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Protein

Fusion glycoprotein F0

Gene

F

Organism
Measles virus (strain IP-3-Ca) (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 IP-3-Ca) (MeV) (Subacute sclerose panencephalitis virus)
Taxonomic identifieri11237 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeMorbillivirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 499ExtracellularBy similarityAdd BLAST473
Transmembranei500 – 520HelicalBy similarityAdd BLAST21
Topological domaini521 – 529CytoplasmicBy similarity9

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_000003926427 – 529Fusion glycoprotein F0Add BLAST503
ChainiPRO_000003926527 – 115Fusion glycoprotein F2Add BLAST89
ChainiPRO_0000039266116 – 529Fusion glycoprotein F1Add BLAST414

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi32N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi64N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi70N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi71 ↔ 198Interchain (between F2 and F1 chains)By similarity
Disulfide bondi337 ↔ 346By similarity
Disulfide bondi361 ↔ 369By similarity
Disulfide bondi393 ↔ 398By similarity
Disulfide bondi400 ↔ 423By 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
Sitei115 – 116Cleavage; by hostBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP26031

Interactioni

Subunit structurei

Homotrimer of disulfide-linked F1-F2.By similarity

Structurei

3D structure databases

ProteinModelPortaliP26031
SMRiP26031
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni116 – 140Fusion peptideBy similarityAdd BLAST25

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili141 – 169Sequence analysisAdd BLAST29
Coiled coili465 – 490Sequence analysisAdd BLAST26

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

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.

P26031-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSIMGLKVNV SAIFMAVLLT LQTPTGQIHW GNLSKIGVVG IGSASYKVMT
60 70 80 90 100
RSSHQSLVIK LMPNITLLNN CTRVEIAEYR RLLRTVLEPI RDALNAMTQN
110 120 130 140 150
IRLVQSVASS RRHKRFAGVV LAGAALGVAT AAQITAGIAL HQSMLSSQAI
160 170 180 190 200
DNLRASLETT NQAIEAIRQA GQEMILAVQG VQDYINNELI PSMNQLSCDL
210 220 230 240 250
IGQKLGLKLL RYYTEILSLF GPSLRDPISA EISIQALSYA LGGDINKVLE
260 270 280 290 300
KLGYSGGDLL GILESRGIKA RITHVDTESY FIVLSIAYPT LSEIKEVIVH
310 320 330 340 350
RLEGVSYNIG SQEWYTTVPK YVATQGYLIS NFDESSCTFM PEGTVCSQNA
360 370 380 390 400
LYPMSPLLQE CLRGSTKSCA RTLVSGSFGN RFILSQGNLI ANCASILCKC
410 420 430 440 450
YTTGTIIRQD PDKILTYIAA DHCPVVEVNG VTIQVGSRRY PDAVDLHRID
460 470 480 490 500
LGPPISLERL DVGTNLGSAI AKLEDAKELL ESSDQILRSM KGLSSTSIVY
510 520
ILIAVCLGGL IGIPALICCC RGRCNKKGE
Length:529
Mass (Da):57,332
Last modified:May 1, 1992 - v1
Checksum:iAE987BC9F07E9AA9
GO

Sequence cautioni

The sequence CAA34568 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16566 Genomic RNA Translation: CAA34567.1
X16566 Genomic RNA Translation: CAA34568.1 Different initiation.

Similar proteinsi

Entry informationi

Entry nameiFUS_MEASI
AccessioniPrimary (citable) accession number: P26031
Secondary accession number(s): Q83298
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: May 23, 2018
This is version 84 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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