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Fusion glycoprotein F0 [Cleaved into: Fusion glycoprotein F2'; Interchain peptide; Fusion glycoprotein F2; Fusion glycoprotein F1]

 FUS_BRSVA               Reviewed;         572 AA.
P29791; Q8V688; Q8V691;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
23-MAY-2018, entry version 92.
RecName: Full=Fusion glycoprotein F0;
Contains:
RecName: Full=Fusion glycoprotein F2' {ECO:0000250|UniProtKB:P03420};
Contains:
RecName: Full=Interchain peptide {ECO:0000250|UniProtKB:P03420};
Contains:
RecName: Full=Fusion glycoprotein F2;
Contains:
RecName: Full=Fusion glycoprotein F1;
Flags: Precursor;
Name=F;
Bovine respiratory syncytial virus (strain A51908) (BRS).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Pneumoviridae; Orthopneumovirus.
NCBI_TaxID=11247;
NCBI_TaxID=9913; Bos taurus (Bovine).
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1312130; DOI=10.1099/0022-1317-73-3-737;
Zamora M., Samal S.K.;
"Sequence analysis of M2 mRNA of bovine respiratory syncytial virus
obtained from an F-M2 dicistronic mRNA suggests structural homology
with that of human respiratory syncytial virus.";
J. Gen. Virol. 73:737-741(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=A51908, and ATCC 51908;
PubMed=11724268; DOI=10.1023/A:1011888019966;
Yunus A.S., Khattar S.K., Collins P.L., Samal S.K.;
"Rescue of bovine respiratory syncytial virus from cloned cDNA: entire
genome sequence of BRSV strain A51908.";
Virus Genes 23:157-164(2001).
[3]
HEPARAN SULFATE BINDING.
PubMed=11172105;
Karger A., Schmidt U., Buchholz U.J.;
"Recombinant bovine respiratory syncytial virus with deletions of the
G or SH genes: G and F proteins bind heparin.";
J. Gen. Virol. 82:631-640(2001).
-!- FUNCTION: During virus entry, induces fusion of viral and cellular
membranes leading to delivery of the nucleocapsid into the
cytoplasm. The fusogenic activity is inactive untill entry into
host cell endosome, where a furin-like protease cleaves off a
small peptide between F1 and F2. Interacts directly with heparan
sulfate and may participate in virus attachment. Later in
infection, proteins F expressed at the plasma membrane of infected
cells can mediate fusion with adjacent cells to form syncytia, a
cytopathic effect that could lead to tissue necrosis. The fusion
protein is also able to trigger p53-dependent apoptosis.
{ECO:0000250|UniProtKB:P03420}.
-!- SUBUNIT: Homotrimer. Interacts with glycoprotein G. Interacts with
host RHOA; this interaction facilitates virus-induced syncytium
formation. {ECO:0000250|UniProtKB:P03420}.
-!- SUBCELLULAR LOCATION: Virion membrane
{ECO:0000250|UniProtKB:P03420}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P03420}. Host cell membrane
{ECO:0000250|UniProtKB:P03420}; Single-pass membrane protein
{ECO:0000250|UniProtKB:P03420}.
-!- PTM: The F glycoprotein is synthesized as a F0 inactive precursor
that is heavily N-glycosylated and processed by host cell furin in
the Golgi to yield the mature F1 and F2 proteins. The cleavage
site between F1 and F2 requires the minimal sequence [KR]-X-[KR]-
R. During entry a furin-like protease cleaves F2 into F2' and a
small peptide, leading to the activation of fusogenic function.
{ECO:0000250|UniProtKB:P03420}.
-!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M82816; AAA42804.1; -; mRNA.
EMBL; AF295543; AAL49399.1; -; Genomic_RNA.
EMBL; AF295544; AAL49410.1; -; Genomic_RNA.
PIR; JQ1481; VGNZBA.
ProteinModelPortal; P29791; -.
SMR; P29791; -.
PRIDE; P29791; -.
OrthoDB; VOG0900006Q; -.
Proteomes; UP000007616; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
GO; GO:0060141; P:positive regulation of syncytium formation by virus; IEA:UniProtKB-KW.
InterPro; IPR000776; Fusion_F0_Paramyxovir.
InterPro; IPR013055; Tachy_Neuro_lke_CS.
Pfam; PF00523; Fusion_gly; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Coiled coil; Complete proteome;
Disulfide bond; Fusion of virus membrane with host cell membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Lipoprotein; Membrane; Palmitate;
Reference proteome; Signal;
Syncytium formation induced by viral infection; Transmembrane;
Transmembrane helix; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 572 Fusion glycoprotein F0.
