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P03420

- FUS_HRSVA

UniProt

P03420 - FUS_HRSVA

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Protein
Fusion glycoprotein F0
Gene
F
Organism
Human respiratory syncytial virus A (strain A2)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei136 – 1372Cleavage; by host By similarity

GO - Biological processi

  1. fusion of virus membrane with host plasma membrane Source: UniProtKB-KW
  2. positive regulation of syncytium formation by virus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Fusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Syncytium formation induced by viral infection, Viral penetration into host cytoplasm, Virus entry into host cell

Protein family/group databases

TCDBi1.G.2.1.3. the viral pore-forming membrane fusion protein-2 (vmfp2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Fusion glycoprotein F0
Short name:
Protein F
Cleaved into the following 2 chains:
Gene namesi
Name:F
OrganismiHuman respiratory syncytial virus A (strain A2)
Taxonomic identifieri11259 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaePneumovirinaePneumovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007678: Genome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 529503Extracellular By similarity
Add
BLAST
Transmembranei530 – 55021Helical; Reviewed prediction
Add
BLAST
Topological domaini551 – 57424Cytoplasmic By similarity
Add
BLAST

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
  4. virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 574553Fusion glycoprotein F0
PRO_0000039234Add
BLAST
Chaini22 – 136115Fusion glycoprotein F2
PRO_0000039235Add
BLAST
Chaini137 – 574438Fusion glycoprotein F1
PRO_0000039236Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi27 – 271N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi69 ↔ 212Interchain (between F2 and F1 chains) By similarity
Glycosylationi70 – 701N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi116 – 1161N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi126 – 1261N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi358 ↔ 367 By similarity
Disulfide bondi382 ↔ 393 By similarity
Glycosylationi500 – 5001N-linked (GlcNAc...); by host Reviewed prediction
Lipidationi550 – 5501S-palmitoyl cysteine; by host1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

Homotrimer of disulfide-linked F1-F2 By similarity. Interacts with glycoprotein G. Interacts with host RHOA; this interaction facilitates virus-induced syncytium formation.3 Publications

Protein-protein interaction databases

DIPiDIP-48772N.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 335
Turni34 – 374
Beta strandi38 – 4912
Beta strandi51 – 6010
Helixi74 – 9825
Helixi139 – 1413
Helixi149 – 15810
Helixi160 – 20142
Helixi204 – 2063
Beta strandi208 – 2114
Helixi217 – 23923
Turni240 – 2423
Beta strandi243 – 2464
Turni249 – 2513
Helixi254 – 26310
Beta strandi264 – 2663
Helixi268 – 2769
Helixi278 – 2836
Beta strandi286 – 2927
Beta strandi294 – 30512
Beta strandi307 – 31812
Beta strandi326 – 3294
Beta strandi333 – 3364
Beta strandi340 – 3456
Beta strandi348 – 3536
Helixi355 – 3573
Beta strandi358 – 3614
Beta strandi364 – 3685
Helixi369 – 3713
Beta strandi373 – 3753
Helixi377 – 3804
Helixi381 – 3844
Beta strandi386 – 3883
Beta strandi389 – 3913
Beta strandi394 – 3985
Beta strandi404 – 4074
Beta strandi409 – 4168
Beta strandi422 – 4265
Turni427 – 4293
Beta strandi430 – 4345
Beta strandi437 – 4448
Beta strandi449 – 4524
Beta strandi455 – 4584
Beta strandi466 – 4694
Helixi474 – 4774
Turni480 – 4823
Helixi487 – 51428

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IXTX-ray2.75C/P254-277[»]
3KPEX-ray1.47A159-209[»]
B482-520[»]
3RKIX-ray3.20A/B/C1-524[»]
3RRRX-ray2.82A/C/E/G/I/M26-109[»]
B/D/F/H/L/N147-513[»]
3RRTX-ray3.20A/C/E26-109[»]
B/D/F147-513[»]
4CCFX-ray2.65A/B/C/D/E/F1-574[»]
4JHWX-ray3.60F26-513[»]
4MMQX-ray3.25A26-107[»]
B137-513[»]
4MMRX-ray3.10A26-107[»]
B137-513[»]
4MMSX-ray2.40A/C/E26-107[»]
B/D/F137-513[»]
4MMTX-ray3.05A26-107[»]
B137-513[»]
4MMUX-ray3.00A26-107[»]
B137-513[»]
4MMVX-ray2.81A26-107[»]
B137-513[»]
ProteinModelPortaliP03420.
SMRiP03420. Positions 158-207, 477-516.

