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P69358 (FUS_MEASZ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Subunit structure

Homotrimer of disulfide-linked F1-F2 By similarity.

Subcellular location

Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass membrane protein By similarity.

Post-translational modification

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.

Sequence similarities

Belongs to the paramyxoviruses fusion glycoprotein family.

Sequence caution

The sequence AAA56660.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 550527Fusion glycoprotein F0
PRO_0000039276
Chain24 – 11289Fusion glycoprotein F2
PRO_0000039277
Chain113 – 550438Fusion glycoprotein F1
PRO_0000039278

Regions

Topological domain24 – 494471Extracellular By similarity
Transmembrane495 – 51521Helical; Potential
Topological domain516 – 55035Cytoplasmic By similarity
Region113 – 13725Fusion peptide By similarity
Coiled coil138 – 16629 Potential
Coiled coil462 – 48726 Potential

Sites

Site112 – 1132Cleavage; by host By similarity

Amino acid modifications

Glycosylation291N-linked (GlcNAc...); by host Potential
Glycosylation611N-linked (GlcNAc...); by host Potential
Glycosylation671N-linked (GlcNAc...); by host Potential
Disulfide bond68 ↔ 195Interchain (between F2 and F1 chains) By similarity
Disulfide bond334 ↔ 343 By similarity
Disulfide bond358 ↔ 366 By similarity
Disulfide bond390 ↔ 395 By similarity
Disulfide bond397 ↔ 420 By similarity

Sequences

Sequence LengthMass (Da)Tools
P69358 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 7AA4F1CA82169093

FASTA55059,532
        10         20         30         40         50         60 
MGLKVNVSAI FMAVLLTLQT PTGQIHWGNL SKIGVVGIGS ASYKVMTRSS HQSLVIKLMP 

        70         80         90        100        110        120 
NITLLNNCTR VEIAEYRRLL RTVLEPIRDA LNAMTQNIRP VQSVASSRRH KRFAGVVLAG 

       130        140        150        160        170        180 
AALGVATAAQ ITAGIALHQS MLNSQAIDNL RASLETTNQA IEAIRQAGQE MILAVQGVQD 

       190        200        210        220        230        240 
YINNELIPSM NQLSCDLIGQ KLGLKLLRYY TEILSLFGPS LRDPISAEIS IQALSYALGG 

       250        260        270        280        290        300 
DINKVLEKLG YSGGDLLGIL ESRGIKARIT HVDTESYFIV LSIAYPTLSE IKGVIVHRLE 

       310        320        330        340        350        360 
GVSYNIGSQE WYTTVPKYVA TQGYLISNFD ESSCTFMPEG TVCSQNALYP MSPLLQECLR 

       370        380        390        400        410        420 
GSTKSCARTL VSGSFGNRFI LSQGNLIANC ASILCKCYTT GTIINQDPDK ILTYIAADHC 

       430        440        450        460        470        480 
PVVEVNGVTI QVGSRRYPDA VYLHRIDLGP PISLERLDVG TNLGNAIAKL EDAKELLESS 

       490        500        510        520        530        540 
DQILRSMKGL SSTSIVYILI AVCLGGLIGI PALICCCRGR CNKKGEQVGM SRPGLKPDLT 

       550 
GTSKSYVRSL 

« Hide

References

[1]"Comparison of sequences of the H, F, and N coding genes of measles virus vaccine strains."
Rota J.S., Wang Z.D., Rota P.A., Bellini W.J.
Virus Res. 31:317-330(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03670 Genomic RNA. Translation: AAA56660.1. Different initiation.

3D structure databases

ProteinModelPortalP69358.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000776. Fusion_F0_Paramyxovir.
[Graphical view]
PfamPF00523. Fusion_gly. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUS_MEASZ
AccessionPrimary (citable) accession number: P69358
Secondary accession number(s): P08300
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: February 19, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families