/FTId=PRO_0000039225.
CHAIN 26 136 Fusion glycoprotein F2.
/FTId=PRO_0000039226.
CHAIN 26 109 Fusion glycoprotein F2'.
{ECO:0000250|UniProtKB:P03420}.
/FTId=PRO_0000432657.
PEPTIDE 110 136 Interchain peptide.
{ECO:0000250|UniProtKB:P03420}.
/FTId=PRO_0000432658.
CHAIN 137 572 Fusion glycoprotein F1.
/FTId=PRO_0000039227.
TOPO_DOM 26 527 Extracellular. {ECO:0000250}.
TRANSMEM 528 548 Helical. {ECO:0000255}.
TOPO_DOM 549 572 Cytoplasmic. {ECO:0000250}.
REGION 137 157 Fusion peptide. {ECO:0000250}.
COILED 155 183 {ECO:0000255}.
COILED 489 514 {ECO:0000255}.
SITE 109 110 Cleavage; by host.
{ECO:0000250|UniProtKB:P03420}.
SITE 136 137 Cleavage; by host. {ECO:0000250}.
SITE 136 137 Cleavage; by host furin.
{ECO:0000250|UniProtKB:P03420}.
LIPID 548 548 S-palmitoyl cysteine; by host.
{ECO:0000250|UniProtKB:P03420}.
CARBOHYD 27 27 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 69 212 Interchain (between F2 and F1 chains).
{ECO:0000250}.
DISULFID 356 365 {ECO:0000250}.
DISULFID 380 391 {ECO:0000250}.
VARIANT 5 5 T -> A (in strain: ATCC 51908).
VARIANT 14 14 L -> F (in strain: ATCC 51908).
VARIANT 20 20 P -> T (in strain: ATCC 51908).
VARIANT 71 71 G -> S (in strain: ATCC 51908).
VARIANT 91 91 A -> V.
VARIANT 102 104 TSS -> ASF (in strain: ATCC 51908).
VARIANT 114 114 S -> L (in strain: ATCC 51908).
VARIANT 216 218 NIA -> KIE (in strain: ATCC 51908).
VARIANT 260 260 I -> L (in strain: ATCC 51908).
VARIANT 276 277 VC -> SNV.
VARIANT 291 292 LR -> VKE.
VARIANT 303 303 L -> I (in strain: ATCC 51908).
VARIANT 325 325 K -> E.
VARIANT 353 353 A -> T (in strain: ATCC 51908).
VARIANT 387 387 S -> A.
VARIANT 387 387 S -> T (in strain: ATCC 51908).
VARIANT 477 477 N -> D (in strain: ATCC 51908).
VARIANT 541 541 T -> A (in strain: ATCC 51908).
VARIANT 551 551 R -> K (in strain: ATCC 51908).
VARIANT 564 564 S -> G (in strain: ATCC 51908).
SEQUENCE 572 AA; 63443 MW; A055E5E65801663E CRC64;
MATTTMRMII SIILISTYVP HITLCQNITE EFYQSTCSAV SRGYLSALRT GWYTSVVTIE
LSKIQKNVCN GTDSKVKLIK QELERYNNAV AELQSLMQNE PTSSSRAKRG IPESIHYTRN
STKKFYGLMG KKRKRRFLGF LLGIGSAIAS GVAVSKVLHL EGEVNKIKNA LLSTNKAVVS
LSNGVSVLTS KVLDLKNYID KELLPKVNNH DCRISNIATV IEFQQKNNRL LEIAREFSVN
AGITTPLSTY MLTNSELLSI INDMPITNDQ KKLMSVCQIV RQQSYSIMSV LREVIAYVVQ
LPLYGVIDTP CWKLHTSPLC TTDNKEGSNI CLTRTDRGWY CDNAGSVSFF PQAETCKVQS
NRVFCDTMNS LTLPTDVNLC NTDIFNSKYD CKIMTSKTDI SSSVITSIGA IVSCYGKTKC
TASNKNRGII KTFSNGCDYV SNKGVDTVSV GNTLYYVNKL EGKALYIKGE PIINYYNPLV
FPSDEFDASI AQVNAKINQS LAFIRRSDEL LHSVDVGKST TNVVITTIII VIVVVILMLI
TVGLLFYCKT RSTPIMLGKD QLSSINNLSF SK


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