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Fusion glycoprotein F0 [Cleaved into: Fusion glycoprotein F2; Fusion glycoprotein F1]

 FUS_PI3H4               Reviewed;         539 AA.
P06828; Q86987;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 2.
10-MAY-2017, entry version 98.
RecName: Full=Fusion glycoprotein F0;
Contains:
RecName: Full=Fusion glycoprotein F2;
Contains:
RecName: Full=Fusion glycoprotein F1;
Flags: Precursor;
Name=F;
Human parainfluenza 3 virus (strain Wash/47885/57) (HPIV-3) (Human
parainfluenza 3 virus (strain NIH 47885)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Respirovirus.
NCBI_TaxID=11217;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3012869; DOI=10.1016/0042-6822(86)90388-0;
Spriggs M.K., Olmsted R.A., Venkatesan S., Coligan J.E., Collins P.L.;
"Fusion glycoprotein of human parainfluenza virus type 3: nucleotide
sequence of the gene, direct identification of the cleavage-activation
site, and comparison with other paramyxoviruses.";
Virology 152:241-251(1986).
[2]
NUCLEOTIDE SEQUENCE.
PubMed=3033123;
Cote M.J., Storey D.G., Kang C.Y., Dimock K.;
"Nucleotide sequence of the coding and flanking regions of the human
parainfluenza virus type 3 fusion glycoprotein gene.";
J. Gen. Virol. 68:1003-1010(1987).
[3]
NUCLEOTIDE SEQUENCE.
PubMed=2825443; DOI=10.1016/0168-1702(87)90016-5;
Galinski M.S., Mink M.A., Pons M.W.;
"Molecular cloning and sequence analysis of the human parainfluenza 3
virus genes encoding the surface glycoproteins, F and HN.";
Virus Res. 8:205-215(1987).
[4]
NUCLEOTIDE SEQUENCE.
PubMed=1311137; DOI=10.1016/0168-1702(92)90089-R;
Prinoski K., Cote M.J., Kang C.Y., Dimock K.;
"Evolution of the fusion protein gene of human parainfluenza virus
3.";
Virus Res. 22:55-69(1992).
-!- FUNCTION: Class I viral fusion protein. Under the current model,
the protein has at least 3 conformational states: pre-fusion
native state, pre-hairpin intermediate state, and post-fusion
hairpin state. During viral and plasma cell membrane fusion, the
heptad repeat (HR) regions assume a trimer-of-hairpins structure,
positioning the fusion peptide in close proximity to the C-
terminal region of the ectodomain. The formation of this structure
appears to drive apposition and subsequent fusion of viral and
plasma cell membranes. Directs fusion of viral and cellular
membranes leading to delivery of the nucleocapsid into the
cytoplasm. This fusion is pH independent and occurs directly at
the outer cell membrane. The trimer of F1-F2 (F protein) probably
interacts with HN at the virion surface. Upon HN binding to its
cellular receptor, the hydrophobic fusion peptide is unmasked and
interacts with the cellular membrane, inducing the fusion between
cell and virion membranes. Later in infection, F proteins
expressed at the plasma membrane of infected cells could mediate
fusion with adjacent cells to form syncytia, a cytopathic effect
that could lead to tissue necrosis (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homotrimer of disulfide-linked F1-F2. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Host cell membrane
{ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
-!- PTM: The inactive precursor F0 is glycosylated and proteolytically
cleaved into F1 and F2 to be functionally active. The cleavage is
mediated by cellular proteases during the transport and maturation
of the polypeptide (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X05303; CAA28932.1; -; Genomic_RNA.
EMBL; D00016; BAA00012.1; -; mRNA.
EMBL; M21649; AAA46852.1; -; Genomic_RNA.
EMBL; S82195; AAB21447.1; -; Genomic_RNA.
PIR; A26764; VGNZH3.
PIR; A47610; A47610.
PDB; 1ZTM; X-ray; 3.05 A; A/B/C=19-493.
PDBsum; 1ZTM; -.
ProteinModelPortal; P06828; -.
SMR; P06828; -.
EvolutionaryTrace; P06828; -.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
InterPro; IPR000776; Fusion_F0_Paramyxovir.
Pfam; PF00523; Fusion_gly; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues; Coiled coil;
Disulfide bond; Fusion of virus membrane with host cell membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Membrane; Signal; Transmembrane;
Transmembrane helix; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 539 Fusion glycoprotein F0.
/FTId=PRO_0000039345.
CHAIN 19 109 Fusion glycoprotein F2.
/FTId=PRO_0000039346.
CHAIN 110 539 Fusion glycoprotein F1.
/FTId=PRO_0000039347.
TOPO_DOM 19 493 Extracellular. {ECO:0000250}.
TRANSMEM 494 514 Helical. {ECO:0000250}.
TOPO_DOM 515 539 Cytoplasmic. {ECO:0000250}.
REGION 110 134 Fusion peptide. {ECO:0000250}.
COILED 135 163 {ECO:0000255}.
COILED 459 484 {ECO:0000255}.
