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1.G.2.1.2
Fusion glycoprotein FO (Class I) (565 aas) (31% identical throughout its length with 1.H.2.1.1) (Lamb and Jardetzky 2007).  Interacts with protein G and protein TM in J paramyxovirus to promote fusion (Li et al. 2015).

Accession Number:P04855
Protein Name:Fusion glycoprotein F0
Length:565
Molecular Weight:61644.00
Species:Sendai virus (strain Z) (SeV) [11198]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Virion membrane1 / Single-pass type I membrane protein2
Substrate small molecules

Cross database links:

Pfam: PF00523   

Gene Ontology

GO:0020002 C:host cell plasma membrane
GO:0016021 C:integral to membrane
GO:0019031 C:viral envelope
GO:0055036 C:virion membrane
GO:0006948 P:induction by virus of host cell-cell fusion

References (17)

[1] “Use of the deoxyinosine-containing probe to isolate and sequence cDNA encoding the fusion (F) glycoprotein of Sendai virus (HVJ).”  Miura N.et.al.   2998947
[2] “Determination of the complete nucleotide sequence of the Sendai virus genome RNA and the predicted amino acid sequences of the F, HN and L proteins.”  Shioda T.et.al.   3005975
[3] “Characterization of a pantropic variant of Sendai virus derived from a host range mutant.”  Tashiro M.et.al.   2841801
[4] “Pneumotropic revertants derived from a pantropic mutant, F1-R, of Sendai virus.”  Tashiro M.et.al.   1651590
[5] “Budding site of Sendai virus in polarized epithelial cells is one of the determinants for tropism and pathogenicity in mice.”  Tashiro M.et.al.   1312267
[6] “Determinants of pantropism of the F1-R mutant of Sendai virus: specific mutations involved are in the F and M genes.”  Okada H.et.al.   9930191
[7] “Nucleotide sequence of a Sendai virus genome region covering the entire M gene and the 3' proximal 1013 nucleotides of the F gene.”  Hidaka Y.et.al.   6095182
[8] “Assignment of disulfide bridges in the fusion glycoprotein of Sendai virus.”  Iwata S.et.al.   8151783
[9] “Carbohydrate structures of HVJ (Sendai virus) glycoproteins.”  Yoshima H.et.al.   6263875
[10] “Tryptase Clara, an activating protease for Sendai virus in rat lungs, is involved in pneumopathogenicity.”  Tashiro M.et.al.   1331518
[11] “Functional interaction of paramyxovirus glycoproteins: identification of a domain in Sendai virus HN which promotes cell fusion.”  Tanabayashi K.et.al.   8709235
[12] “A leucine zipper motif in the ectodomain of Sendai virus fusion protein assembles in solution and in membranes and specifically binds biologically-active peptides and the virus.”  Ghosh J.K.et.al.   9398274
[13] “The roles of individual cysteine residues of Sendai virus fusion protein in intracellular transport.”  Segawa H.et.al.   9603994
[14] “Kinetics of interactions of sendai virus envelope glycoproteins, F and HN, with endoplasmic reticulum-resident molecular chaperones, BiP, calnexin, and calreticulin.”  Tomita Y.et.al.   10578061
[15] “Functional analysis of the individual oligosaccharide chains of sendai virus fusion protein.”  Segawa H.et.al.   10876159
[16] “Assembly of Sendai virus: M protein interacts with F and HN proteins and with the cytoplasmic tail and transmembrane domain of F protein.”  Ali A.et.al.   11040121
[17] “The 3D structure of the fusion primed Sendai F-protein determined by electron cryomicroscopy.”  Ludwig K.et.al.   12881411

External Searches:

  • Search: DB with
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  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MTAYIQRSQC ISTSLLVVLT TLVSCQIPRD RLSNIGVIVD EGKSLKIAGS HESRYIVLSL 
61:	VPGVDFENGC GTAQVIQYKS LLNRLLIPLR DALDLQEALI TVTNDTTQNA GAPQSRFFGA 
121:	VIGTIALGVA TSAQITAGIA LAEAREAKRD IALIKESMTK THKSIELLQN AVGEQILALK 
181:	TLQDFVNDEI KPAISELGCE TAALRLGIKL TQHYSELLTA FGSNFGTIGE KSLTLQALSS 
241:	LYSANITEIM TTIKTGQSNI YDVIYTEQIK GTVIDVDLER YMVTLSVKIP ILSEVPGVLI 
301:	HKASSISYNI DGEEWYVTVP SHILSRASFL GGADITDCVE SRLTYICPRD PAQLIPDSQQ 
361:	KCILGDTTRC PVTKVVDSLI PKFAFVNGGV VANCIASTCT CGTGRRPISQ DRSKGVVFLT 
421:	HDNCGLIGVN GVELYANRRG HDATWGVQNL TVGPAIAIRP IDISLNLADA TNFLQDSKAE 
481:	LEKARKILSE VGRWYNSRET VITIIVVMVV ILVVIIVIII VLYRLRRSML MGNPDDRIPR 
541:	DTYTLEPKIR HMYTNGGFDA MAEKR