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 04-NOV-2026, entry version 113. 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; Orthoavulavirus javaense; Avian paramyxovirus 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 GlyCosmos; P10865; 6 sites, No reported glycans. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell. 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:symbiont entry into host cell; IEA:UniProtKB-KW. DR Gene3D; 1.10.287.2480; -; 1. DR Gene3D; 6.10.10.110; -; 1. DR Gene3D; 2.60.40.1690; Head and neck region of the ectodomain of NDV fusion glycoprotein; 1. DR Gene3D; 2.40.490.10; Newcastle disease virus like domain; 1. DR InterPro; IPR000776; Fusion_F0_Paramyxovir. DR Pfam; PF00523; Fusion_gly; 1. DR SUPFAM; SSF69922; Head and neck region of the ectodomain of NDV fusion glycoprotein; 1. DR SUPFAM; SSF58069; Virus ectodomain; 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 //