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Fusion glycoprotein F0 (Protein F) [Cleaved into: Fusion glycoprotein F2; Fusion glycoprotein F1]

 FUS_SENDF               Reviewed;         565 AA.
P12575; Q88412;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
10-MAY-2017, entry version 87.
RecName: Full=Fusion glycoprotein F0;
Short=Protein F;
Contains:
RecName: Full=Fusion glycoprotein F2;
Contains:
RecName: Full=Fusion glycoprotein F1;
Flags: Precursor;
Name=F;
Sendai virus (strain Fushimi) (SeV).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Respirovirus.
NCBI_TaxID=11195;
NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
NCBI_TaxID=36483; Cricetidae sp. (Hamster).
NCBI_TaxID=10090; Mus musculus (Mouse).
NCBI_TaxID=10116; Rattus norvegicus (Rat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2824671; DOI=10.1099/0022-1317-68-11-2939;
Itoh M., Shibuta H., Homma M.;
"Single amino acid substitution of Sendai virus at the cleavage site
of the fusion protein confers trypsin resistance.";
J. Gen. Virol. 68:2939-2944(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND MUTAGENESIS OF
106-THR--GLN-108; 106-THR--SER-115; 112-VAL--SER-115 AND
114-GLN-SER-115.
PubMed=7625124; DOI=10.1016/0168-1702(94)00102-I;
Heminaway B.R., Yang Y., Tanaka Y., Panin M., Huang Y.T.,
Galinski M.S.;
"Role of basic residues in the proteolytic activation of Sendai virus
fusion glycoprotein.";
Virus Res. 36:15-35(1995).
-!- 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) interacts
with HN tetramer 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). {ECO:0000250}.
-!- SUBUNIT: Homotrimer of disulfide-linked F1-F2. Interacts with HN
and M proteins (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Host cell membrane
{ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
-!- DOMAIN: The cytoplasmic region mediates the interaction with HN
and M proteins. {ECO:0000250}.
-!- PTM: In natural infection, inactive F0 is matured into F1 and F2
outside the cell by one or more trypsin-like, arginine-specific
endoprotease secreted by the bronchial epithelial cells. One
identified protease that may be involved in this process is
tryptase Clara. Unlike most paramyxoviruses, Sendai F0 processing
occurs on the cell surface and induces a conformational change in
the protein that unmasks the fusion peptide. F0 maturation is a
primary determinant for organ tropism and pathogenicity. F1 and F2
display interchain and intrachain disulfide bonds, that are
necessary for correct folding and intracellular transport (By
similarity). {ECO:0000250}.
-!- PTM: N-glycosylated; glycans consist of a mixture of high mannose-
type oligosaccharides and of complex-type oligosaccharides.
Glycosylation at Asn-245 is essential for membrane localization
and F0 cleavage (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: Sendai virus or recombinant F protein are widely
used in cellular biology to fuse cells.
-!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D00152; BAA00107.1; -; Genomic_RNA.
EMBL; U06432; AAC54271.1; -; Genomic_RNA.
PIR; A30037; VGNZFS.
ProteinModelPortal; P12575; -.
SMR; P12575; -.
OrthoDB; VOG0900006Q; -.
Proteomes; UP000006825; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
InterPro; IPR000776; Fusion_F0_Paramyxovir.
Pfam; PF00523; Fusion_gly; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Disulfide bond;
Fusion of virus membrane with host cell membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Membrane; Signal; Transmembrane;
Transmembrane helix; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
SIGNAL 1 25 {ECO:0000250}.
CHAIN 26 565 Fusion glycoprotein F0. {ECO:0000250}.
/FTId=PRO_0000039366.
CHAIN 26 116 Fusion glycoprotein F2. {ECO:0000250}.
/FTId=PRO_0000039367.
CHAIN 117 565 Fusion glycoprotein F1. {ECO:0000250}.
/FTId=PRO_0000039368.
TOPO_DOM 26 500 Extracellular. {ECO:0000250}.
TRANSMEM 501 521 Helical. {ECO:0000250}.
TOPO_DOM 522 565 Cytoplasmic. {ECO:0000250}.
REGION 117 141 Fusion peptide. {ECO:0000250}.
REGION 269 307 Leucine-zipper. {ECO:0000255}.
COILED 142 170 {ECO:0000255}.
COILED 466 491 {ECO:0000255}.
SITE 116 117 Cleavage; by arginine-specific
endoprotease. {ECO:0000250}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250}.
CARBOHYD 245 245 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250}.
CARBOHYD 449 449 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000250}.
DISULFID 70 199 Interchain (between F2 and F1 chains).
{ECO:0000250}.
DISULFID 338 347 {ECO:0000250}.
DISULFID 362 370 {ECO:0000250}.
DISULFID 394 399 {ECO:0000250}.
DISULFID 401 424 {ECO:0000250}.
VARIANT 461 461 I -> V.
MUTAGEN 106 115 TTQNAGVPQS->DEENAGRRRK: No effect.
{ECO:0000269|PubMed:7625124}.
MUTAGEN 106 115 TTQNAGVPQS->DEENAGVPRK: Cleaved by
intracellular CV-1 protease. Displays
cell fusion activity.
{ECO:0000269|PubMed:7625124}.
MUTAGEN 106 108 TTQ->DEE: Partially cleaved by
intracellular CV-1 protease. No cell
fusion activity.
{ECO:0000269|PubMed:7625124}.
MUTAGEN 112 115 VPQS->RRRK: Cleaved by intracellular CV-1
protease. Displays cell fusion activity.
{ECO:0000269|PubMed:7625124}.
MUTAGEN 114 115 QS->RK: Cleaved by intracellular CV-1
protease. Partial cell fusion activity.
{ECO:0000269|PubMed:7625124}.
SEQUENCE 565 AA; 61552 MW; 16491C66F8E38F84 CRC64;
MTAYIQRSQC ISTSLLVVLT TLVSCQIPRD RLSNIGVIVD EGKSLKIAGS HESRYIVLSL
VPGVDLENGC GTAQVIQYKS LLNRLLIPLR DALDLQEALI TVTNDTTQNA GVPQSRFFGA
VIGTIALGVA TSAQITAGIA LAEAREAKRD IALIKESMTK THKSIELLQN AVGEQILALK
TLQDFVNDEI KPAISELGCE TAALRLGIKL TQHYSGLLTA FGSNFGTIGE KSLTLQALSS
LYSANITEIM TTIRTGQSNI YDVIYTEQIK GTVIDVDLER YMVTLSVKIP ILSEVPGVLI
HKASSISYNI DGEEWYVTVP SHILSRASFL GGADITDCVE SRLTYICPRD PAQLIPDSQQ
KCILGDTTRC PVTKVVDSLI PKFAFVNGGV VANCIASTCT CGTGRRPISQ DRSKGVVFLT
HDNCGLIGVN GVELYANRRG HDATWGVQNL TVGPAIAIRP IDISLNLADA TNFLQDSKAE
LEKARKILSE VGRWYNSRET VITIIVVMVV ILVVIIVIVI VLYRLKRSML MGNPDDRIPR
DTYTLEPKIR HMYTNGGFDA MAEKR


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