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Protein

Fusion glycoprotein F0

Gene

F

Organism
Human metapneumovirus (strain CAN97-83) (HMPV)
Status
Reviewed-Annotation score: -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. The F protein also interacts with heparan sulfate moieties expressed at the host cell surface to provide initial attachment. Once the virus is attached to the cell, F interacts with host ITGAV/ITGB1 through its RGD motif to promote infection.1 Publication

Miscellaneous

The cleavage peptide sequence for the hMPV F protein (RQSR) varies from the one described for other pneumoviruses, and differs from the furin protease motif (R/K-X-R/K-R).

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
OrganismiHuman metapneumovirus (strain CAN97-83) (HMPV)
Taxonomic identifieri694067 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesPneumoviridaeMetapneumovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000001398 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei492 – 512HelicalSequence analysisAdd BLAST21

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 – 18Sequence analysisAdd BLAST18
ChainiPRO_000039480619 – 539Fusion glycoprotein F0Add BLAST521
ChainiPRO_000039480720 – 102Fusion glycoprotein F2Add BLAST83
ChainiPRO_0000394808103 – 539Fusion glycoprotein F1Add BLAST437

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi57N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi60 ↔ 182Interchain (between F2 and F1 chains)By similarity
Glycosylationi172N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi326 ↔ 335By similarity
Disulfide bondi350 ↔ 361By similarity
Glycosylationi353N-linked (GlcNAc...) asparagine; by hostSequence analysis1

Post-translational modificationi

The F glycoprotein is synthesized as a inactive precursor and processed to yield the mature F1 and F2 proteins.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ6WB98

Interactioni

Subunit structurei

Homotrimer of disulfide-linked F1-F2 (By similarity). Interacts with host integrin ITGAV/ITGB1.By similarity1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ6WB98
SMRiQ6WB98
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni103 – 124Fusion peptideBy similarityAdd BLAST22

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi329 – 331Cell attachment siteSequence analysis3

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19261
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.

Q6WB98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWKVVIIFS LLITPQHGLK ESYLEESCST ITEGYLSVLR TGWYTNVFTL
60 70 80 90 100
EVGDVENLTC SDGPSLIKTE LDLTKSALRE LKTVSADQLA REEQIENPRQ
110 120 130 140 150
SRFVLGAIAL GVATAAAVTA GVAIAKTIRL ESEVTAIKNA LKTTNEAVST
160 170 180 190 200
LGNGVRVLAT AVRELKDFVS KNLTRAINKN KCDIDDLKMA VSFSQFNRRF
210 220 230 240 250
LNVVRQFSDN AGITPAISLD LMTDAELARA VSNMPTSAGQ IKLMLENRAM
260 270 280 290 300
VRRKGFGILI GVYGSSVIYM VQLPIFGVID TPCWIVKAAP SCSGKKGNYA
310 320 330 340 350
CLLREDQGWY CQNAGSTVYY PNEKDCETRG DHVFCDTAAG INVAEQSKEC
360 370 380 390 400
NINISTTNYP CKVSTGRHPI SMVALSPLGA LVACYKGVSC SIGSNRVGII
410 420 430 440 450
KQLNKGCSYI TNQDADTVTI DNTVYQLSKV EGEQHVIKGR PVSSSFDPIK
460 470 480 490 500
FPEDQFNVAL DQVFENIENS QALVDQSNRI LSSAEKGNTG FIIVIILIAV
510 520 530
LGSSMILVSI FIIIKKTKKP TGAPPELSGV TNNGFIPHS
Length:539
Mass (Da):58,477
Last modified:July 5, 2004 - v1
Checksum:i2987E611786A64BA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY297749 Genomic RNA Translation: AAQ67695.1
RefSeqiYP_012608.1, NC_004148.2

Genome annotation databases

GeneIDi2799939
KEGGivg:2799939

Similar proteinsi

Entry informationi

Entry nameiFUS_HMPVC
AccessioniPrimary (citable) accession number: Q6WB98
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2004
Last modified: May 23, 2018
This is version 57 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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