FUS_AMPV1
ID FUS_AMPV1 Reviewed; 537 AA.
AC Q2Y2M3;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Fusion glycoprotein F0;
DE Short=Protein F;
DE Contains:
DE RecName: Full=Fusion glycoprotein F2;
DE Contains:
DE RecName: Full=Fusion glycoprotein F1;
DE Flags: Precursor;
GN Name=F;
OS Avian metapneumovirus (isolate Canada goose/Minnesota/15a/2001) (AMPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX NCBI_TaxID=652954;
OH NCBI_TaxID=8847; Anser sp. (goose).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15666873; DOI=10.1637/7208-051804r;
RA Bennett R.S., Nezworski J., Velayudhan B.T., Nagaraja K.V., Zeman D.H.,
RA Dyer N., Graham T., Lauer D.C., Njenga M.K., Halvorson D.A.;
RT "Evidence of avian pneumovirus spread beyond Minnesota among wild and
RT domestic birds in central North America.";
RL Avian Dis. 48:902-908(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16282483; DOI=10.1128/jvi.79.23.14834-14842.2005;
RA Bennett R.S., LaRue R., Shaw D., Yu Q., Nagaraja K.V., Halvorson D.A.,
RA Njenga M.K.;
RT "A wild goose metapneumovirus containing a large attachment glycoprotein is
RT avirulent but immunoprotective in domestic turkeys.";
RL J. Virol. 79:14834-14842(2005).
CC -!- FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved
CC to give rise to the mature F1 and F2 fusion glycoproteins.
CC {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. {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. {ECO:0000250|UniProtKB:P03420}.
CC -!- SUBUNIT: [Fusion glycoprotein F1]: Homotrimer. Heterodimer with fusion
CC protein F2; disulfide-linked. As a heterodimer with F2, interacts with
CC host heparan sulfate. Part of a complex composed of F1, F2 and G
CC glycoproteins. {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. Part of a complex composed of F1, F2 and G
CC 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. The coiled coil (heptad repeat) regions are probably involved
CC in homotrimerization, heterodimerization and in the formation of a
CC 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. The coiled coil (heptad repeat) regions are probably involved
CC in homotrimerization, heterodimerization and in the formation of a
CC 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.
CC {ECO:0000250|UniProtKB:P03420}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; DQ009484; AAY81657.1; -; Viral_cRNA.
DR RefSeq; YP_443840.1; NC_007652.1.
DR SMR; Q2Y2M3; -.
DR Proteomes; UP000002471; 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: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; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..537
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000390366"
FT CHAIN 19..102
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000390367"
FT CHAIN 103..537
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000390368"
FT TOPO_DOM 27..493
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 103..127
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P11209"
FT REGION 103..124
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT COILED 125..153
FT /evidence="ECO:0000255"
FT COILED 459..484
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 28..407
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 60..182
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 283..311
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 292..301
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 326..335
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 350..361
FT /evidence="ECO:0000250|UniProtKB:P03420"
FT DISULFID 384..390
FT /evidence="ECO:0000250|UniProtKB:P03420"
SQ SEQUENCE 537 AA; 58076 MW; 8820E3D3D6D1433F CRC64;
MSWKVVLLLV LLATPTGGLE ESYLEESCST VTRGYLSVLR TGWYTNVFTL EVGDVENLTC
TDGPSLIRTE LELTKNALEE LKTVSADQLA KEARIMSPRK ARFVLGAIAL GVATAAAVTA
GVAIAKTIRL EGEVAAIKGA LRKTNEAVST LGNGVRVLAT AVNDLKDFIS KKLTPAINKN
KCDISDLKMA VSFGQYNRRF LNVVRQFSDN AGITPAISLD LMTDAELVRA VSNMPTSSGQ
INLMLENRAM VRRKGFGILI GVYGSSVVYM VQLPIFGVID TPCWKVKAAP LCSGKDGSYA
CLLREDQGWY CQNAGSTVYY PNEEDCEVRS DHVFCDTAAG INVAKESEEC NRNISTTKYP
CKVSTGRHPI SMVALSPLGA LVACYDGVSC SIGSNKVGII RPLGKGCSYI SNQDADTVTI
DNPVYQLSKV EGEQHTIKGK PVSSNFDPIE FPEDQFNIAL DQVFESVEKS KNLIDQSNKI
LDSTEKGNAG FVMVIVLIVL LMLAAVGVGI FFVVKKRKAA PKFPMEMNGV NNKGFIP
