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Protein

Fusion glycoprotein F0

Gene

F

Organism
Measles virus (strain Edmonston-Zagreb vaccine) (MeV) (Subacute sclerose panencephalitis virus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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

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
OrganismiMeasles virus (strain Edmonston-Zagreb vaccine) (MeV) (Subacute sclerose panencephalitis virus)
Taxonomic identifieri70149 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeMorbillivirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

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

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 – 23Sequence analysisAdd BLAST23
ChainiPRO_000003927624 – 550Fusion glycoprotein F0Add BLAST527
ChainiPRO_000003927724 – 112Fusion glycoprotein F2Add BLAST89
ChainiPRO_0000039278113 – 550Fusion glycoprotein F1Add BLAST438

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi29N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi61N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi67N-linked (GlcNAc...); 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

ProteinModelPortaliP69358.
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

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.

P69358-1 [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 HVDTESYFIV 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
PISLERLDVG TNLGNAIAKL EDAKELLESS DQILRSMKGL SSTSIVYILI
510 520 530 540 550
AVCLGGLIGI PALICCCRGR CNKKGEQVGM SRPGLKPDLT GTSKSYVRSL
Length:550
Mass (Da):59,532
Last modified:August 1, 1988 - v1
Checksum:i7AA4F1CA82169093
GO

Sequence cautioni

The sequence AAA56660 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03670 Genomic RNA. Translation: AAA56660.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03670 Genomic RNA. Translation: AAA56660.1. Different initiation.

3D structure databases

ProteinModelPortaliP69358.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

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

Entry informationi

Entry nameiFUS_MEASZ
AccessioniPrimary (citable) accession number: P69358
Secondary accession number(s): P08300
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 2, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. 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.