FUS_SENDH
ID FUS_SENDH Reviewed; 565 AA.
AC P04856;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Fusion glycoprotein F0;
DE Short=Protein F;
DE Contains:
DE RecName: Full=Fusion glycoprotein F2;
DE Contains:
DE RecName: Full=Fusion glycoprotein F1;
DE Flags: Precursor;
GN Name=F;
OS Sendai virus (strain Harris) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11196;
OH NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH NCBI_TaxID=36483; Cricetidae sp. (Hamster).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2981971; DOI=10.1099/0022-1317-66-2-317;
RA Blumberg B.M., Giorgi C., Rose K., Kolakofsky D.;
RT "Sequence determination of the Sendai virus fusion protein gene.";
RL J. Gen. Virol. 66:317-331(1985).
CC -!- FUNCTION: Class I viral fusion protein. Under the current model, the
CC protein has at least 3 conformational states: pre-fusion native state,
CC pre-hairpin intermediate state, and post-fusion hairpin state. During
CC viral and plasma cell membrane fusion, the heptad repeat (HR) regions
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and plasma cell membranes. Directs fusion of viral and
CC cellular membranes leading to delivery of the nucleocapsid into the
CC cytoplasm. This fusion is pH independent and occurs directly at the
CC outer cell membrane. The trimer of F1-F2 (F protein) interacts with HN
CC tetramer at the virion surface. Upon HN binding to its cellular
CC receptor, the hydrophobic fusion peptide is unmasked and interacts with
CC the cellular membrane, inducing the fusion between cell and virion
CC membranes. Later in infection, F proteins expressed at the plasma
CC membrane of infected cells could mediate fusion with adjacent cells to
CC form syncytia, a cytopathic effect that could lead to tissue necrosis
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer of disulfide-linked F1-F2. Interacts with HN and M
CC proteins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The cytoplasmic region mediates the interaction with HN and M
CC proteins. {ECO:0000250}.
CC -!- PTM: In natural infection, inactive F0 is matured into F1 and F2
CC outside the cell by one or more trypsin-like, arginine-specific
CC endoprotease secreted by the bronchial epithelial cells. One identified
CC protease that may be involved in this process is tryptase Clara. Unlike
CC most paramyxoviruses, Sendai F0 processing occurs on the cell surface
CC and induces a conformational change in the protein that unmasks the
CC fusion peptide. F0 maturation is a primary determinant for organ
CC tropism and pathogenicity. F1 and F2 display interchain and intrachain
CC disulfide bonds, that are necessary for correct folding and
CC intracellular transport (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated; glycans consist of a mixture of high mannose-type
CC oligosaccharides and of complex-type oligosaccharides. Glycosylation at
CC Asn-245 is essential for membrane localization and F0 cleavage (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Sendai virus or recombinant F protein are widely used in
CC cellular biology to fuse cells.
CC -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; X02131; CAA26043.1; -; Genomic_RNA.
DR SMR; P04856; -.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR000776; Fusion_F0_Paramyxovir.
DR Pfam; PF00523; Fusion_gly; 1.
PE 3: Inferred from homology;
KW Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..565
FT /note="Fusion glycoprotein F0"
FT /evidence="ECO:0000250"
FT /id="PRO_0000039369"
FT CHAIN 26..116
FT /note="Fusion glycoprotein F2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000039370"
FT CHAIN 117..565
FT /note="Fusion glycoprotein F1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000039371"
FT TOPO_DOM 26..500
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 522..565
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 117..141
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT REGION 278..306
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT COILED 142..170
FT /evidence="ECO:0000255"
FT COILED 466..491
FT /evidence="ECO:0000255"
FT SITE 116..117
FT /note="Cleavage; by arginine-specific endoprotease"
FT /evidence="ECO:0000250"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT DISULFID 70..199
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250"
FT DISULFID 338..347
FT /evidence="ECO:0000250"
FT DISULFID 362..370
FT /evidence="ECO:0000250"
FT DISULFID 401..424
FT /evidence="ECO:0000250"
SQ SEQUENCE 565 AA; 61666 MW; 576D4B64C80205CD CRC64;
MTAYIQRSQC ISTSLLVVLT TLVSCQIPRD RLSNIGVIVD EGKSLKIAGS HESRYIVLSL
VPGVDLENGC GTAQVIQYKS LLNRLLIPLR DALDLQEALI TVTNDTTQNA GVPQSRFFGA
VIGTIALGVA TSAQITAGIA LAEAREAKRD IALIKESMTK THKSVELLQN AVGEQILALK
TLQDFVNDEI KPAISELGCE TAALRLGIKL TQHYFGLLTA FGSNFGTIGE KSRTLQALSS
LYSANITEIM TTIRTGQSNI YDVIYTEQIK GTVIDVDLER YMVTLSVKIP ILSEVPGVLI
HKASSISYNI DGEEWYVTVP SHILSRASFL GGADITDCVE SRLTYICPRD PAQLIPDSQQ
KCILGDTTRC PVTKVVDSLI PKFAFVNGGV VANRIASTCT CGTGRRPISQ DRSKGVAFLT
HDNCGLIGVN GVELYANRRG HDATWGVQNL TVGPAIAIRP VDISLNLADA TNFLQDSKAE
LEKARKILSE VGRWYNSRET VITIIVVMVV ILVVIIVIVI VLYRLKRSML MGNPDERIPR
DTYTLEPKIR HMYTNGGFDA MAEKR
