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Protein

Fusion glycoprotein F0

Gene

F

Organism
Measles virus (strain Edmonston-AIK-C vaccine) (MeV) (Subacute sclerose panencephalitis virus)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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 H 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
Cleaved into the following 2 chains:
Gene namesi
Name:F
OrganismiMeasles virus (strain Edmonston-AIK-C vaccine) (MeV) (Subacute sclerose panencephalitis virus)
Taxonomic identifieri36408 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeMorbillivirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007775 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini24 – 494ExtracellularBy similarityAdd BLAST471
Transmembranei495 – 515HelicalSequence analysisAdd BLAST21
Topological domaini516 – 550CytoplasmicBy similarityAdd BLAST35

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 – 23Sequence analysisAdd BLAST23
ChainiPRO_000003925224 – 550Fusion glycoprotein F0Add BLAST527
ChainiPRO_000003925324 – 112Fusion glycoprotein F2Add BLAST89
ChainiPRO_0000039254113 – 550Fusion glycoprotein F1Add BLAST438

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi29N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi61N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi67N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi68 ↔ 195Interchain (between F2 and F1 chains)By similarity
Disulfide bondi334 ↔ 343By similarity
Disulfide bondi358 ↔ 366By similarity
Disulfide bondi390 ↔ 395By similarity
Disulfide bondi397 ↔ 420By similarity

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
Sitei112 – 113Cleavage; by hostBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer of disulfide-linked F1-F2.By similarity

Structurei

3D structure databases

ProteinModelPortaliP35973
SMRiP35973
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni113 – 137Fusion peptideBy similarityAdd BLAST25

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili138 – 166Sequence analysisAdd BLAST29
Coiled coili462 – 487Sequence 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.

P35973-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGLKVNVSAI FMAVLLTLQT PTGQIHWGNL SKIGVVGIGS ASYKVMTRSS
60 70 80 90 100
HQSLVIKLMP NITLLNNCTR VEIAEYRRLL RTVLEPIRDA LNAMTQNIRP
110 120 130 140 150
VQSVASSRRH KRFAGVVLAG AALGVATAAQ ITAGIALHQS MLNSQAIDNL
160 170 180 190 200
RASLETTNQA IEAIRQAGQE MILAVQGVQD YINNELIPSM NQLSCDLIGQ
210 220 230 240 250
KLGLKLLRYY TEILSLFGPS LRDPISAEIS IQALSYALGG DINKVLEKLG
260 270 280 290 300
YSGGDLLGIL ESRGIKARIT HVDTESYLIV LSIAYPTLSE IKGVIVHRLE
310 320 330 340 350
GVSYNIGSQE WYTTVPKYVA TQGYLISNFD ESSCTFMPEG TVCSQNALYP
360 370 380 390 400
MSPLLQECLR GSTKSCARTL VSGSFGNRFI LSQGNLIANC ASILCKCYTT
410 420 430 440 450
GTIINQDPDK ILTYIAADHC PVVEVNGVTI QVGSRRYPDA VYLHRIDLGP
460 470 480 490 500
PILLERLDVG TNLGNAIAKL EDAKELLESS DQILRSMKGL SSTCIVYILI
510 520 530 540 550
AVCLGGLIGI PALICCCRGR CNKKGEQVGM SRPGLKPDLT GTSKSYVRSL
Length:550
Mass (Da):59,540
Last modified:June 1, 1994 - v1
Checksum:iAAC4DAB92DE0D938
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S58435 Genomic RNA Translation: AAB26145.1
PIRiE48556

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S58435 Genomic RNA Translation: AAB26145.1
PIRiE48556

3D structure databases

ProteinModelPortaliP35973
SMRiP35973
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG0900006Q

Family and domain databases

InterProiView protein in InterPro
IPR000776 Fusion_F0_Paramyxovir
PfamiView protein in Pfam
PF00523 Fusion_gly, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiFUS_MEASA
AccessioniPrimary (citable) accession number: P35973
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 10, 2017
This is version 79 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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