| IED ID | IndEnz0002005236 |
| Enzyme Type ID | protease005236 |
| Protein Name |
Fusion glycoprotein F0 Protein F Cleaved into: Fusion glycoprotein F2; Fusion glycoprotein F1 |
| Gene Name | F |
| Organism | Human metapneumovirus (strain CAN97-83) (HMPV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Negarnaviricota Haploviricotina Monjiviricetes Mononegavirales Pneumoviridae Metapneumovirus Human metapneumovirus Human metapneumovirus (strain CAN97-83) (HMPV) |
| Enzyme Sequence | MSWKVVIIFSLLITPQHGLKESYLEESCSTITEGYLSVLRTGWYTNVFTLEVGDVENLTCSDGPSLIKTELDLTKSALRELKTVSADQLAREEQIENPRQSRFVLGAIALGVATAAAVTAGVAIAKTIRLESEVTAIKNALKTTNEAVSTLGNGVRVLATAVRELKDFVSKNLTRAINKNKCDIDDLKMAVSFSQFNRRFLNVVRQFSDNAGITPAISLDLMTDAELARAVSNMPTSAGQIKLMLENRAMVRRKGFGILIGVYGSSVIYMVQLPIFGVIDTPCWIVKAAPSCSGKKGNYACLLREDQGWYCQNAGSTVYYPNEKDCETRGDHVFCDTAAGINVAEQSKECNINISTTNYPCKVSTGRHPISMVALSPLGALVACYKGVSCSIGSNRVGIIKQLNKGCSYITNQDADTVTIDNTVYQLSKVEGEQHVIKGRPVSSSFDPIKFPEDQFNVALDQVFENIENSQALVDQSNRILSSAEKGNTGFIIVIILIAVLGSSMILVSIFIIIKKTKKPTGAPPELSGVTNNGFIPHS |
| Enzyme Length | 539 |
| Uniprot Accession Number | Q6WB98 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved to give rise to the mature F1 and F2 fusion glycoproteins. {ECO:0000250|UniProtKB:P03420}.; FUNCTION: [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. {ECO:0000250|UniProtKB:P03420}.; FUNCTION: [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). {ECO:0000250|UniProtKB:P03420, ECO:0000269|PubMed:22238303}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Disulfide bond (7); Glycosylation (3); Motif (1); Region (2); Signal peptide (1); Transmembrane (1) |
| Keywords | Cleavage on pair of basic residues;Disulfide bond;Fusion of virus membrane with host cell membrane;Fusion of virus membrane with host membrane;Glycoprotein;Host cell membrane;Host membrane;Membrane;Reference proteome;Signal;Transmembrane;Transmembrane helix;Viral envelope protein;Viral penetration into host cytoplasm;Virion;Virus entry into host cell |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein. Host cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Fusion glycoprotein F0]: The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed. {ECO:0000250|UniProtKB:P03420}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 329..331; /note=Cell attachment site; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 58,477 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |