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O36634

- FUS_HRSVB

UniProt

O36634 - FUS_HRSVB

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Protein

Fusion glycoprotein F0

Gene

F

Organism
Human respiratory syncytial virus B (strain B1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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 (By similarity).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

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 B (strain B1)
Taxonomic identifieri79692 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaePneumovirinaePneumovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000002472: Genome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei530 – 55021HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell plasma membrane Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. viral envelope Source: UniProtKB-KW
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 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 574549Fusion glycoprotein F0PRO_0000390376Add
BLAST
Chaini26 – 136111Fusion glycoprotein F2PRO_0000390377Add
BLAST
Chaini137 – 574438Fusion glycoprotein F1PRO_0000390378Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi27 – 271N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi69 ↔ 212Interchain (between F2 and F1 chains)By similarity
Glycosylationi70 – 701N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi116 – 1161N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi120 – 1201N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi126 – 1261N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi358 ↔ 367By similarity
Disulfide bondi382 ↔ 393By similarity
Glycosylationi500 – 5001N-linked (GlcNAc...); by hostSequence Analysis

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 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliO36634.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili73 – 10028Sequence AnalysisAdd
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.

O36634-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELLIHRLSA IFLTLAINAL YLTSSQNITE EFYQSTCSAV SRGYFSALRT
60 70 80 90 100
GWYTSVITIE LSNIKETKCN GTDTKVKLIK QELDKYKNAV TELQLLMQNT
110 120 130 140 150
PAANNRARRE APQYMNYTIN TTKNLNVSIS KKRKRRFLGF LLGVGSAIAS
160 170 180 190 200
GIAVSKVLHL EGEVNKIKNA LLSTNKAVVS LSNGVSVLTS KVLDLKNYIN
210 220 230 240 250
NQLLPIVNQQ SCRISNIETV IEFQQKNSRL LEINREFSVN AGVTTPLSTY
260 270 280 290 300
MLTNSELLSL INDMPITNDQ KKLMSSNVQI VRQQSYSIMS IIKEEVLAYV
310 320 330 340 350
VQLPIYGVID TPCWKLHTSP LCTTNIKEGS NICLTRTDRG WYCDNAGSVS
360 370 380 390 400
FFPQADTCKV QSNRVFCDTM NSLTLPSEVS LCNTDIFNSK YDCKIMTSKT
410 420 430 440 450
DISSSVITSL GAIVSCYGKT KCTASNKNRG IIKTFSNGCD YVSNKGVDTV
460 470 480 490 500
SVGNTLYYVN KLEGKNLYVK GEPIINYYDP LVFPSDEFDA SISQVNEKIN
510 520 530 540 550
QSLAFIRRSD ELLHNVNTGK STTNIMITTI IIVIIVVLLS LIAIGLLLYC
560 570
KAKNTPVTLS KDQLSGINNI AFSK
Length:574
Mass (Da):63,710
Last modified:January 1, 1998 - v1
Checksum:i29A127B128BF5E92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF013254 Genomic RNA. Translation: AAB82436.1.
RefSeqiNP_056863.1. NC_001781.1.

Genome annotation databases

GeneIDi1489825.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF013254 Genomic RNA. Translation: AAB82436.1 .
RefSeqi NP_056863.1. NC_001781.1.

3D structure databases

ProteinModelPortali O36634.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1489825.

Family and domain databases

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

Publicationsi

  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].

Entry informationi

Entry nameiFUS_HRSVB
AccessioniPrimary (citable) accession number: O36634
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 61 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3