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Protein

Fusion glycoprotein F0

Gene

F

Organism
Bovine respiratory syncytial virus (strain Copenhagen) (BRS)
Status
Reviewed-Annotation score: Annotation score: 4 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. Interacts directly with heparan sulfate and may participate in virus attachment. 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.By similarity

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

Names & Taxonomyi

Protein namesi
Recommended name:
Fusion glycoprotein F0
Cleaved into the following 4 chains:
Fusion glycoprotein F2'By similarity
Interchain peptideBy similarity
Gene namesi
Name:F
OrganismiBovine respiratory syncytial virus (strain Copenhagen) (BRS)
Taxonomic identifieri11248 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesPneumoviridaeOrthopneumovirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 529ExtracellularBy similarityAdd BLAST503
Transmembranei530 – 550HelicalSequence analysisAdd BLAST21
Topological domaini551 – 574CytoplasmicBy similarityAdd BLAST24

GO - Cellular componenti

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_000003922826 – 574Fusion glycoprotein F0Add BLAST549
ChainiPRO_000003922926 – 136Fusion glycoprotein F2Add BLAST111
ChainiPRO_000043265926 – 109Fusion glycoprotein F2'By similarityAdd BLAST84
PeptideiPRO_0000432660110 – 136Interchain peptideBy similarityAdd BLAST27
ChainiPRO_0000039230137 – 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
Glycosylationi120N-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 hostBy similarity1

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. 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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei109 – 110Cleavage; by hostBy similarity2
Sitei136 – 137Cleavage; by hostBy similarity2
Sitei136 – 137Cleavage; by host furinBy similarity2

Keywords - PTMi

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

Interactioni

Subunit structurei

Homotrimer. Interacts with glycoprotein G. Interacts with host RHOA; this interaction facilitates virus-induced syncytium formation.By similarity

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 – 60Combined sources23
Helixi74 – 95Combined sources22
Helixi96 – 98Combined sources3
Beta strandi99 – 102Combined sources4
Turni146 – 148Combined sources3
Helixi149 – 157Combined sources9
Helixi163 – 168Combined sources6
Helixi169 – 171Combined sources3
Turni172 – 174Combined sources3
Beta strandi175 – 179Combined sources5
Beta strandi187 – 194Combined sources8
Helixi196 – 199Combined sources4
Turni200 – 203Combined sources4
Helixi204 – 208Combined sources5
Turni209 – 211Combined sources3
Helixi218 – 237Combined sources20
Turni238 – 242Combined sources5
Beta strandi243 – 246Combined sources4
Turni249 – 251Combined sources3
Helixi254 – 261Combined sources8
Beta strandi264 – 266Combined sources3
Helixi268 – 276Combined sources9
Helixi278 – 283Combined sources6
Beta strandi287 – 293Combined sources7
Beta strandi296 – 318Combined sources23
Beta strandi325 – 327Combined sources3
Helixi328 – 330Combined sources3
Beta strandi333 – 336Combined sources4
Beta strandi340 – 345Combined sources6
Beta strandi348 – 354Combined sources7
Helixi355 – 357Combined sources3
Beta strandi359 – 361Combined sources3
Beta strandi364 – 368Combined sources5
Helixi369 – 371Combined sources3
Beta strandi373 – 375Combined sources3
Helixi377 – 383Combined sources7
Beta strandi389 – 391Combined sources3
Beta strandi394 – 398Combined sources5
Beta strandi404 – 407Combined sources4
Beta strandi409 – 416Combined sources8
Beta strandi422 – 426Combined sources5
Turni427 – 429Combined sources3
Beta strandi430 – 434Combined sources5
Beta strandi437 – 443Combined sources7
Beta strandi449 – 452Combined sources4
Beta strandi455 – 458Combined sources4
Beta strandi465 – 469Combined sources5
Turni474 – 477Combined sources4
Beta strandi485 – 491Combined sources7
Helixi492 – 507Combined sources16
Turni508 – 511Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5TDLX-ray3.50A1-513[»]
ProteinModelPortaliP22167.
SMRiP22167.
ModBaseiSearch...
MobiDBiSearch...

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

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.

P22167-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATAMRMII SIIFISTYMT HITLCQNITE EFYQSTCSAV SRGYLSALRT
60 70 80 90 100
GWYTSVVTIE LSKIQKNVCK STDSKVKLIK QELERYNNAV IELQSLMQNE
110 120 130 140 150
PASFSRAKRG IPELIHYTRN STKRFYGLMG KKRKRRFLGF LLGIGSAIAS
160 170 180 190 200
GVAVSKVLHL EGEVNKIKNA LLSTNKAVVS LSNGVSVLTS KVLDLKNYID
210 220 230 240 250
KELLPKVNNH DCRISNIETV IEFQQKNNRL LEIAREFSVN AGITTPLSTY
260 270 280 290 300
MLTNSELLSL INDMPITNDQ KKLMSSNVQI VRQQSYSIMS VVKEEVIAYV
310 320 330 340 350
VQLPIYGVID TPCWKLHTSP LCTTDNKEGS NICLTRTDRG WYCDNAGSVS
360 370 380 390 400
FFPQAETCKV QSNRVFCDTM NSLTLPTDVN LCNTDIFNTK YDCKIMTSKT
410 420 430 440 450
DISSSVITSI GAIVSCYGKT KCTASNKNRG IIKTFSNGCD YVSNKGVDTV
460 470 480 490 500
SVGNTLYYVN KLEGKALYIK GEPIINYYDP LVFPSDEFDA SIAQVNAKIN
510 520 530 540 550
QSLAFIRRSD ELLHSVDVGK STTNVVITTI IIVIVVVILM LIAVGLLFYC
560 570
KTRSTPIMLG KDQLSGINNL SFSK
Length:574
Mass (Da):63,822
Last modified:August 1, 1991 - v1
Checksum:i6341D60AB80F827B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58350 mRNA. Translation: AAA42808.1.
PIRiA38492. VGNZBR.

Similar proteinsi

Entry informationi

Entry nameiFUS_BRSVC
AccessioniPrimary (citable) accession number: P22167
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: November 22, 2017
This is version 94 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

Documents

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