (PubMed:19164533).
Part of a complex composed of F1, F2 and G glycoproteins (By similarity).
As a heterodimer with F2, interacts with host integrin ITGAV/ITGB1 (PubMed:19164533).
Part of a complex composed of F1, F2 and G glycoproteins (By similarity).
Fusion glycoprotein F2
Homotrimer. Heterodimer with fusion protein F1; disulfide-linked. As a heterodimer with F1, interacts with host heparan sulfate (PubMed:22238303).
As a heterodimer with F2, interacts with host integrin ITGAV/ITGB1 (PubMed:19164533).
Part of a complex composed of F1, F2 and G glycoproteins (By similarity).
As a heterodimer with F2, interacts with host integrin ITGAV/ITGB1 (PubMed:19164533).
Part of a complex composed of F1, F2 and G glycoproteins (By similarity).
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 103-127 | Fusion peptide | ||||
Sequence: FVLGAIALGVATAAAVTAGVAIAKT | ||||||
Motif | 329-331 | Cell attachment site | ||||
Sequence: RGD | ||||||
Region | 520-539 | Disordered | ||||
Sequence: PTGAPPELSGVTNNGFIPHS |
Domain
Fusion glycoprotein F0
The N-terminus is a hydrophobic fusion peptide that inserts into the target host membrane (By similarity).
It is buried in the center of the trimer cavity before cleavage. The coiled coil (heptad repeat) regions are probably involved in homotrimerization, heterodimerization and in the formation of a fusion-active hairpin structure (By similarity).
It is buried in the center of the trimer cavity before cleavage. The coiled coil (heptad repeat) regions are probably involved in homotrimerization, heterodimerization and in the formation of a fusion-active hairpin structure (By similarity).
Fusion glycoprotein F1
The N-terminus is a hydrophobic fusion peptide that inserts into the target host membrane (By similarity).
It is buried in the center of the trimer cavity before cleavage. The coiled coil (heptad repeat) regions are probably involved in homotrimerization, heterodimerization and in the formation of a fusion-active hairpin structure (By similarity).
It is buried in the center of the trimer cavity before cleavage. The coiled coil (heptad repeat) regions are probably involved in homotrimerization, heterodimerization and in the formation of a fusion-active hairpin structure (By similarity).
Sequence similarities
Belongs to the paramyxoviruses fusion glycoprotein family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length539
- Mass (Da)58,477
- Last updated2004-07-05 v1
- Checksum2987E611786A64BA
Keywords
- Technical term