FUS_TRTV
ID FUS_TRTV Reviewed; 538 AA.
AC P24614;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 96.
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 Turkey rhinotracheitis virus (TRTV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX NCBI_TaxID=11264;
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UK/3B/85;
RX PubMed=1990068; DOI=10.1099/0022-1317-72-1-75;
RA Yu Q., Davis P.J., Barrett T., Binns M.M., Boursnell M.E.G., Cavanagh D.;
RT "Deduced amino acid sequence of the fusion glycoprotein of turkey
RT rhinotracheitis virus has greater identity with that of human respiratory
RT syncytial virus, a pneumovirus, than that of paramyxoviruses and
RT morbilliviruses.";
RL J. Gen. Virol. 72:75-81(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 500-538.
RX PubMed=1629697; DOI=10.1099/0022-1317-73-7-1709;
RA Ling R., Easton A.J., Pringle C.R.;
RT "Sequence analysis of the 22K, SH and G genes of turkey rhinotracheitis
RT virus and their intergenic regions reveals a gene order different from that
RT of other pneumoviruses.";
RL J. Gen. Virol. 73:1709-1715(1992).
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; D00850; BAA00726.1; -; Genomic_RNA.
DR EMBL; S40185; AAB22543.1; -; mRNA.
DR PIR; JQ0938; VGNZTR.
DR SMR; P24614; -.
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 2: Evidence at transcript 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; Lipoprotein;
KW Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..538
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039246"
FT CHAIN 19..102
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039247"
FT CHAIN 103..538
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039248"
FT TOPO_DOM 19..489
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..538
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 SITE 102..103
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT LIPID 513
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
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 538 AA; 58729 MW; D95008EE15CDF4D7 CRC64;
MDVRICLLLF LISNPSSCIQ ETYNEESCST VTRGYKSVLR TGWYTNVFNL EIGNVENITC
NDGPSLIDTE LVLTKNALRE LKTVSADQVA KESRLSSPRR RRFVLGAIAL GVATAAAVTA
GVALAKTIRL EGEVKAIKNA LRNTNEAVST LGNGVRVLAT AVNDLKEFIS KKLTPAINQN
KCNIADIKMA ISFGQNNRRF LNVVRQFSDS AGITSAVSLD LMTDDELVRA INRMPTSSGQ
ISLMLNNRAM VRRKGFGILI GVYDGTVVYM VQLPIFGVIE TPCWRVVAAP LCRKEKGNYA
CILREDQGWY CTNAGSTAYY PNKDDCEVRD DYVFCDTAAG INVALEVEQC NYNISTSKYP
CKVSTGRHPV SMVALTPLGG LVSCYESVSC SIGSNKVGII KQLGKGCTHI PNNEADTITI
DNTVYQLSKV VGEQRTIKGA PVVNNFNPIL FPEDQFNVAL DQVFESIDRS QDLIDKSNDL
LGADAKSKAG IAIAIVVLVI LGIFFLLAVI YYCSRVRKTK PKHDYPATTG HSSMAYVS
