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

 FUS_PI1HC               Reviewed;         555 AA.
P12605;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
10-MAY-2017, entry version 87.
RecName: Full=Fusion glycoprotein F0;
Contains:
RecName: Full=Fusion glycoprotein F2;
Contains:
RecName: Full=Fusion glycoprotein F1;
Flags: Precursor;
Name=F;
Human parainfluenza 1 virus (strain C39) (HPIV-1).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Respirovirus.
NCBI_TaxID=11210;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2847427; DOI=10.1016/0042-6822(88)90058-X;
Merson J.R., Hull R.A., Estes M.K., Kasel J.A.;
"Molecular cloning and sequence determination of the fusion protein
gene of human parainfluenza virus type 1.";
Virology 167:97-105(1988).
-!- 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; M22347; AAA46800.1; -; mRNA.
PIR; A31287; VGNZ11.
ProteinModelPortal; P12605; -.
SMR; P12605; -.
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.
2: Evidence at transcript level;
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 21 {ECO:0000255}.
CHAIN 22 555 Fusion glycoprotein F0.
/FTId=PRO_0000039330.
CHAIN 22 112 Fusion glycoprotein F2.
/FTId=PRO_0000039331.
CHAIN 113 555 Fusion glycoprotein F1.
/FTId=PRO_0000039332.
TOPO_DOM 22 496 Extracellular. {ECO:0000250}.
TRANSMEM 497 517 Helical. {ECO:0000250}.
TOPO_DOM 518 555 Cytoplasmic. {ECO:0000250}.
REGION 113 137 Fusion peptide. {ECO:0000250}.
COILED 138 166 {ECO:0000255}.
COILED 462 487 {ECO:0000255}.
COMPBIAS 498 503 Poly-Ile.
COMPBIAS 506 511 Poly-Ile.
SITE 112 113 Cleavage; by host. {ECO:0000250}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 66 195 Interchain (between F2 and F1 chains).
{ECO:0000250}.
DISULFID 334 343 {ECO:0000250}.
DISULFID 358 366 {ECO:0000250}.
DISULFID 390 395 {ECO:0000250}.
DISULFID 397 420 {ECO:0000250}.
SEQUENCE 555 AA; 60786 MW; 6F0DF6E2C969B9F0 CRC64;
MQKSEILFLI YSSLLLSSSL CQIPVDKLSN VGVIINEGKL LKIAGSYESR YIVLSLVPSI
DLEDGCGTTQ IIQYKNLLNR LLIPLKDALD LQESLITITN DTTVTNDNPQ SRFFGAVIGT
IALGVATAAQ ITAGIALAEA REARKDIALI KDSIIKTHNS VELIQRGIGE QIIALKTLQD
FVNNEIRPAI GELRCETTAL KLGIKLTQHY SELATAFSSN LGTIGEKSLT LQALSSLYSA
NITEILSTIK KDKSDIYDII YTEQVKGTVI DVDLEKYMVT LLVKIPILSE IPGVLIYRAS
SISYNIEGEE WHVAIPNYII NKASSLGGAD VTNCIESRLA YICPRDPTQL IPDNQQKCIL
GDVSKCPVTK VINNLVPKFA FINGGVVANC IASTCTCGTN RIPVNQDRSR GVTFLTYTNC
GLIGINGIEL YANKRGRDTT WGNQIIKVGP AVSIRPVDIS LNLASATNFL EESKIELMKA
KAIISAVGGW HNTESTQIII IIIVCILIII ICGILYYLYR VRRLLVMINS THNSPVNTYT
LESRMRNPYI GNNSN


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