COMPBIAS 511 514 Poly-Ile.
SITE 109 110 Cleavage; by host. {ECO:0000250}.
CARBOHYD 238 238 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 359 359 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 446 446 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 63 192 Interchain (between F2 and F1 chains).
{ECO:0000250}.
DISULFID 331 340 {ECO:0000250}.
DISULFID 355 363 {ECO:0000250}.
DISULFID 387 392 {ECO:0000250}.
DISULFID 394 417 {ECO:0000250}.
CONFLICT 35 35 P -> S (in Ref. 1; BAA00012).
{ECO:0000305}.
CONFLICT 277 277 T -> A (in Ref. 1; BAA00012).
{ECO:0000305}.
CONFLICT 295 295 R -> K (in Ref. 2 and 4). {ECO:0000305}.
CONFLICT 328 328 V -> I (in Ref. 2; CAA28932).
{ECO:0000305}.
CONFLICT 369 369 K -> T (in Ref. 2 and 4). {ECO:0000305}.
CONFLICT 450 450 A -> S (in Ref. 2; CAA28932).
{ECO:0000305}.
HELIX 26 28 {ECO:0000244|PDB:1ZTM}.
STRAND 30 32 {ECO:0000244|PDB:1ZTM}.
STRAND 36 54 {ECO:0000244|PDB:1ZTM}.
HELIX 65 93 {ECO:0000244|PDB:1ZTM}.
HELIX 144 181 {ECO:0000244|PDB:1ZTM}.
HELIX 183 214 {ECO:0000244|PDB:1ZTM}.
TURN 215 219 {ECO:0000244|PDB:1ZTM}.
HELIX 228 231 {ECO:0000244|PDB:1ZTM}.
TURN 232 234 {ECO:0000244|PDB:1ZTM}.
HELIX 239 242 {ECO:0000244|PDB:1ZTM}.
STRAND 244 246 {ECO:0000244|PDB:1ZTM}.
HELIX 250 259 {ECO:0000244|PDB:1ZTM}.
STRAND 263 270 {ECO:0000244|PDB:1ZTM}.
TURN 271 274 {ECO:0000244|PDB:1ZTM}.
STRAND 275 287 {ECO:0000244|PDB:1ZTM}.
STRAND 291 298 {ECO:0000244|PDB:1ZTM}.
STRAND 301 303 {ECO:0000244|PDB:1ZTM}.
STRAND 306 309 {ECO:0000244|PDB:1ZTM}.
STRAND 314 319 {ECO:0000244|PDB:1ZTM}.
STRAND 322 326 {ECO:0000244|PDB:1ZTM}.
STRAND 335 342 {ECO:0000244|PDB:1ZTM}.
HELIX 350 357 {ECO:0000244|PDB:1ZTM}.
HELIX 360 362 {ECO:0000244|PDB:1ZTM}.
STRAND 375 378 {ECO:0000244|PDB:1ZTM}.
STRAND 380 385 {ECO:0000244|PDB:1ZTM}.
TURN 387 389 {ECO:0000244|PDB:1ZTM}.
STRAND 392 396 {ECO:0000244|PDB:1ZTM}.
STRAND 410 413 {ECO:0000244|PDB:1ZTM}.
TURN 414 416 {ECO:0000244|PDB:1ZTM}.
STRAND 418 422 {ECO:0000244|PDB:1ZTM}.
STRAND 425 427 {ECO:0000244|PDB:1ZTM}.
STRAND 436 438 {ECO:0000244|PDB:1ZTM}.
HELIX 457 480 {ECO:0000244|PDB:1ZTM}.
SEQUENCE 539 AA; 60060 MW; E94F4BDB1E658BE5 CRC64;
MPTSILLIIT TMIMASFCQI DITKLQHVGV LVNSPKGMKI SQNFETRYLI LSLIPKIEDS
NSCGDQQIKQ YKRLLDRLII PLYDGLRLQK DVIVSNQESN ENTDPRTKRF FGGVIGTIAL
GVATSAQITA AVALVEAKQA RSDIEKLKEA IRDTNKAVQS VQSSIGNLIV AIKSVQDYVN
KEIVPSIARL GCEAAGLQLG IALTQHYSEL TNIFGDNIGS LQEKGIKLQG IASLYRTNIT
EIFTTSTVDK YDIYDLLFTE SIKVRVIDVD LNDYSITLQV RLPLLTRLLN TQIYRVDSIS
YNIQNREWYI PLPSHIMTKG AFLGGADVKE CIEAFSSYIC PSDPGFVLNH EMESCLSGNI
SQCPRTVVKS DIVPRYAFVN GGVVANCITT TCTCNGIGNR INQPPDQGVK IITHKECNTI
GINGMLFNTN KEGTLAFYTP NDITLNNSVA LDPIDISIEL NKAKSDLEES KEWIRRSNQK
LDSIGNWHQS STTIIIVLIM IIILFIINVT IIIIAVKYYR IQKRNRVDQN DKPYVLTNK


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