FUS_BRSVA
ID FUS_BRSVA Reviewed; 572 AA.
AC P29791; Q8V688; Q8V691;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Fusion glycoprotein F0;
DE Contains:
DE RecName: Full=Fusion glycoprotein F2 {ECO:0000250|UniProtKB:P03420};
DE Short=F2;
DE Contains:
DE RecName: Full=p27 {ECO:0000250|UniProtKB:P03420};
DE AltName: Full=Intervening segment;
DE AltName: Full=Pep27;
DE AltName: Full=Peptide 27;
DE Contains:
DE RecName: Full=Fusion glycoprotein F1 {ECO:0000250|UniProtKB:P03420};
DE Short=F1;
DE Flags: Precursor;
GN Name=F;
OS Bovine respiratory syncytial virus (strain A51908) (BRS).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11247;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1312130; DOI=10.1099/0022-1317-73-3-737;
RA Zamora M., Samal S.K.;
RT "Sequence analysis of M2 mRNA of bovine respiratory syncytial virus
RT obtained from an F-M2 dicistronic mRNA suggests structural homology with
RT that of human respiratory syncytial virus.";
RL J. Gen. Virol. 73:737-741(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=A51908, and ATCC 51908;
RX PubMed=11724268; DOI=10.1023/a:1011888019966;
RA Yunus A.S., Khattar S.K., Collins P.L., Samal S.K.;
RT "Rescue of bovine respiratory syncytial virus from cloned cDNA: entire
RT genome sequence of BRSV strain A51908.";
RL Virus Genes 23:157-164(2001).
RN [3]
RP HEPARAN SULFATE BINDING.
RX PubMed=11172105; DOI=10.1099/0022-1317-82-3-631;
RA Karger A., Schmidt U., Buchholz U.J.;
RT "Recombinant bovine respiratory syncytial virus with deletions of the G or
RT SH genes: G and F proteins bind heparin.";
RL J. Gen. Virol. 82:631-640(2001).
CC -!- FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved
CC at two sites by a furin-like protease to give rise to the mature F1 and
CC F2 fusion glycoproteins. {ECO:0000250|UniProtKB:P03420}.
CC -!- FUNCTION: [Fusion glycoprotein F1]: Class I viral fusion protein. Under
CC the current model, the protein has at least 3 conformational states:
CC pre-fusion native state, pre-hairpin intermediate state, and post-
CC fusion hairpin state. During viral and plasma cell membrane fusion, the
CC coiled coil regions assume a trimer-of-hairpins structure, positioning
CC the fusion peptide in close proximity to the C-terminal region of the
CC ectodomain. The formation of this structure appears to drive apposition
CC and subsequent fusion of viral and cellular membranes leading to
CC delivery of the nucleocapsid into the cytoplasm. This fusion is pH
CC independent and occurs at the plasma or endosomal membrane. The trimer
CC of F1-F2 (F protein) also facilitates the attachment and entry into the
CC host cell. Later in infection, F protein expressed at the plasma
CC membrane of infected cells can mediate fusion with adjacent cells to
CC form syncytia, a cytopathic effect that could lead to tissue necrosis.
CC {ECO:0000250|UniProtKB:P03420}.
CC -!- FUNCTION: [Fusion glycoprotein F2]: Major determinant of the species
CC specificity of RSV infection. The trimer of F1-F2 (F protein) also
CC facilitates the attachment and entry into the host cell. Later in
CC infection, F protein expressed at the plasma membrane of infected cells
CC can mediate fusion with adjacent cells to form syncytia, a cytopathic
CC effect that could lead to tissue necrosis.
CC {ECO:0000250|UniProtKB:P03420}.
CC -!- SUBUNIT: [Fusion glycoprotein F1]: Homotrimer. Heterodimer with fusion
CC protein F2; disulfide-linked. Part of a complex composed of F1, F2 and
CC G glycoproteins. As a heterodimer with F2, interacts with host RHOA;
CC this interaction facilitates virus-induced syncytium formation.
CC {ECO:0000250|UniProtKB:P03420}.
CC -!- SUBUNIT: [Fusion glycoprotein F2]: Homotrimer. Heterodimer with fusion
CC protein F1; disulfide-linked. Part of a complex composed of F1, F2 and
CC G glycoproteins. As a heterodimer with F1, interacts with host RHOA;
CC this interaction facilitates virus-induced syncytium formation.
CC {ECO:0000250|UniProtKB:P03420}.
CC -!- SUBCELLULAR LOCATION: [Fusion glycoprotein F0]: Host Golgi apparatus
CC membrane {ECO:0000250|UniProtKB:P03420}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P03420}.
CC -!- SUBCELLULAR LOCATION: [Fusion glycoprotein F1]: Virion membrane
CC {ECO:0000250|UniProtKB:P03420}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P03420}. Host cell membrane
CC {ECO:0000250|UniProtKB:P03420}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P03420}. Note=Localized at the host apical
CC membrane. {ECO:0000250|UniProtKB:P03420}.
