ID   FUS_NDVB                Reviewed;         553 AA.
AC   P06156;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Fusion glycoprotein F0;
DE   Contains:
DE     RecName: Full=Fusion glycoprotein F2;
DE   Contains:
DE     RecName: Full=Fusion glycoprotein F1;
DE   Flags: Precursor;
GN   Name=F;
OS   Newcastle disease virus (strain Beaudette C/45) (NDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC   Orthoavulavirus; Avian orthoavulavirus 1.
OX   NCBI_TaxID=11178;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3025345; DOI=10.1099/0022-1317-67-12-2685;
RA   Chambers P., Millar N.S., Emmerson P.T.;
RT   "Nucleotide sequence of the gene encoding the fusion glycoprotein of
RT   Newcastle disease virus.";
RL   J. Gen. Virol. 67:2685-2694(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2705298; DOI=10.1016/0042-6822(89)90152-9;
RA   Toyoda T., Sakaguchi T., Hirota H., Gotoh B., Kuma K., Miyata T., Nagai Y.;
RT   "Newcastle disease virus evolution. II. Lack of gene recombination in
RT   generating virulent and avirulent strains.";
RL   Virology 169:273-282(1989).
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) probably interacts
CC       with HN 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. {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   -!- PTM: The inactive precursor F0 is glycosylated and proteolytically
CC       cleaved into F1 and F2 to be functionally active. The cleavage is
CC       mediated by cellular proteases during the transport and maturation of
CC       the polypeptide (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; X04719; CAA28426.1; -; Genomic_RNA.
DR   EMBL; M24697; AAA46648.1; -; Genomic_RNA.
DR   PIR; A27008; VGNZNV.
DR   SMR; P06156; -.
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   Cleavage on pair of basic residues; 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; Lipoprotein; Membrane; Palmitate;
KW   Signal; Transmembrane; Transmembrane helix; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..553
FT                   /note="Fusion glycoprotein F0"
FT                   /id="PRO_0000039294"
FT   CHAIN           32..116
FT                   /note="Fusion glycoprotein F2"
FT                   /id="PRO_0000039295"
FT   CHAIN           117..553
FT                   /note="Fusion glycoprotein F1"
FT                   /id="PRO_0000039296"
FT   TOPO_DOM        32..500
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        501..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        522..553
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          117..141
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000250"
FT   COILED          142..170
FT                   /evidence="ECO:0000255"
FT   COILED          466..491
FT                   /evidence="ECO:0000255"
FT   SITE            116..117
FT                   /note="Cleavage; by host"
FT                   /evidence="ECO:0000250"
FT   LIPID           523
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        471
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..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"
SQ   SEQUENCE   553 AA;  59041 MW;  63BFD1692AFDE191 CRC64;
     MGPRPSTKNP VPMMLTVRVA LVLSCICPAN SIDGRPLAAA GIVVTGDKAV NIYTSSQTGS
     IIVKLLPNLP KDKEACAKAP LDAYNRTLTT LLTPLGDSIR RIQESVTTSG GRRQKRFIGA
     IIGGVALGVA TAAQITAAAA LIQAKQNAAN ILRLKESIAA TNEAVHEVTD GLSQLAVAVG
     KMQQFVNDQF NKTAQELGCI RIAQQVGVEL NLYLTELTTV FGPQITSPAL NKLTIQALYN
     LAGGNMDYLL TKLGVGNNQL SSLIGSGLIT GNPILYDSQT QLLGIQVTLP SVGNLNNMRA
     TYLETLSVST TRGFASALVP KVVTQVGSVI EELDTSYCIE TDLDLYCTRI VTFPMSPGIY
     SCLSGNTSAC MYSKTEGALT TPYMTIKGSV IANCKMTTCR CVNPPGIISQ NYGEAVSLID
     KQSCNVLSLD GITLRLSGEF DATYQKNISI QDSQVIITGN LDISTELGNV NNSISNALNK
     LEESNSKLDK VNVKLTSTSA LITYIVLTII SLVFGILSLV LACYLMYKQK AQQKTLLWLG
     NNTLDQMRAT TKM