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Protein

Fusion glycoprotein F0

Gene

F

Organism
Human respiratory syncytial virus A (strain A2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 participates 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 - Biological processi

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 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
  • UP000007678 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

Complete GO annotation...

Keywords - Cellular componenti

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

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...); by hostSequence analysis1
Disulfide bondi69 ↔ 212Interchain (between F2 and F1 chains)By similarity
Glycosylationi70N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi116N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi126N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi358 ↔ 367By similarity
Disulfide bondi382 ↔ 393By similarity
Glycosylationi500N-linked (GlcNAc...); 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

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

Protein-protein interaction databases

DIPiDIP-48772N.
IntActiP03420. 2 interactors.

Structurei

Secondary structure

1574
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 33Combined sources5
Turni34 – 37Combined sources4
Beta strandi38 – 49Combined sources12
Beta strandi51 – 60Combined sources10
Helixi74 – 96Combined sources23
Beta strandi102 – 105Combined sources4
Helixi138 – 141Combined sources4
Helixi145 – 147Combined sources3
Helixi149 – 157Combined sources9
Helixi160 – 201Combined sources42
Helixi204 – 206Combined sources3
Beta strandi208 – 211Combined sources4
Helixi217 – 239Combined sources23
Turni240 – 242Combined sources3
Beta strandi243 – 246Combined sources4
Turni249 – 251Combined sources3
Helixi254 – 262Combined sources9
Beta strandi264 – 266Combined sources3
Helixi268 – 275Combined sources8
Helixi278 – 283Combined sources6
Beta strandi286 – 293Combined sources8
Beta strandi296 – 305Combined sources10
Beta strandi308 – 318Combined sources11
Beta strandi327 – 329Combined sources3
Beta strandi333 – 336Combined sources4
Beta strandi340 – 345Combined sources6
Beta strandi348 – 353Combined sources6
Helixi355 – 357Combined sources3
Beta strandi358 – 361Combined sources4
Beta strandi364 – 368Combined sources5
Helixi369 – 371Combined sources3
Beta strandi373 – 375Combined sources3
Helixi377 – 380Combined sources4
Helixi381 – 384Combined sources4
Beta strandi386 – 388Combined sources3
Beta strandi389 – 391Combined sources3
Beta strandi394 – 399Combined sources6
Beta strandi404 – 407Combined sources4
Beta strandi409 – 416Combined sources8
Beta strandi422 – 426Combined sources5
Turni427 – 429Combined sources3
Beta strandi430 – 434Combined sources5
Beta strandi437 – 444Combined sources8
Beta strandi449 – 452Combined sources4
Beta strandi455 – 458Combined sources4
Beta strandi465 – 469Combined sources5
Helixi474 – 477Combined sources4
Turni480 – 482Combined sources3
Helixi487 – 514Combined sources28

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[»]
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[»]
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

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

        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.

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[»]
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[»]
ProteinModelPortaliP03420.
SMRiP03420.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48772N.
IntActiP03420. 2 interactors.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP03420.

Family and domain databases

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

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: November 30, 2016
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.