Miscellaneous databases

EvolutionaryTraceiP03420.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni137 – 15721Fusion peptide By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili155 – 18329 Reviewed prediction
Add
BLAST
Coiled coili491 – 51626 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR000776. Fusion_F0_Paramyxovir.
[Graphical view]
PfamiPF00523. Fusion_gly. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P03420-1 [UniParc]FASTAAdd to Basket

« Hide

MELLILKANA ITTILTAVTF CFASGQNITE EFYQSTCSAV SKGYLSALRT    50
GWYTSVITIE LSNIKENKCN GTDAKVKLIK QELDKYKNAV TELQLLMQST 100
PPTNNRARRE LPRFMNYTLN NAKKTNVTLS KKRKRRFLGF LLGVGSAIAS 150
GVAVSKVLHL EGEVNKIKSA LLSTNKAVVS LSNGVSVLTS KVLDLKNYID 200
KQLLPIVNKQ SCSISNIETV IEFQQKNNRL LEITREFSVN AGVTTPVSTY 250
MLTNSELLSL INDMPITNDQ KKLMSNNVQI VRQQSYSIMS IIKEEVLAYV 300
VQLPLYGVID TPCWKLHTSP LCTTNTKEGS NICLTRTDRG WYCDNAGSVS 350
FFPQAETCKV QSNRVFCDTM NSLTLPSEIN LCNVDIFNPK YDCKIMTSKT 400
DVSSSVITSL GAIVSCYGKT KCTASNKNRG IIKTFSNGCD YVSNKGMDTV 450
SVGNTLYYVN KQEGKSLYVK GEPIINFYDP LVFPSDEFDA SISQVNEKIN 500
QSLAFIRKSD ELLHNVNAGK STTNIMITTI IIVIIVILLS LIAVGLLLYC 550
KARSTPVTLS KDQLSGINNI AFSN 574
Length:574
Mass (Da):63,453
Last modified:July 21, 1986 - v1
Checksum:iA4066D9DC98933AA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti102 – 1021P → A in strain: Cold-passage attenuated.
Natural varianti218 – 2181E → A in strain: Cold-passage attenuated.
Natural varianti379 – 3791I → V in strain: Cold-passage attenuated.
Natural varianti447 – 4471M → V in strain: Cold-passage attenuated.
Natural varianti523 – 5231T → I in strain: Cold-passage attenuated.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11486 Genomic RNA. Translation: AAB59858.1.
U50362 Genomic RNA. Translation: AAB86664.1.
U50363 Genomic RNA. Translation: AAB86676.1.
AF035006 Genomic RNA. Translation: AAC14902.1.
U63644 Genomic RNA. Translation: AAC55970.1.
PIRiA04035. VGNZA2.
B28929.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11486 Genomic RNA. Translation: AAB59858.1 .
U50362 Genomic RNA. Translation: AAB86664.1 .
U50363 Genomic RNA. Translation: AAB86676.1 .
AF035006 Genomic RNA. Translation: AAC14902.1 .
U63644 Genomic RNA. Translation: AAC55970.1 .
PIRi A04035. VGNZA2.
B28929.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IXT X-ray 2.75 C/P 254-277 [» ]
3KPE X-ray 1.47 A 159-209 [» ]
B 482-520 [» ]
3RKI X-ray 3.20 A/B/C 1-524 [» ]
3RRR X-ray 2.82 A/C/E/G/I/M 26-109 [» ]
B/D/F/H/L/N 147-513 [» ]
3RRT X-ray 3.20 A/C/E 26-109 [» ]
B/D/F 147-513 [» ]
4CCF X-ray 2.65 A/B/C/D/E/F 1-574 [» ]
4JHW X-ray 3.60 F 26-513 [» ]
4MMQ X-ray 3.25 A 26-107 [» ]
B 137-513 [» ]
4MMR X-ray 3.10 A 26-107 [» ]
B 137-513 [» ]
4MMS X-ray 2.40 A/C/E 26-107 [» ]
B/D/F 137-513 [» ]
4MMT X-ray 3.05 A 26-107 [» ]
B 137-513 [» ]
4MMU X-ray 3.00 A 26-107 [» ]
B 137-513 [» ]
4MMV X-ray 2.81 A 26-107 [» ]
B 137-513 [» ]
ProteinModelPortali P03420.
SMRi P03420. Positions 158-207, 477-516.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48772N.

