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Protein

Fusion glycoprotein F0

Gene

F

Organism
Human respiratory syncytial virus A (strain A2)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

During virus entry, induces fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. The fusogenic activity is inactive untill entry into host cell endosome, where a furin-like protease cleaves off a small peptide between F1 and F2 (PubMed:18216092). Interacts directly with heparan sulfate and may participate in virus attachment (PubMed:10864656). Furthermore, the F2 subunit was identifed as the major determinant of RSV host cell specificity (PubMed:11493675). Later in infection, proteins F expressed at the plasma membrane of infected cells can 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 (PubMed:12663767).5 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

Keywordsi

Biological processFusion 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 4 chains:
Fusion glycoprotein F2'1 Publication
Interchain peptide1 Publication
Gene namesi
Name:F
OrganismiHuman respiratory syncytial virus A (strain A2)
Taxonomic identifieri11259 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesPneumoviridaeOrthopneumovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000181559 Componenti: Genome
  • UP000181262 Componenti: Genome
  • UP000181145 Componenti: Genome
  • UP000007678 Componenti: Genome
  • UP000134464 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 529Extracellular1 PublicationAdd BLAST503
Transmembranei530 – 550HelicalSequence analysisAdd BLAST21
Topological domaini551 – 574Cytoplasmic1 PublicationAdd BLAST24

GO - Cellular componenti

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3856166

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000003923426 – 574Fusion glycoprotein F0Add BLAST549
ChainiPRO_000003923526 – 136Fusion glycoprotein F21 PublicationAdd BLAST111
ChainiPRO_000043266326 – 109Fusion glycoprotein F2'1 PublicationAdd BLAST84
PeptideiPRO_0000432664110 – 136Interchain peptide1 PublicationAdd BLAST27
ChainiPRO_0000039236137 – 574Fusion glycoprotein F1Add BLAST438

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi27N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi69 ↔ 212Interchain (between F2 and F1 chains)By similarity
Glycosylationi70N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi116N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi126N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi358 ↔ 367By similarity
Disulfide bondi382 ↔ 393By similarity
Glycosylationi500N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Lipidationi550S-palmitoyl cysteine; by host1 Publication1

Post-translational modificationi

The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed by host cell furin in the Golgi to yield the mature F1 and F2 proteins (PubMed:11369882). The cleavage site between F1 and F2 requires the minimal sequence [KR]-X-[KR]-R. During entry a furin-like protease cleaves F2 into F2' and a small peptide, leading to the activation of fusogenic function (PubMed:23593008).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei109 – 110Cleavage; by host1 Publication2
Sitei136 – 137Cleavage; by host furin1 Publication2

Keywords - PTMi

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

Proteomic databases

PRIDEiP03420

Interactioni

Subunit structurei

Homotrimer (PubMed:10846072). Interacts with glycoprotein G (PubMed:18036342). Interacts with host RHOA; this interaction facilitates virus-induced syncytium formation (PubMed:10438814).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself8EBI-10042897,EBI-10042897

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-48772N
ELMiP03420
IntActiP03420, 2 interactors

Structurei

Secondary structure

1574
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP03420
SMRiP03420
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03420

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni137 – 157Fusion peptideBy similarityAdd BLAST21

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili155 – 183Sequence analysisAdd BLAST29
Coiled coili491 – 516Sequence analysisAdd BLAST26

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG0900006Q

Family and domain databases

InterProiView protein in InterPro
IPR000776 Fusion_F0_Paramyxovir
PfamiView protein in Pfam
PF00523 Fusion_gly, 1 hit

Sequencei

Sequence statusi: Complete.

