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Fusion glycoprotein F0 (Protein F) [Cleaved into: Fusion glycoprotein F2; Fusion glycoprotein F1]

 FUS_SENDZ               Reviewed;         565 AA.
P04855; P04854; P27564; Q6LC43; Q84202; Q84203; Q88251; Q88252;
Q88253; Q88254; Q88255; Q88256; Q88257; Q88258; Q88259; Q88260;
Q9YIY9; Q9YJP8; Q9YNH1; Q9YNH2; Q9YNH3; Q9YNH4; Q9YZ79;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 3.
25-OCT-2017, entry version 109.
RecName: Full=Fusion glycoprotein F0;
Short=Protein F;
Contains:
RecName: Full=Fusion glycoprotein F2;
Contains:
RecName: Full=Fusion glycoprotein F1;
Flags: Precursor;
Name=F;
Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Paramyxoviridae; Respirovirus.
NCBI_TaxID=11198;
NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
NCBI_TaxID=36483; Cricetidae sp. (Hamster).
NCBI_TaxID=10090; Mus musculus (Mouse).
NCBI_TaxID=10116; Rattus norvegicus (Rat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2998947; DOI=10.1016/0378-1119(85)90228-8;
Miura N., Ohtsuka E., Yamaberi N., Ikehara M., Uchida T., Okada Y.;
"Use of the deoxyinosine-containing probe to isolate and sequence cDNA
encoding the fusion (F) glycoprotein of Sendai virus (HVJ).";
Gene 38:271-274(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3005975; DOI=10.1093/nar/14.4.1545;
Shioda T., Iwasaki K., Shibuta H.;
"Determination of the complete nucleotide sequence of the Sendai virus
genome RNA and the predicted amino acid sequences of the F, HN and L
proteins.";
Nucleic Acids Res. 14:1545-1563(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Mutant F1-R, and Mutant ts-f1;
PubMed=2841801; DOI=10.1016/0042-6822(88)90601-0;
Tashiro M., Pritzer E., Khoshnan M.A., Yamakawa M., Kuroda K.,
Klenk H.-D., Rott R., Seto J.T.;
"Characterization of a pantropic variant of Sendai virus derived from
a host range mutant.";
Virology 165:577-583(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Mutant F1-R, and Mutant F1-R / T-5 revertant;
PubMed=1651590; DOI=10.1016/0042-6822(91)90839-4;
Tashiro M., James I., Karri S., Wahn K., Tobita K., Klenk H.-D.,
Rott R., Seto J.T.;
"Pneumotropic revertants derived from a pantropic mutant, F1-R, of
Sendai virus.";
Virology 184:227-234(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND CLEAVAGE BETWEEN F1 AND F2.
STRAIN=Mutant KD-11, Mutant KD-11M, Mutant KD-21, Mutant KD-22,
Mutant KD-22M, Mutant KD-31, Mutant KD-32, Mutant KD-32M,
Mutant KD-41, Mutant KD-51, Mutant KD-51M, Mutant KD-52,
Mutant KD-52M, Mutant KD-61, and Mutant KD-62;
PubMed=1312267; DOI=10.1016/0042-6822(92)90443-S;
Tashiro M., Seto J.T., Choosakul S., Yamakawa M., Klenk H.-D.,
Rott R.;
"Budding site of Sendai virus in polarized epithelial cells is one of
the determinants for tropism and pathogenicity in mice.";
Virology 187:413-422(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Mutant BF-132, Mutant BF-41, Mutant BF-53, Mutant BF-82,
Mutant BY-13, Mutant BY-4, Mutant BY-5, and Mutant BY-8;
PubMed=9930191; DOI=10.1007/s007050050465;
Okada H., Seto J.T., McQueen N.L., Klenk H.-D., Rott R., Tashiro M.;
"Determinants of pantropism of the F1-R mutant of Sendai virus:
specific mutations involved are in the F and M genes.";
Arch. Virol. 143:2343-2352(1998).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-320.