Protein family/group databases

TCDBi 1.G.2.1.3. the viral pore-forming membrane fusion protein-2 (vmfp2) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P03420.

Family and domain databases

InterProi IPR000776. Fusion_F0_Paramyxovir.
[Graphical view ]
Pfami PF00523. Fusion_gly. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of the gene encoding the fusion (F) glycoprotein of human respiratory syncytial virus."
    Collins P.L., Huang Y.T., Wertz G.W.
    Proc. Natl. Acad. Sci. U.S.A. 81:7683-7687(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Nucleotide sequence analysis of the respiratory syncytial virus subgroup A cold-passaged (cp) temperature sensitive (ts) cpts-248/404 live attenuated virus vaccine candidate."
    Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R., Crowe J.E. Jr.
    Virology 225:419-422(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Cold-passage attenuated.
  3. "Acquisition of the ts phenotype by a chemically mutagenized cold-passaged human respiratory syncytial virus vaccine candidate results from the acquisition of a single mutation in the polymerase (L) gene."
    Crowe J.E. Jr., Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R.
    Virus Genes 13:269-273(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Cold-passage attenuated.
  4. "A cold-passaged, attenuated strain of human respiratory syncytial virus contains mutations in the F and L genes."
    Connors M., Crowe J.E. Jr., Firestone C.Y., Murphy B.R., Collins P.L.
    Virology 208:478-484(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Cold-passage attenuated.
  5. "Recombinant respiratory syncytial virus (RSV) bearing a set of mutations from cold-passaged RSV is attenuated in chimpanzees."
    Whitehead S.S., Juhasz K., Firestone C.Y., Collins P.L., Murphy B.R.
    J. Virol. 72:4467-4471(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Cold-passage attenuated.
  6. "Fatty acid acylation of the fusion glycoprotein of human respiratory syncytial virus."
    Arumugham R.G., Seid R.C. Jr., Doyle S., Hildreth S.W., Paradisio P.R.
    J. Biol. Chem. 264:10339-10342(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-550.
  7. "RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation."
    Pastey M.K., Crowe J.E. Jr., Graham B.S.
    J. Virol. 73:7262-7270(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST RHOA.
  8. "The fusion glycoprotein of human respiratory syncytial virus facilitates virus attachment and infectivity via an interaction with cellular heparan sulfate."
    Feldman S.A., Audet S., Beeler J.A.
    J. Virol. 74:6442-6447(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEPARAN SULFATE.
  9. "Furin cleavage of the respiratory syncytial virus fusion protein is not a requirement for its transport to the surface of virus-infected cells."
    Sugrue R.J., Brown C., Brown G., Aitken J., McL Rixon H.W.
    J. Gen. Virol. 82:1375-1386(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY HOST FURIN.
  10. "Respiratory syncytial virus (RSV) fusion protein subunit F2, not attachment protein G, determines the specificity of RSV infection."
    Schlender J., Zimmer G., Herrler G., Conzelmann K.K.
    J. Virol. 77:4609-4616(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HOST CELL SPECIFICITY.
  11. "The fusion protein of respiratory syncytial virus triggers p53-dependent apoptosis."
    Eckardt-Michel J., Lorek M., Baxmann D., Grunwald T., Keil G.M., Zimmer G.
    J. Virol. 82:3236-3249(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS.
  12. "The RSV F and G glycoproteins interact to form a complex on the surface of infected cells."
    Low K.W., Tan T., Ng K., Tan B.H., Sugrue R.J.
    Biochem. Biophys. Res. Commun. 366:308-313(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GLYCOPROTEIN G.

Entry informationi

Entry nameiFUS_HRSVA
AccessioniPrimary (citable) accession number: P03420
Secondary accession number(s): P88811
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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