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O36634 (FUS_HRSVB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fusion glycoprotein F0

Short name=Protein F

Cleaved into the following 2 chains:

  1. Fusion glycoprotein F2
  2. Fusion glycoprotein F1
Gene names
Name:F
OrganismHuman respiratory syncytial virus B (strain B1) [Reference proteome]
Taxonomic identifier79692 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaePneumovirinaePneumovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 heptad repeat (HR) 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 plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (protein F) interacts with glycoprotein G at the virion surface. Upon binding of G to heparan sulfate, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between host cell and virion membranes. Notably, RSV fusion protein is able to interact directly with heparan sulfate and therefore actively participates in virus attachment. Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity. Later in infection, proteins F expressed at the plasma membrane of infected cells mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis. The fusion protein is also able to trigger p53-dependent apoptosis By similarity.

Subunit structure

Homotrimer of disulfide-linked F1-F2 By similarity. Interacts with glycoprotein G. Interacts with host RHOA; this interaction facilitates virus-induced syncytium formation By similarity.

Subcellular location

Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass membrane protein By similarity.

Post-translational modification

The F glycoprotein is synthesized as a inactive precursor that is heavily N-glycosylated and processed by host cell furin in the Golgi to yield the mature F1 and F2 proteins. The cleavage site between F1 and F2 requires the minimal sequence [KR]-X-[KR]-R.

Sequence similarities

Belongs to the paramyxoviruses fusion glycoprotein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 574549Fusion glycoprotein F0
PRO_0000390376
Chain26 – 136111Fusion glycoprotein F2
PRO_0000390377
Chain137 – 574438Fusion glycoprotein F1
PRO_0000390378

Regions

Transmembrane530 – 55021Helical; Potential
Coiled coil73 – 10028 Potential

Amino acid modifications

Glycosylation271N-linked (GlcNAc...); by host Potential
Glycosylation701N-linked (GlcNAc...); by host Potential
Glycosylation1161N-linked (GlcNAc...); by host Potential
Glycosylation1201N-linked (GlcNAc...); by host Potential
Glycosylation1261N-linked (GlcNAc...); by host Potential
Glycosylation5001N-linked (GlcNAc...); by host Potential
Disulfide bond69 ↔ 212Interchain (between F2 and F1 chains) By similarity
Disulfide bond358 ↔ 367 By similarity
Disulfide bond382 ↔ 393 By similarity

Sequences

Sequence LengthMass (Da)Tools
O36634 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 29A127B128BF5E92

FASTA57463,710
        10         20         30         40         50         60 
MELLIHRLSA IFLTLAINAL YLTSSQNITE EFYQSTCSAV SRGYFSALRT GWYTSVITIE 

        70         80         90        100        110        120 
LSNIKETKCN GTDTKVKLIK QELDKYKNAV TELQLLMQNT PAANNRARRE APQYMNYTIN 

       130        140        150        160        170        180 
TTKNLNVSIS KKRKRRFLGF LLGVGSAIAS GIAVSKVLHL EGEVNKIKNA LLSTNKAVVS 

       190        200        210        220        230        240 
LSNGVSVLTS KVLDLKNYIN NQLLPIVNQQ SCRISNIETV IEFQQKNSRL LEINREFSVN 

       250        260        270        280        290        300 
AGVTTPLSTY MLTNSELLSL INDMPITNDQ KKLMSSNVQI VRQQSYSIMS IIKEEVLAYV 

       310        320        330        340        350        360 
VQLPIYGVID TPCWKLHTSP LCTTNIKEGS NICLTRTDRG WYCDNAGSVS FFPQADTCKV 

       370        380        390        400        410        420 
QSNRVFCDTM NSLTLPSEVS LCNTDIFNSK YDCKIMTSKT DISSSVITSL GAIVSCYGKT 

       430        440        450        460        470        480 
KCTASNKNRG IIKTFSNGCD YVSNKGVDTV SVGNTLYYVN KLEGKNLYVK GEPIINYYDP 

       490        500        510        520        530        540 
LVFPSDEFDA SISQVNEKIN QSLAFIRRSD ELLHNVNTGK STTNIMITTI IIVIIVVLLS 

       550        560        570 
LIAIGLLLYC KAKNTPVTLS KDQLSGINNI AFSK 

« Hide

References

[1]"Respiratory syncytial virus (RSV) SH and G proteins are not essential for viral replication in vitro: clinical evaluation and molecular characterization of a cold-passaged, attenuated RSV subgroup B mutant."
Karron R.A., Buonagurio D.A., Georgiu A.F., Whitehead S.S., Adamus J.E., Clements-Mann M.L., Harris D.O., Randolph V.B., Udem S.A., Murphy B.R., Sidhu M.S.
Proc. Natl. Acad. Sci. U.S.A. 94:13961-13966(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF013254 Genomic RNA. Translation: AAB82436.1.
RefSeqNP_056863.1. NC_001781.1.

3D structure databases

ProteinModelPortalO36634.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1489825.

Family and domain databases

InterProIPR000776. Fusion_F0_Paramyxovir.
[Graphical view]
PfamPF00523. Fusion_gly. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUS_HRSVB
AccessionPrimary (citable) accession number: O36634
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families