ID   FUS_SENDO               Reviewed;         565 AA.
AC   O57295; Q88248;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 89.
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 Ohita) (SeV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Respirovirus.
OX   NCBI_TaxID=302272;
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].
RC   STRAIN=Isolate MVC11, and Isolate vaccinal MVCES1;
RX   PubMed=8151795; DOI=10.1128/jvi.68.5.3369-3373.1994;
RA   Wang X.-L., Itoh M., Hotta H., Homma M.;
RT   "A protease activation mutant, MVCES1, as a safe and potent live vaccine
RT   derived from currently prevailing Sendai virus.";
RL   J. Virol. 68:3369-3373(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate MVC11;
RX   PubMed=9400971; DOI=10.1099/0022-1317-78-12-3207;
RA   Itoh M., Isegawa Y., Hotta H., Homma M.;
RT   "Isolation of an avirulent mutant of Sendai virus with two amino acid
RT   mutations from a highly virulent field strain through adaptation to LLC-MK2
RT   cells.";
RL   J. Gen. Virol. 78:3207-3215(1997).
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; D17335; BAA04154.1; -; Genomic_RNA.
DR   EMBL; AB005795; BAA24390.1; -; Genomic_RNA.
DR   EMBL; AB005796; BAA24399.1; -; Genomic_RNA.
DR   RefSeq; NP_056877.1; NC_001552.1.
DR   SMR; O57295; -.
DR   GeneID; 1489775; -.
DR   KEGG; vg:1489775; -.
DR   Proteomes; UP000006563; Genome.
DR   Proteomes; UP000007311; Genome.
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; Reference proteome; Signal;
KW   Transmembrane; 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_0000039372"
FT   CHAIN           26..116
FT                   /note="Fusion glycoprotein F2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000039373"
FT   CHAIN           117..565
FT                   /note="Fusion glycoprotein F1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000039374"
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          269..307
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        394..399
FT                   /evidence="ECO:0000250"
FT   DISULFID        401..424
FT                   /evidence="ECO:0000250"
FT   VARIANT         97
FT                   /note="E -> R (in strain: Isolate MVC11 and Isolate
FT                   vaccinal MVCES1)"
FT   VARIANT         116..117
FT                   /note="RF -> IS (in strain: Isolate vaccinal MVCES1)"
FT   VARIANT         227
FT                   /note="T -> A (in strain: Isolate MVC11 and Isolate
FT                   vaccinal MVCES1)"
FT   VARIANT         439..440
FT                   /note="KG -> ER (in strain: Isolate MVC11 and Isolate
FT                   vaccinal MVCES1)"
SQ   SEQUENCE   565 AA;  61410 MW;  0348FB2D9388DDEB CRC64;
     MATYIQRVQC ISALLSVVLT TLVSCQIPRD RLSNIGVIVD EGKSLKIAGS HESRYIVLSL
     VPGIDLENGC GTAQVIQYKS LLNRLLIPLR DALDLQEALI TVTNDTMTGA DVPQSRFFGA
     VIGTIALGVA TSAQITAGIA LAEAREAKRD IALIKESMTK THKSIELLQN AVGEQILALK
     TLQDFVNDEI KPAISELGCE TAALRLGIKL TQHYSELLTA FGSNFGTIGE KSLTLQALSS
     LYSANITEIM TTIRTGQSNI YDVIYTEQIK GTVIDVDLER YMVTLSVKIP ILSEVPGVLI
     HKASSISYNI DGEEWYVTVP SHILSRASFL GGANIADCVE SRLTYICPRD PAQLIPDSQQ
     KCILGDTTRC PVTKVVDNII PKFAFVNGGV VANCIASTCT CGTGRRPISQ DRSKGVVFLT
     HDNCGLIGVN GIELYANRKG HDATWGVQNL TVGPAIAIRP VDISLNLAAA TDFLQDSRAE
     LEKARKILSE VGRWYNSGAT LITIIVVMIV VLVVIIVIVI VLYRLRRSML MSNPAGRISR
     DTYTLEPKIR HMYTNGGFDA MTEKR