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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 virusesMononegaviralesParamyxoviridaeRubulavirus
Virus hostiCanis lupus familiaris (Dog) (Canis familiaris) [TaxID: 9615]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007232 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 487ExtracellularBy similarityAdd BLAST468
Transmembranei488 – 508HelicalBy similarityAdd BLAST21
Topological domaini509 – 529CytoplasmicBy similarityAdd BLAST21

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 – 19Sequence analysisAdd BLAST19
ChainiPRO_000003937820 – 529Fusion glycoprotein F0Add BLAST510
ChainiPRO_000003937920 – 102Fusion glycoprotein F2Add BLAST83
ChainiPRO_0000039380103 – 529Fusion glycoprotein F1Add BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi64 ↔ 185Interchain (between F2 and F1 chains)By similarity
Glycosylationi65N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi73N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi324 ↔ 333By similarity
Disulfide bondi348 ↔ 356By similarity
Glycosylationi352N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi380 ↔ 385By similarity
Disulfide bondi387 ↔ 410By similarity
Glycosylationi427N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi431N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi457N-linked (GlcNAc...); by hostSequence analysis1

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)DescriptionActionsGraphical viewLength
Sitei102 – 103Cleavage; by hostBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer of disulfide-linked F1-F2.

Structurei

Secondary structure

1529
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 26Combined sources5
Turni27 – 29Combined sources3
Beta strandi30 – 52Combined sources23
Helixi67 – 93Combined sources27
Beta strandi95 – 98Combined sources4
Beta strandi102 – 104Combined sources3
Helixi110 – 113Combined sources4
Beta strandi115 – 117Combined sources3
Helixi123 – 174Combined sources52
Helixi176 – 182Combined sources7
Helixi185 – 203Combined sources19
Turni204 – 206Combined sources3
Helixi214 – 216Combined sources3
Beta strandi217 – 219Combined sources3
Helixi221 – 228Combined sources8
Helixi229 – 231Combined sources3
Helixi232 – 239Combined sources8
Beta strandi242 – 244Combined sources3
Helixi246 – 250Combined sources5
Beta strandi256 – 263Combined sources8
Turni264 – 267Combined sources4
Beta strandi268 – 291Combined sources24
Beta strandi294 – 296Combined sources3
Beta strandi299 – 303Combined sources5
Beta strandi307 – 312Combined sources6
Beta strandi315 – 318Combined sources4
Beta strandi324 – 326Combined sources3
Beta strandi328 – 332Combined sources5
Helixi343 – 349Combined sources7
Helixi353 – 355Combined sources3
Beta strandi358 – 360Combined sources3
Helixi365 – 367Combined sources3
Beta strandi368 – 372Combined sources5
Beta strandi375 – 378Combined sources4
Turni380 – 382Combined sources3
Beta strandi385 – 389Combined sources5
Beta strandi392 – 394Combined sources3
Beta strandi401 – 405Combined sources5
Turni407 – 409Combined sources3
Beta strandi411 – 415Combined sources5
Beta strandi418 – 421Combined sources4
Helixi438 – 440Combined sources3
Helixi450 – 475Combined sources26

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04849.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni103 – 127Fusion peptideAdd BLAST25

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili128 – 156Sequence analysisAdd BLAST29
Coiled coili452 – 477Sequence analysisAdd BLAST26

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi98 – 102Poly-Arg5

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
PDB 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.
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...

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: November 30, 2016
This is version 116 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, Reference 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.