P10865 (FUS_NDVM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fusion glycoprotein F0

Cleaved into the following 2 chains:

1. Fusion glycoprotein F2
2. Fusion glycoprotein F1

Gene names

Name:

F

Organism

Newcastle disease virus (strain Miyadera/51) (NDV)

Taxonomic identifier

11185 [NCBI]

Taxonomic lineage

Viruses › ssRNA viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Paramyxovirinae › Avulavirus › Newcastle disease virus

Virus host

Gallus gallus (Chicken) [TaxID: 9031]

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis By similarity.
Subunit structure	Homotrimer of disulfide-linked F1-F2 By similarity.
Subcellular location	Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass membrane protein By similarity.
Post-translational modification	The inactive precursor F0 is glycosylated and proteolytically cleaved into F1 and F2 to be functionally active. The cleavage is mediated by cellular proteases during the transport and maturation of the polypeptide By similarity.
Sequence similarities	Belongs to the paramyxoviruses fusion glycoprotein family.

Ontologies

Keywords
Biological process	Fusion of virus membrane with host cell membrane Fusion of virus membrane with host membrane Viral penetration into host cytoplasm Virus entry into host cell
Cellular component	Host cell membrane Host membrane Membrane Viral envelope protein Virion
Domain	Coiled coil Signal Transmembrane Transmembrane helix
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Lipoprotein Palmitate
Gene Ontology (GO)
Biological_process	induction by virus of host cell-cell fusion Inferred from electronic annotation. Source: InterPro viral entry into host cell via membrane fusion with the plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Inferred from electronic annotation. Source: UniProtKB-KW virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Potential
	Chain	32 – 553	522	Fusion glycoprotein F0		PRO_0000039312
	Chain	32 – 116	85	Fusion glycoprotein F2		PRO_0000039313
	Chain	117 – 553	437	Fusion glycoprotein F1		PRO_0000039314
Regions
	Topological domain	32 – 500	469	Extracellular By similarity
	Transmembrane	501 – 521	21	Helical; By similarity
	Topological domain	522 – 553	32	Cytoplasmic By similarity
	Region	117 – 141	25	Fusion peptide By similarity
	Coiled coil	142 – 170	29	Potential
	Coiled coil	466 – 491	26	Potential
Sites
	Site	116 – 117	2	Cleavage; by host By similarity
Amino acid modifications
	Lipidation	523	1	S-palmitoyl cysteine; by host Potential
	Glycosylation	85	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	191	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	192	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	366	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	447	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	471	1	N-linked (GlcNAc...); by host Potential
	Disulfide bond	76 ↔ 199		Interchain (between F2 and F1 chains) By similarity
	Disulfide bond	338 ↔ 347		By similarity
	Disulfide bond	362 ↔ 370		By similarity
	Disulfide bond	394 ↔ 399		By similarity
	Disulfide bond	401 ↔ 424		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P10865 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 9AEEE7D60A8FAC2A	FASTA	553	59,059
	10 20 30 40 50 60 MASRSSTRIP APLMLTIWIA LALGCVRLTS SLDGRPLAAA GIVVTGDKAV NIYTSSQTGS 70 80 90 100 110 120 IIIKLLPNMP KDKEACAKAP LEAYNRTLTT LLTPLGDSIR RIQESVTTSG GRRQRRFIGA 130 140 150 160 170 180 IIGSVALGVA TAAQITAASA LIQANQNAAN ILRLKESIAA TNEAVHEVTD GLSQLAVAVG 190 200 210 220 230 240 KMQQFVNDQF NNTTQELDCI KITHEVGVEL NLYLTELTTV FGPQITSPAL NQLTIQALYN 250 260 270 280 290 300 LAGGNMDYLL TKLGLGNNQL SSLIGSGLIT GNPILYDSQT QLLGIQVTLP SVGNLNNMRA 310 320 330 340 350 360 TYLETSSVST TKGFASALVP KVVTQVGSVI EELDTSYCIE TDLDLYCTRI VTFPMSPGIY 370 380 390 400 410 420 SCLTGNTSAC MYSKTEGALT TPYMTLKGSV IANCKMTTCR CADPPGIISQ NYGEAVSLID 430 440 450 460 470 480 RHSCNVLSLD GITLRLSGEF DAAYQKNVSI LNSQVIVTGN LDISTELGNA NNSISNALNK 490 500 510 520 530 540 LEESNSKLDK VNVRLTNTSA LITYIVLTVI SLVCGILSLV LACYLMHKQK AQQKTLLWLG 550 NNTLDQMRAT TKA

References

[1]	"Structural comparison of the cleavage-activation site of the fusion glycoprotein between virulent and avirulent strains of Newcastle disease virus." Toyoda T., Sakaguchi T., Imai K., Inocencio N.M., Gotoh B., Hamaguchi M., Nagai Y. Virology 158:242-247(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Newcastle disease virus evolution. II. Lack of gene recombination in generating virulent and avirulent strains." Toyoda T., Sakaguchi T., Hirota H., Gotoh B., Kuma K., Miyata T., Nagai Y. Virology 169:273-282(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M18456 Genomic RNA. Translation: AAA46639.1. M24701 Genomic RNA. Translation: AAA46651.1.
PIR	VGNZND. A26185.
3D structure databases
ProteinModelPortal	P10865.
SMR	P10865. Positions 33-454.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR000776. Fusion_F0_Paramyxovir. [Graphical view]
Pfam	PF00523. Fusion_gly. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUS_NDVM

Accession

Primary (citable) accession number: P10865

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program