FUS_NDVM
ID FUS_NDVM Reviewed; 553 AA.
AC P10865;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 106.
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 Miyadera/51) (NDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC Orthoavulavirus; Avian orthoavulavirus 1.
OX NCBI_TaxID=11185;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3576973; DOI=10.1016/0042-6822(87)90261-3;
RA Toyoda T., Sakaguchi T., Imai K., Inocencio N.M., Gotoh B., Hamaguchi M.,
RA Nagai Y.;
RT "Structural comparison of the cleavage-activation site of the fusion
RT glycoprotein between virulent and avirulent strains of Newcastle disease
RT virus.";
RL Virology 158:242-247(1987).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M18456; AAA46639.1; -; Genomic_RNA.
DR EMBL; M24701; AAA46651.1; -; Genomic_RNA.
DR PIR; A26185; VGNZND.
DR SMR; P10865; -.
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_0000039312"
FT CHAIN 32..116
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039313"
FT CHAIN 117..553
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039314"
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 192
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; 59059 MW; 9AEEE7D60A8FAC2A CRC64;
MASRSSTRIP APLMLTIWIA LALGCVRLTS SLDGRPLAAA GIVVTGDKAV NIYTSSQTGS
IIIKLLPNMP KDKEACAKAP LEAYNRTLTT LLTPLGDSIR RIQESVTTSG GRRQRRFIGA
IIGSVALGVA TAAQITAASA LIQANQNAAN ILRLKESIAA TNEAVHEVTD GLSQLAVAVG
KMQQFVNDQF NNTTQELDCI KITHEVGVEL NLYLTELTTV FGPQITSPAL NQLTIQALYN
LAGGNMDYLL TKLGLGNNQL SSLIGSGLIT GNPILYDSQT QLLGIQVTLP SVGNLNNMRA
TYLETSSVST TKGFASALVP KVVTQVGSVI EELDTSYCIE TDLDLYCTRI VTFPMSPGIY
SCLTGNTSAC MYSKTEGALT TPYMTLKGSV IANCKMTTCR CADPPGIISQ NYGEAVSLID
RHSCNVLSLD GITLRLSGEF DAAYQKNVSI LNSQVIVTGN LDISTELGNA NNSISNALNK
LEESNSKLDK VNVRLTNTSA LITYIVLTVI SLVCGILSLV LACYLMHKQK AQQKTLLWLG
NNTLDQMRAT TKA
