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

 FUS_PIV5                Reviewed;         529 AA.
P04849;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
12-SEP-2018, entry version 130.
RecName: Full=Fusion glycoprotein F0;
Contains:
RecName: Full=Fusion glycoprotein F2;
Contains:
RecName: Full=Fusion glycoprotein F1;
Flags: Precursor;
Name=F;
Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Rubulavirus.
NCBI_TaxID=11208;
NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=6093114; DOI=10.1073/pnas.81.21.6706;
Paterson R.G., Harris T.J.R., Lamb R.A.;
"Fusion protein of the paramyxovirus simian virus 5: nucleotide
sequence of mRNA predicts a highly hydrophobic glycoprotein.";
Proc. Natl. Acad. Sci. U.S.A. 81:6706-6710(1984).
[2]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 122-185 AND 440-477.
PubMed=10198633; DOI=10.1016/S1097-2765(00)80458-X;
Baker K.A., Dutch R.E., Lamb R.A., Jardetzky T.S.;
"Structural basis for paramyxovirus-mediated membrane fusion.";
Mol. Cell 3:309-319(1999).
-!- 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.
-!- 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.
-!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein
family. {ECO:0000305}.
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EMBL; K02253; AAA47881.1; -; Genomic_RNA.
EMBL; AF052755; AAC95515.1; -; Genomic_RNA.
PIR; A21688; VGNZSP.
PDB; 1SVF; X-ray; 1.40 A; A/C=122-185, B/D=440-477.
PDB; 2B9B; X-ray; 2.85 A; A/B/C=20-475.
PDB; 4GIP; X-ray; 2.00 A; A/B/C=20-100, D/E/F=103-477.
PDB; 4WSG; X-ray; 3.00 A; A/B/C=23-477.
PDBsum; 1SVF; -.
PDBsum; 2B9B; -.
PDBsum; 4GIP; -.
PDBsum; 4WSG; -.
ProteinModelPortal; P04849; -.
SMR; P04849; -.
KEGG; vg:3160801; -.
OrthoDB; VOG0900006Q; -.
EvolutionaryTrace; P04849; -.
Proteomes; UP000007232; Genome.
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.
GO; GO:0046761; P:viral budding from plasma membrane; IDA:UniProtKB.
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;
Complete proteome; 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 19 {ECO:0000255}.
CHAIN 20 529 Fusion glycoprotein F0.
/FTId=PRO_0000039378.
CHAIN 20 102 Fusion glycoprotein F2.
/FTId=PRO_0000039379.
CHAIN 103 529 Fusion glycoprotein F1.
/FTId=PRO_0000039380.
TOPO_DOM 20 487 Extracellular. {ECO:0000250}.
TRANSMEM 488 508 Helical. {ECO:0000250}.
TOPO_DOM 509 529 Cytoplasmic. {ECO:0000250}.
REGION 103 127 Fusion peptide.
COILED 128 156 {ECO:0000255}.
COILED 452 477 {ECO:0000255}.
COMPBIAS 98 102 Poly-Arg.
SITE 102 103 Cleavage; by host. {ECO:0000250}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 427 427 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 457 457 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 64 185 Interchain (between F2 and F1 chains).
{ECO:0000250}.
DISULFID 324 333 {ECO:0000250}.
DISULFID 348 356 {ECO:0000250}.
DISULFID 380 385 {ECO:0000250}.
DISULFID 387 410 {ECO:0000250}.
HELIX 22 26 {ECO:0000244|PDB:4GIP}.
TURN 27 29 {ECO:0000244|PDB:4GIP}.
STRAND 30 52 {ECO:0000244|PDB:4GIP}.
HELIX 67 93 {ECO:0000244|PDB:4GIP}.
STRAND 95 98 {ECO:0000244|PDB:4GIP}.
HELIX 110 113 {ECO:0000244|PDB:4GIP}.
STRAND 115 117 {ECO:0000244|PDB:4GIP}.