CC -!- SUBCELLULAR LOCATION: [Fusion glycoprotein F2]: Virion membrane
CC {ECO:0000250|UniProtKB:P03420}. Host cell membrane
CC {ECO:0000250|UniProtKB:P03420}. Note=Localized at the host apical
CC membrane. {ECO:0000250|UniProtKB:P03420}.
CC -!- DOMAIN: [Fusion glycoprotein F0]: The N-terminus is a hydrophobic
CC fusion peptide that inserts into the target host membrane (By
CC similarity). It is buried in the center of the trimer cavity before
CC cleavage by host furin. The coiled coil (heptad repeat) regions are
CC probably involved in homotrimerization, heterodimerization and in the
CC formation of a fusion-active hairpin structure (By similarity).
CC {ECO:0000250|UniProtKB:P03420, ECO:0000250|UniProtKB:P11209}.
CC -!- DOMAIN: [Fusion glycoprotein F1]: The N-terminus is a hydrophobic
CC fusion peptide that inserts into the target host membrane (By
CC similarity). It is buried in the center of the trimer cavity before
CC cleavage by host furin. The coiled coil (heptad repeat) regions are
CC probably involved in homotrimerization, heterodimerization and in the
CC formation of a fusion-active hairpin structure (By similarity).
CC {ECO:0000250|UniProtKB:P03420, ECO:0000250|UniProtKB:P11209}.
CC -!- PTM: [Fusion glycoprotein F0]: The F glycoprotein is synthesized as a
CC F0 inactive precursor that is heavily N-glycosylated and processed at
CC two sites by a host furin-like protease probably in the Golgi. The
CC cleavage site between p27 and F1 may occur after endocytosis to yield
CC the mature F1 and F2 proteins. Both cleavages are required for membrane
CC fusion and p27 is released from the processed protein.
CC {ECO:0000250|UniProtKB:P03420}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; M82816; AAA42804.1; -; mRNA.
DR EMBL; AF295543; AAL49399.1; -; Genomic_RNA.
DR EMBL; AF295544; AAL49410.1; -; Genomic_RNA.
DR PIR; JQ1481; VGNZBA.
DR SMR; P29791; -.
DR Proteomes; UP000007616; Genome.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
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:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0060141; P:positive regulation of syncytium formation by virus; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR000776; Fusion_F0_Paramyxovir.
DR InterPro; IPR013055; Tachy_Neuro_lke_CS.
DR Pfam; PF00523; Fusion_gly; 1.
PE 1: Evidence at protein level;
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 Golgi apparatus; Host membrane;
KW Host-virus interaction; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Syncytium formation induced by viral infection;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral attachment to host entry receptor; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..572
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039225"
FT CHAIN 26..109
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039226"
FT PEPTIDE 110..136
FT /note="p27"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT /id="PRO_0000432658"
FT CHAIN 137..572
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039227"
FT TOPO_DOM 26..522
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT TRANSMEM 523..548
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT TOPO_DOM 549..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT REGION 137..157
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P11209"
FT COILED 76..96
FT /evidence="ECO:0000250|UniProtKB:P11209"
FT COILED 156..207
FT /evidence="ECO:0000250|UniProtKB:P11209"
FT COILED 479..514
FT /evidence="ECO:0000250|UniProtKB:P11209"
FT SITE 109..110
FT /note="Cleavage; by host furin-like protease"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT SITE 136..137
FT /note="Cleavage; by host furin-like protease"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT LIPID 548
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 37..437
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 69..212
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 311..341
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 320..331
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 356..365
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 380..391
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 414..420
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT VARIANT 5
FT /note="T -> A (in strain: ATCC 51908)"
FT VARIANT 14
FT /note="L -> F (in strain: ATCC 51908)"
FT VARIANT 20
FT /note="P -> T (in strain: ATCC 51908)"
FT VARIANT 71
FT /note="G -> S (in strain: ATCC 51908)"
FT VARIANT 91
FT /note="A -> V"
FT VARIANT 102..104
FT /note="TSS -> ASF (in strain: ATCC 51908)"
FT VARIANT 114
FT /note="S -> L (in strain: ATCC 51908)"
FT VARIANT 216..218
FT /note="NIA -> KIE (in strain: ATCC 51908)"
FT VARIANT 260
FT /note="I -> L (in strain: ATCC 51908)"
FT VARIANT 276..277
FT /note="VC -> SNV"
FT VARIANT 291..292
FT /note="LR -> VKE"
FT VARIANT 303
FT /note="L -> I (in strain: ATCC 51908)"
FT VARIANT 325
FT /note="K -> E"
FT VARIANT 353
FT /note="A -> T (in strain: ATCC 51908)"
FT VARIANT 387
FT /note="S -> A"
FT VARIANT 387
FT /note="S -> T (in strain: ATCC 51908)"
FT VARIANT 477
FT /note="N -> D (in strain: ATCC 51908)"
FT VARIANT 541
FT /note="T -> A (in strain: ATCC 51908)"
FT VARIANT 551
FT /note="R -> K (in strain: ATCC 51908)"
FT VARIANT 564
FT /note="S -> G (in strain: ATCC 51908)"
SQ 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
