FUS_MPV15
ID FUS_MPV15 Reviewed; 537 AA.
AC P35949; Q5MKM2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 112.
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 Murine pneumonia virus (strain 15) (MPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=296738;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1629698; DOI=10.1099/0022-1317-73-7-1717;
RA Chambers P., Pringle C.R., Easton A.J.;
RT "Sequence analysis of the gene encoding the fusion glycoprotein of
RT pneumonia virus of mice suggests possible conserved secondary structure
RT elements in paramyxovirus fusion glycoproteins.";
RL J. Gen. Virol. 73:1717-1724(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15604443; DOI=10.1099/vir.0.80315-0;
RA Thorpe L.C., Easton A.J.;
RT "Genome sequence of the non-pathogenic strain 15 of pneumonia virus of mice
RT and comparison with the genome of the pathogenic strain J3666.";
RL J. Gen. Virol. 86:159-169(2005).
CC -!- FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved
CC by a furin-like protease to give rise to the mature F1 and F2 fusion
CC 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. {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. {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 by a
CC host furin-like protease probably in the Golgi.
CC {ECO:0000250|UniProtKB:P03420}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; AY743910; AAW02840.1; -; Genomic_RNA.
DR PIR; JQ1619; JQ1619.
DR SMR; P35949; -.
DR Proteomes; UP000133604; 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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR000776; Fusion_F0_Paramyxovir.
DR Pfam; PF00523; Fusion_gly; 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 Golgi apparatus; Host membrane;
KW Host-virus interaction; Membrane; Reference proteome; Signal;
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..537
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039348"
FT CHAIN 22..101
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039349"
FT CHAIN 102..537
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039350"
FT TOPO_DOM 26..486
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT TRANSMEM 487..515
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT TOPO_DOM 516..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT REGION 102..122
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P11209"
FT COILED 120..174
FT /evidence="ECO:0000255"
FT COILED 444..479
FT /evidence="ECO:0000255"
FT SITE 101..102
FT /note="Cleavage; by host furin-like protease"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 33..402
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 65..177
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 278..306
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 287..296
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 321..330
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 345..356
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 379..385
FT /evidence="ECO:0000250|UniProtKB:P03420"
SQ SEQUENCE 537 AA; 59367 MW; BA6116EE2FABE702 CRC64;
MIPGRIFLVL LVIFNTKPIH PNTLTEKYYE STCSVETAGY KSALRTGWHM TVMSIKLSQI
NIESCKSSNS LLAHELAIYS SAVDELRTLS SNALKSKRKK RFLGLILGLG AAVTAGVALA
KTVQLESEIA LIRDAVRNTN EAVVSLTNGM SVLAKVVDDL KNFISKELLP KINRVSCDVH
DITAVIRFQQ LNKRLLEVSR EFSSNAGLTH TVSSFMLTDR ELTSIVGGMA VSAGQKEIML
SSKAIMRRNG LAILSSVNAD TLVYVIQLPL FGVMDTDCWV IRSSIDCHNI ADKYACLARA
DNGWYCHNAG SLSYFPSPTD CEIHNGYAFC DTLKSLTVPV TSRECNSNMY TTNYDCKIST
SKTYVSTAVL TTMGCLVSCY GHNSCTVINN DKGIIRTLPD GCHYISNKGV DRVQVGNTVY
YLSKEVGKSI VVRGEPLVLK YDPLSFPDDK FDVAIRDVEH SINQTRTFFK ASDQLLDLSE
NRENKNLNKS YILTTLLFVV MLIIIMAVIG FILYKVLKMI RDNKLKSKST PGLTVLS