HELIX 123 174 {ECO:0000244|PDB:1SVF}.
HELIX 176 182 {ECO:0000244|PDB:1SVF}.
HELIX 185 203 {ECO:0000244|PDB:4GIP}.
TURN 204 206 {ECO:0000244|PDB:4GIP}.
HELIX 214 216 {ECO:0000244|PDB:4GIP}.
STRAND 217 219 {ECO:0000244|PDB:4WSG}.
HELIX 221 228 {ECO:0000244|PDB:4GIP}.
HELIX 229 231 {ECO:0000244|PDB:4GIP}.
HELIX 232 239 {ECO:0000244|PDB:4GIP}.
STRAND 242 244 {ECO:0000244|PDB:4GIP}.
HELIX 246 250 {ECO:0000244|PDB:4GIP}.
STRAND 256 263 {ECO:0000244|PDB:4GIP}.
TURN 264 267 {ECO:0000244|PDB:4GIP}.
STRAND 268 291 {ECO:0000244|PDB:4GIP}.
STRAND 294 296 {ECO:0000244|PDB:4GIP}.
STRAND 299 303 {ECO:0000244|PDB:4GIP}.
STRAND 307 312 {ECO:0000244|PDB:4GIP}.
STRAND 315 318 {ECO:0000244|PDB:4GIP}.
STRAND 324 326 {ECO:0000244|PDB:4GIP}.
STRAND 328 332 {ECO:0000244|PDB:4GIP}.
HELIX 343 349 {ECO:0000244|PDB:4GIP}.
HELIX 353 355 {ECO:0000244|PDB:4GIP}.
STRAND 358 360 {ECO:0000244|PDB:4GIP}.
HELIX 365 367 {ECO:0000244|PDB:4GIP}.
STRAND 368 372 {ECO:0000244|PDB:4GIP}.
STRAND 375 378 {ECO:0000244|PDB:4GIP}.
TURN 380 382 {ECO:0000244|PDB:4GIP}.
STRAND 385 389 {ECO:0000244|PDB:4GIP}.
STRAND 392 394 {ECO:0000244|PDB:4GIP}.
STRAND 401 405 {ECO:0000244|PDB:4GIP}.
TURN 407 409 {ECO:0000244|PDB:4GIP}.
STRAND 411 415 {ECO:0000244|PDB:4GIP}.
STRAND 418 421 {ECO:0000244|PDB:4GIP}.
HELIX 438 440 {ECO:0000244|PDB:4GIP}.
HELIX 450 475 {ECO:0000244|PDB:1SVF}.
SEQUENCE 529 AA; 56597 MW; 3152C37B1AEA2C7E CRC64;
MGTIIQFLVV SCLLAGAGSL DPAALMQIGV IPTNVRQLMY YTEASSAFIV VKLMPTIDSP
ISGCNITSIS SYNATVTKLL QPIGENLETI RNQLIPTRRR RRFAGVVIGL AALGVATAAQ
VTAAVALVKA NENAAAILNL KNAIQKTNAA VADVVQATQS LGTAVQAVQD HINSVVSPAI
TAANCKAQDA IIGSILNLYL TELTTIFHNQ ITNPALSPIT IQALRILLGS TLPTVVEKSF
NTQISAAELL SSGLLTGQIV GLDLTYMQMV IKIELPTLTV QPATQIIDLA TISAFINNQE
VMAQLPTRVM VTGSLIQAYP ASQCTITPNT VYCRYNDAQV LSDDTMACLQ GNLTRCTFSP
VVGSFLTRFV LFDGIVYANC RSMLCKCMQP AAVILQPSSS PVTVIDMYKC VSLQLDNLRF
TITQLANVTY NSTIKLESSQ ILSIDPLDIS QNLAAVNKSL SDALQHLAQS DTYLSAITSA
TTTSVLSIIA ICLGSLGLIL IILLSVVVWK LLTIVVANRN RMENFVYHK


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