FUS_NDVD
ID FUS_NDVD Reviewed; 553 AA.
AC P35936;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 105.
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 D26/76) (NDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC Orthoavulavirus; Avian orthoavulavirus 1.
OX NCBI_TaxID=11180;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 32-499, GLYCOSYLATION AT ASN-85
RP AND ASN-447, AND DISULFIDE BONDS.
RX PubMed=11286892; DOI=10.1016/s0969-2126(01)00581-0;
RA Chen L., Gorman J.J., McKimm-Breschkin J., Lawrence L.J., Tulloch P.A.,
RA Smith B.J., Colman P.M., Lawrence M.C.;
RT "The structure of the fusion glycoprotein of Newcastle disease virus
RT suggests a novel paradigm for the molecular mechanism of membrane fusion.";
RL Structure 9:255-266(2001).
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; M24692; AAA46643.1; -; Genomic_RNA.
DR PIR; A46329; A46329.
DR PDB; 1G5G; X-ray; 3.30 A; A/B/C/D/E/F=32-499.
DR PDBsum; 1G5G; -.
DR SMR; P35936; -.
DR iPTMnet; P35936; -.
DR EvolutionaryTrace; P35936; -.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000039297"
FT CHAIN 32..116
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039298"
FT CHAIN 117..553
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039299"
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:0000269|PubMed:11286892"
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:0000269|PubMed:11286892"
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:0000269|PubMed:11286892"
FT DISULFID 338..347
FT /evidence="ECO:0000269|PubMed:11286892"
FT DISULFID 362..370
FT /evidence="ECO:0000269|PubMed:11286892"
FT DISULFID 394..399
FT /evidence="ECO:0000269|PubMed:11286892"
FT DISULFID 401..424
FT /evidence="ECO:0000269|PubMed:11286892"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1G5G"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:1G5G"
FT HELIX 74..104
FT /evidence="ECO:0007829|PDB:1G5G"
FT HELIX 172..226
FT /evidence="ECO:0007829|PDB:1G5G"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:1G5G"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:1G5G"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:1G5G"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1G5G"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:1G5G"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 293..305
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:1G5G"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:1G5G"
FT HELIX 357..363
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:1G5G"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:1G5G"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:1G5G"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:1G5G"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:1G5G"
SQ SEQUENCE 553 AA; 58892 MW; B90AA98D77CCC470 CRC64;
MGSRSSTRIP VPLMLTVRIM LALSCVCPTS SLDGRPLAAA GIVVTGDKAV NIYTSSQTGS
IIIKLLPNMP KDKEACAKAP LEAYNRTLTT LLTPLGDSIR RIQESVTTSG GGKQGRLIGA
IIGGVALGVA TAAQITAASA LIQANQNAAN ILRLKESIAA TNEAVHEVTD GLSQLAVAVG
KMQQFVNDQF NKTAQELDCI KITQQVGVEL NLYLTELTTV FGPQITSPAL TQLTIQALYN
LAGGNMDYLL TKLGVGNNQL SSLIGSGLIT GNPILYDSQT QLLGIQVTLP SVGNLNNMRA
TYLETLSVST TKGFASALVP KVVTQVGSVI EELDTSYCIE TDLDLYCTRI VTFPMSPGIY
SCLSGNTSAC MYSKTEGALT TPYMTLKGSV IANCKMTTCR CADPPGIISQ NYGEAVSLID
RQSCNILSLD GITLRLSGEF DATYQKNISI QDSQVIVTGN LDISTELGNV NNSISNALDK
LEESNSKLDK VNVKLTSTSA LITYIFLTVI SLVCGILSLV LACYLMYKQK AQQKTLLWLG
NNTLDQMRAT TKM
