FUS_HRSVB
ID FUS_HRSVB Reviewed; 574 AA.
AC O36634;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Fusion glycoprotein F0;
DE Short=Protein F;
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 Human respiratory syncytial virus B (strain B1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=79692;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9391135; DOI=10.1073/pnas.94.25.13961;
RA Karron R.A., Buonagurio D.A., Georgiu A.F., Whitehead S.S., Adamus J.E.,
RA Clements-Mann M.L., Harris D.O., Randolph V.B., Udem S.A., Murphy B.R.,
RA Sidhu M.S.;
RT "Respiratory syncytial virus (RSV) SH and G proteins are not essential for
RT viral replication in vitro: clinical evaluation and molecular
RT characterization of a cold-passaged, attenuated RSV subgroup B mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13961-13966(1997).
RN [2]
RP PALMITOYLATION AT CYS-550.
RX PubMed=2732224; DOI=10.1016/s0021-9258(18)81623-4;
RA Arumugham R.G., Seid R.C. Jr., Doyle S., Hildreth S.W., Paradisio P.R.;
RT "Fatty acid acylation of the fusion glycoprotein of human respiratory
RT syncytial virus.";
RL J. Biol. Chem. 264:10339-10342(1989).
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 to host cell by
CC binding to host heparan sulfate. F protein is involved in the entry
CC into the host cell through the interaction with host IGFR1. This
CC interaction activates PRKCZ/PKCzeta that recruits host NCL/nucleolin to
CC the apical cell surface where it can bind fusion glycoprotein F1. Later
CC in infection, F protein expressed at the plasma membrane of infected
CC cells can mediate fusion with adjacent cells to form syncytia, a
CC cytopathic effect that could lead to tissue necrosis. F protein may
CC trigger p53-dependent apoptosis. {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 to host cell by binding to host heparan
CC sulfate. F protein is involved in the entry into the host cell through
CC the interaction with host IGFR1. This interaction activates
CC PRKCZ/PKCzeta that recruits host NCL/nucleolin to the apical cell
CC surface where it can bind fusion glycoprotein F1. Later in infection, F
CC protein expressed at the plasma membrane of infected cells can mediate
CC fusion with adjacent cells to form syncytia, a cytopathic effect that
CC could lead to tissue necrosis. F protein seems to trigger p53-dependent
CC apoptosis. {ECO:0000250|UniProtKB:P03420}.
CC -!- SUBUNIT: [Fusion glycoprotein F1]: Homotrimer. Heterodimer with fusion
CC protein F2; disulfide-linked. Interacts with host NCL; this interaction
CC plays a role in viral entry into the host cell. As a heterodimer with
CC F2, interacts with host heparan sulfate. As a heterodimer with F2,
CC interacts with host IGFR1; this interaction activates PRKCZ/PKCzeta
CC that recruits NCL/nucleolin from the host nucleus to the plasma
CC membrane. Part of a complex composed of F1, F2 and G glycoproteins. As
CC a heterodimer with F2, interacts with host RHOA; this interaction
CC facilitates virus-induced syncytium formation.
CC {ECO:0000250|UniProtKB:P03420}.
CC -!- SUBUNIT: [Fusion glycoprotein F2]: Homotrimer. Heterodimer with fusion
CC protein F1; disulfide-linked. As a heterodimer with F1, interacts with
CC host heparan sulfate. As a heterodimer with F1, interacts with host
CC IGFR1; this interaction activates PRKCZ/PKCzeta that recruits
CC NCL/nucleolin from the host nucleus to the plasma membrane. Part of a
CC complex composed of F1, F2 and G glycoproteins. As a heterodimer with
CC F1, interacts with host RHOA; this interaction facilitates virus-
CC induced syncytium formation. {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; AF013254; AAB82436.1; -; Genomic_RNA.
DR RefSeq; NP_056863.1; NC_001781.1.
DR SMR; O36634; -.
DR PRIDE; O36634; -.
DR ABCD; O36634; 3 sequenced antibodies.
DR GeneID; 1489825; -.
DR KEGG; vg:1489825; -.
DR Proteomes; UP000002472; 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 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..574
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000390376"
FT CHAIN 26..109
FT /note="Fusion glycoprotein F2"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT /id="PRO_0000390377"
FT PEPTIDE 110..136
FT /note="p27"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT /id="PRO_0000432668"
FT CHAIN 137..574
FT /note="Fusion glycoprotein F1"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT /id="PRO_0000390378"
FT TOPO_DOM 26..524
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT TRANSMEM 525..550
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT TOPO_DOM 551..574
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 158..209
FT /evidence="ECO:0000250|UniProtKB:P11209"
FT COILED 481..516
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 550
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:2732224"
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 116
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 37..439
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 313..343
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 322..333
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 358..367
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 382..393
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 416..422
FT /evidence="ECO:0000250|UniProtKB:P03420"
SQ SEQUENCE 574 AA; 63710 MW; 29A127B128BF5E92 CRC64;
MELLIHRLSA IFLTLAINAL YLTSSQNITE EFYQSTCSAV SRGYFSALRT GWYTSVITIE
LSNIKETKCN GTDTKVKLIK QELDKYKNAV TELQLLMQNT PAANNRARRE APQYMNYTIN
TTKNLNVSIS KKRKRRFLGF LLGVGSAIAS GIAVSKVLHL EGEVNKIKNA LLSTNKAVVS
LSNGVSVLTS KVLDLKNYIN NQLLPIVNQQ SCRISNIETV IEFQQKNSRL LEINREFSVN
AGVTTPLSTY MLTNSELLSL INDMPITNDQ KKLMSSNVQI VRQQSYSIMS IIKEEVLAYV
VQLPIYGVID TPCWKLHTSP LCTTNIKEGS NICLTRTDRG WYCDNAGSVS FFPQADTCKV
QSNRVFCDTM NSLTLPSEVS LCNTDIFNSK YDCKIMTSKT DISSSVITSL GAIVSCYGKT
KCTASNKNRG IIKTFSNGCD YVSNKGVDTV SVGNTLYYVN KLEGKNLYVK GEPIINYYDP
LVFPSDEFDA SISQVNEKIN QSLAFIRRSD ELLHNVNTGK STTNIMITTI IIVIIVVLLS
LIAIGLLLYC KAKNTPVTLS KDQLSGINNI AFSK
