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Protein

Fusion glycoprotein F0

Gene

F

Organism
Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5)
Status
Reviewed-Annotation score: 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 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Fusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Viral penetration into host cytoplasm, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Fusion glycoprotein F0
Cleaved into the following 2 chains:
Gene namesi
Name:F
OrganismiParainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5)
Taxonomic identifieri11208 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeRubulavirus
Virus hostiCanis lupus familiaris (Dog) (Canis familiaris) [TaxID: 9615]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007232 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 487468ExtracellularBy similarityAdd
BLAST
Transmembranei488 – 50821HelicalBy similarityAdd
BLAST
Topological domaini509 – 52921CytoplasmicBy similarityAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 529510Fusion glycoprotein F0PRO_0000039378Add
BLAST
Chaini20 – 10283Fusion glycoprotein F2PRO_0000039379Add
BLAST
Chaini103 – 529427Fusion glycoprotein F1PRO_0000039380Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi64 ↔ 185Interchain (between F2 and F1 chains)By similarity
Glycosylationi65 – 651N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi73 – 731N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi324 ↔ 333By similarity
Disulfide bondi348 ↔ 356By similarity
Glycosylationi352 – 3521N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi380 ↔ 385By similarity
Disulfide bondi387 ↔ 410By similarity
Glycosylationi427 – 4271N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi431 – 4311N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi457 – 4571N-linked (GlcNAc...); by hostSequence analysis

Post-translational modificationi

The inactive precursor F0 is glycosylated and proteolytically cleaved into F1 and F2 to be functionally active. The cleavage is mediated by cellular proteases during the transport and maturation of the polypeptide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei102 – 1032Cleavage; by hostBy similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer of disulfide-linked F1-F2.

Structurei

Secondary structure

1
529
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 265Combined sources
Turni27 – 293Combined sources
Beta strandi30 – 5223Combined sources
Helixi67 – 9327Combined sources
Beta strandi95 – 984Combined sources
Beta strandi102 – 1043Combined sources
Helixi110 – 1134Combined sources
Beta strandi115 – 1173Combined sources
Helixi123 – 17452Combined sources
Helixi176 – 1827Combined sources
Helixi185 – 20319Combined sources
Turni204 – 2063Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2193Combined sources
Helixi221 – 2288Combined sources
Helixi229 – 2313Combined sources
Helixi232 – 2398Combined sources
Beta strandi242 – 2443Combined sources
Helixi246 – 2505Combined sources
Beta strandi256 – 2638Combined sources
Turni264 – 2674Combined sources
Beta strandi268 – 29124Combined sources
Beta strandi294 – 2963Combined sources
Beta strandi299 – 3035Combined sources
Beta strandi307 – 3126Combined sources
Beta strandi315 – 3184Combined sources
Beta strandi324 – 3263Combined sources
Beta strandi328 – 3325Combined sources
Helixi343 – 3497Combined sources
Helixi353 – 3553Combined sources
Beta strandi358 – 3603Combined sources
Helixi365 – 3673Combined sources
Beta strandi368 – 3725Combined sources
Beta strandi375 – 3784Combined sources
Turni380 – 3823Combined sources
Beta strandi385 – 3895Combined sources
Beta strandi392 – 3943Combined sources
Beta strandi401 – 4055Combined sources
Turni407 – 4093Combined sources
Beta strandi411 – 4155Combined sources
Beta strandi418 – 4214Combined sources
Helixi438 – 4403Combined sources
Helixi450 – 47526Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SVFX-ray1.40A/C122-185[»]
B/D440-477[»]
2B9BX-ray2.85A/B/C20-475[»]
4GIPX-ray2.00A/B/C20-100[»]
D/E/F103-477[»]
4WSGX-ray3.00A/B/C23-477[»]
ProteinModelPortaliP04849.
SMRiP04849. Positions 20-477.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04849.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni103 – 12725Fusion peptideAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili128 – 15629Sequence analysisAdd
BLAST
Coiled coili452 – 47726Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi98 – 1025Poly-Arg

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.

P04849-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTIIQFLVV SCLLAGAGSL DPAALMQIGV IPTNVRQLMY YTEASSAFIV
60 70 80 90 100
VKLMPTIDSP ISGCNITSIS SYNATVTKLL QPIGENLETI RNQLIPTRRR
110 120 130 140 150
RRFAGVVIGL AALGVATAAQ VTAAVALVKA NENAAAILNL KNAIQKTNAA
160 170 180 190 200
VADVVQATQS LGTAVQAVQD HINSVVSPAI TAANCKAQDA IIGSILNLYL
210 220 230 240 250
TELTTIFHNQ ITNPALSPIT IQALRILLGS TLPTVVEKSF NTQISAAELL
260 270 280 290 300
SSGLLTGQIV GLDLTYMQMV IKIELPTLTV QPATQIIDLA TISAFINNQE
310 320 330 340 350
VMAQLPTRVM VTGSLIQAYP ASQCTITPNT VYCRYNDAQV LSDDTMACLQ
360 370 380 390 400
GNLTRCTFSP VVGSFLTRFV LFDGIVYANC RSMLCKCMQP AAVILQPSSS
410 420 430 440 450
PVTVIDMYKC VSLQLDNLRF TITQLANVTY NSTIKLESSQ ILSIDPLDIS
460 470 480 490 500
QNLAAVNKSL SDALQHLAQS DTYLSAITSA TTTSVLSIIA ICLGSLGLIL
510 520
IILLSVVVWK LLTIVVANRN RMENFVYHK
Length:529
Mass (Da):56,597
Last modified:August 13, 1987 - v1
Checksum:i3152C37B1AEA2C7E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02253 Genomic RNA. Translation: AAA47881.1.
AF052755 Genomic RNA. Translation: AAC95515.1.
PIRiA21688. VGNZSP.
RefSeqiYP_138515.1. NC_006430.1.

Genome annotation databases

GeneIDi3160801.
KEGGivg:3160801.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02253 Genomic RNA. Translation: AAA47881.1.
AF052755 Genomic RNA. Translation: AAC95515.1.
PIRiA21688. VGNZSP.
RefSeqiYP_138515.1. NC_006430.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SVFX-ray1.40A/C122-185[»]
B/D440-477[»]
2B9BX-ray2.85A/B/C20-475[»]
4GIPX-ray2.00A/B/C20-100[»]
D/E/F103-477[»]
4WSGX-ray3.00A/B/C23-477[»]
ProteinModelPortaliP04849.
SMRiP04849. Positions 20-477.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3160801.
KEGGivg:3160801.

Miscellaneous databases

EvolutionaryTraceiP04849.

Family and domain databases

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

Publicationsi

  1. "Fusion protein of the paramyxovirus simian virus 5: nucleotide sequence of mRNA predicts a highly hydrophobic glycoprotein."
    Paterson R.G., Harris T.J.R., Lamb R.A.
    Proc. Natl. Acad. Sci. U.S.A. 81:6706-6710(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Structural basis for paramyxovirus-mediated membrane fusion."
    Baker K.A., Dutch R.E., Lamb R.A., Jardetzky T.S.
    Mol. Cell 3:309-319(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 122-185 AND 440-477.

Entry informationi

Entry nameiFUS_PIV5
AccessioniPrimary (citable) accession number: P04849
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 8, 2016
This is version 113 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.