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

P03420-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELLILKANA ITTILTAVTF CFASGQNITE EFYQSTCSAV SKGYLSALRT
60 70 80 90 100
GWYTSVITIE LSNIKENKCN GTDAKVKLIK QELDKYKNAV TELQLLMQST
110 120 130 140 150
PPTNNRARRE LPRFMNYTLN NAKKTNVTLS KKRKRRFLGF LLGVGSAIAS
160 170 180 190 200
GVAVSKVLHL EGEVNKIKSA LLSTNKAVVS LSNGVSVLTS KVLDLKNYID
210 220 230 240 250
KQLLPIVNKQ SCSISNIETV IEFQQKNNRL LEITREFSVN AGVTTPVSTY
260 270 280 290 300
MLTNSELLSL INDMPITNDQ KKLMSNNVQI VRQQSYSIMS IIKEEVLAYV
310 320 330 340 350
VQLPLYGVID TPCWKLHTSP LCTTNTKEGS NICLTRTDRG WYCDNAGSVS
360 370 380 390 400
FFPQAETCKV QSNRVFCDTM NSLTLPSEIN LCNVDIFNPK YDCKIMTSKT
410 420 430 440 450
DVSSSVITSL GAIVSCYGKT KCTASNKNRG IIKTFSNGCD YVSNKGMDTV
460 470 480 490 500
SVGNTLYYVN KQEGKSLYVK GEPIINFYDP LVFPSDEFDA SISQVNEKIN
510 520 530 540 550
QSLAFIRKSD ELLHNVNAGK STTNIMITTI IIVIIVILLS LIAVGLLLYC
560 570
KARSTPVTLS KDQLSGINNI AFSN
Length:574
Mass (Da):63,453
Last modified:July 21, 1986 - v1
Checksum:iA4066D9DC98933AA
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti102P → A in strain: Cold-passage attenuated. 1
Natural varianti218E → A in strain: Cold-passage attenuated. 1
Natural varianti379I → V in strain: Cold-passage attenuated. 1
Natural varianti447M → V in strain: Cold-passage attenuated. 1
Natural varianti523T → I in strain: Cold-passage attenuated. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2MDPNMR-A1-85[»]
3IXTX-ray2.75C/P254-277[»]
3KPEX-ray1.47A159-209[»]
B482-520[»]
3O41X-ray1.95C/P423-436[»]
3O45X-ray2.87C/P423-438[»]
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[»]
4ZYPX-ray5.50A/B/C26-513[»]
5C69X-ray2.30A26-513[»]
5C6BX-ray2.40F26-108[»]
F113-513[»]
5EA3X-ray2.75F1-513[»]
5EA4X-ray2.30F1-513[»]
5EA5X-ray3.05F1-513[»]
5EA6X-ray2.75F1-513[»]
5EA7X-ray2.85F1-513[»]
5EA8X-ray2.60F1-513[»]
5J3DX-ray4.08E/G/J26-98[»]
F/I/K147-513[»]
5K6BX-ray2.98F26-105[»]
F145-509[»]
5K6CX-ray3.58F26-103[»]
F145-509[»]
5K6FX-ray2.59F26-101[»]
F145-509[»]
5K6GX-ray2.90F26-96[»]
F145-509[»]
5K6HX-ray2.65F26-103[»]
F145-509[»]
5K6IX-ray2.92F26-101[»]
F145-509[»]
5KWWX-ray2.50F1-513[»]
5TOJX-ray3.30A/B/C1-513[»]
5TOKX-ray3.80A/B/C1-513[»]
5TPNX-ray3.14A27-108[»]
A113-513[»]
5U68X-ray3.08A/B/C1-513[»]
5UDCX-ray3.45A/D/F1-513[»]
5W23X-ray3.40A/B/C1-513[»]
ProteinModelPortaliP03420
SMRiP03420
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48772N
ELMiP03420
IntActiP03420, 2 interactors

Chemistry databases

ChEMBLiCHEMBL3856166

Protein family/group databases

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

Proteomic databases

PRIDEiP03420

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG0900006Q

Miscellaneous databases

EvolutionaryTraceiP03420

Family and domain databases

InterProiView protein in InterPro
IPR000776 Fusion_F0_Paramyxovir
PfamiView protein in Pfam
PF00523 Fusion_gly, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiFUS_HRSVA
AccessioniPrimary (citable) accession number: P03420
Secondary accession number(s): P88811
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 18, 2018
This is version 121 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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