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Protein

Fusion glycoprotein F0

Gene

F

Organism
Nipah virus
Status
Reviewed-Annotation score: Annotation score: 4 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

Keywordsi

Biological processFusion 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
Short name:
Protein F
Cleaved into the following 2 chains:
Gene namesi
Name:F
OrganismiNipah virus
Taxonomic identifieri121791 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeHenipavirus
Virus hostiCynopterus brachyotis (Lesser short-nosed fruit bat) (Pachysoma brachyotis) [TaxID: 58060]
Eonycteris spelaea (Lesser dawn bat) (Macroglossus spelaeus) [TaxID: 58065]
Homo sapiens (Human) [TaxID: 9606]
Pteropus hypomelanus (Island flying fox) (Variable flying fox) [TaxID: 9405]
Pteropus vampyrus (Large flying fox) [TaxID: 132908]
Scotophilus kuhlii (Lesser asiatic yellow bat) [TaxID: 153297]
Sus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000002330 Componenti: Genome
  • UP000008676 Componenti: Genome
  • UP000007527 Componenti: Genome
  • UP000170143 Componenti: Genome
  • UP000100567 Componenti: Genome
  • UP000130871 Componenti: Genome
  • UP000110983 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 497ExtracellularSequence analysisAdd BLAST471
Transmembranei498 – 518HelicalSequence analysisAdd BLAST21
Topological domaini519 – 546CytoplasmicSequence analysisAdd BLAST28

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 – 26Sequence analysisAdd BLAST26
ChainiPRO_000023600527 – 546Fusion glycoprotein F0Add BLAST520
ChainiPRO_000023600627 – 109Fusion glycoprotein F2Add BLAST83
ChainiPRO_0000236007110 – 546Fusion glycoprotein F1Add BLAST437

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi64N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi67N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi71 ↔ 192Interchain (between F2 and F1 chains)By similarity
Glycosylationi99N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi331 ↔ 340By similarity
Disulfide bondi355 ↔ 363By similarity
Disulfide bondi387 ↔ 392By similarity
Disulfide bondi394 ↔ 417By similarity
Glycosylationi414N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi464N-linked (GlcNAc...) asparagine; 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei109 – 110Cleavage; by hostBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer of disulfide-linked F1-F2.By similarity

Structurei

Secondary structure

1546
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 34Combined sources5
Turni35 – 37Combined sources3
Beta strandi38 – 48Combined sources11
Beta strandi53 – 60Combined sources8
Helixi66 – 68Combined sources3
Helixi75 – 98Combined sources24
Beta strandi101 – 103Combined sources3
Beta strandi112 – 116Combined sources5
Helixi117 – 120Combined sources4
Beta strandi122 – 124Combined sources3
Helixi140 – 174Combined sources35
Helixi176 – 181Combined sources6
Helixi184 – 186Combined sources3
Turni187 – 189Combined sources3
Helixi194 – 214Combined sources21
Helixi228 – 231Combined sources4
Helixi232 – 235Combined sources4
Helixi239 – 244Combined sources6
Helixi253 – 258Combined sources6
Beta strandi263 – 270Combined sources8
Turni271 – 274Combined sources4
Beta strandi275 – 282Combined sources8
Beta strandi286 – 298Combined sources13
Beta strandi301 – 310Combined sources10
Beta strandi314 – 319Combined sources6
Beta strandi322 – 326Combined sources5
Helixi328 – 330Combined sources3
Beta strandi331 – 333Combined sources3
Beta strandi335 – 342Combined sources8
Helixi350 – 355Combined sources6
Turni356 – 358Combined sources3
Helixi360 – 362Combined sources3
Beta strandi365 – 367Combined sources3
Beta strandi376 – 379Combined sources4
Beta strandi382 – 385Combined sources4
Turni387 – 389Combined sources3
Beta strandi392 – 394Combined sources3
Turni395 – 397Combined sources3
Beta strandi410 – 412Combined sources3
Turni414 – 416Combined sources3
Beta strandi418 – 422Combined sources5
Beta strandi425 – 428Combined sources4
Helixi438 – 441Combined sources4
Helixi456 – 481Combined sources26

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WP7X-ray2.20A/B/C137-178[»]
A/B/C453-485[»]
3N27X-ray1.80A/B/C137-178[»]
5EVMX-ray3.37A/B/C/D/E/F1-488[»]
ProteinModelPortaliQ9IH63.
SMRiQ9IH63.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9IH63.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni110 – 134Fusion peptideBy similarityAdd BLAST25

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili135 – 163Sequence analysisAdd BLAST29
Coiled coili459 – 484Sequence 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.

Q9IH63-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVILDKRCY CNLLILILMI SECSVGILHY EKLSKIGLVK GVTRKYKIKS
60 70 80 90 100
NPLTKDIVIK MIPNVSNMSQ CTGSVMENYK TRLNGILTPI KGALEIYKNN
110 120 130 140 150
THDLVGDVRL AGVIMAGVAI GIATAAQITA GVALYEAMKN ADNINKLKSS
160 170 180 190 200
IESTNEAVVK LQETAEKTVY VLTALQDYIN TNLVPTIDKI SCKQTELSLD
210 220 230 240 250
LALSKYLSDL LFVFGPNLQD PVSNSMTIQA ISQAFGGNYE TLLRTLGYAT
260 270 280 290 300
EDFDDLLESD SITGQIIYVD LSSYYIIVRV YFPILTEIQQ AYIQELLPVS
310 320 330 340 350
FNNDNSEWIS IVPNFILVRN TLISNIEIGF CLITKRSVIC NQDYATPMTN
360 370 380 390 400
NMRECLTGST EKCPRELVVS SHVPRFALSN GVLFANCISV TCQCQTTGRA
410 420 430 440 450
ISQSGEQTLL MIDNTTCPTA VLGNVIISLG KYLGSVNYNS EGIAIGPPVF
460 470 480 490 500
TDKVDISSQI SSMNQSLQQS KDYIKEAQRL LDTVNPSLIS MLSMIILYVL
510 520 530 540
SIASLCIGLI TFISFIIVEK KRNTYSRLED RRVRPTSSGD LYYIGT
Length:546
Mass (Da):60,282
Last modified:October 1, 2000 - v1
Checksum:i3C78F4D1127EFD0E
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti250T → I in strain: Isolate NiV/MY/99/VRI-0626. 1
Natural varianti348M → T in strain: Isolate Malaysian flying-fox. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF238466 mRNA. Translation: AAF73956.1.
AF212302 Genomic RNA. Translation: AAK29087.1.
AY029767 Genomic RNA. Translation: AAK50544.1.
AY029768 Genomic RNA. Translation: AAK50553.1.
AF376747 Genomic RNA. Translation: AAM13405.1.
AJ564621 Genomic RNA. Translation: CAD92350.1.
AJ564622 Genomic RNA. Translation: CAD92356.1.
AJ564623 Genomic RNA. Translation: CAD92362.1.
AJ627196 Genomic RNA. Translation: CAF25496.1.
RefSeqiNP_112026.1. NC_002728.1.

Genome annotation databases

GeneIDi920954.
KEGGivg:920954.

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.

Entry informationi

Entry nameiFUS_NIPAV
AccessioniPrimary (citable) accession number: Q9IH63
Secondary accession number(s): Q5K4D9, Q8QU00
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: October 1, 2000
Last modified: May 10, 2017
This is version 87 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

Documents

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