PubMed=6095182; DOI=10.1093/nar/12.21.7965;
Hidaka Y., Kanda T., Iwasaki K., Nomoto A., Shioda T., Shibuta H.;
"Nucleotide sequence of a Sendai virus genome region covering the
entire M gene and the 3' proximal 1013 nucleotides of the F gene.";
Nucleic Acids Res. 12:7965-7973(1984).
[8]
PROTEIN SEQUENCE OF 117-121 AND 283-287, AND DISULFIDE BONDS.
PubMed=8151783;
Iwata S., Schmidt A.C., Titani K., Suzuki M., Kido H., Gotoh B.,
Hamaguchi M., Nagai Y.;
"Assignment of disulfide bridges in the fusion glycoprotein of Sendai
virus.";
J. Virol. 68:3200-3206(1994).
[9]
GLYCOSYLATION AT ASN-104; ASN-245 AND ASN-449.
PubMed=6263875;
Yoshima H., Nakanishi M., Okada Y., Kobata A.;
"Carbohydrate structures of HVJ (Sendai virus) glycoproteins.";
J. Biol. Chem. 256:5355-5361(1981).
[10]
CLEAVAGE BY TRYPTASE CLARA.
PubMed=1331518;
Tashiro M., Yokogoshi Y., Tobita K., Seto J.T., Rott R., Kido H.;
"Tryptase Clara, an activating protease for Sendai virus in rat lungs,
is involved in pneumopathogenicity.";
J. Virol. 66:7211-7216(1992).
[11]
INTERACTION WITH HN PROTEIN.
PubMed=8709235;
Tanabayashi K., Compans R.W.;
"Functional interaction of paramyxovirus glycoproteins: identification
of a domain in Sendai virus HN which promotes cell fusion.";
J. Virol. 70:6112-6118(1996).
[12]
DOMAIN LEUCINE-ZIPPER.
PubMed=9398274; DOI=10.1021/bi971152i;
Ghosh J.K., Ovadia M., Shai Y.;
"A leucine zipper motif in the ectodomain of Sendai virus fusion
protein assembles in solution and in membranes and specifically binds
biologically-active peptides and the virus.";
Biochemistry 36:15451-15462(1997).
[13]
DISULFIDE BONDS, AND MUTAGENESIS OF CYS-70; CYS-199; CYS-338; CYS-347;
CYS-362; CYS-370; CYS-394; CYS-399; CYS-401 AND CYS-424.
PubMed=9603994; DOI=10.1093/oxfordjournals.jbchem.a022044;
Segawa H., Kato M., Yamashita T., Taira H.;
"The roles of individual cysteine residues of Sendai virus fusion
protein in intracellular transport.";
J. Biochem. 123:1064-1072(1998).
[14]
INTERACTION WITH CHAPERONES.
PubMed=10578061; DOI=10.1093/oxfordjournals.jbchem.a022554;
Tomita Y., Yamashita T., Sato H., Taira H.;
"Kinetics of interactions of sendai virus envelope glycoproteins, F
and HN, with endoplasmic reticulum-resident molecular chaperones, BiP,
calnexin, and calreticulin.";
J. Biochem. 126:1090-1100(1999).
[15]
GLYCOSYLATION AT ASN-104; ASN-245 AND ASN-449, AND MUTAGENESIS OF
ASN-104; ASN-245 AND ASN-449.
PubMed=10876159; DOI=10.1093/oxfordjournals.jbchem.a022731;
Segawa H., Yamashita T., Kawakita M., Taira H.;
"Functional analysis of the individual oligosaccharide chains of
sendai virus fusion protein.";
J. Biochem. 128:65-72(2000).
[16]
INTERACTION WITH M PROTEIN.
PubMed=11040121; DOI=10.1006/viro.2000.0556;
Ali A., Nayak D.P.;
"Assembly of Sendai virus: M protein interacts with F and HN proteins
and with the cytoplasmic tail and transmembrane domain of F protein.";
Virology 276:289-303(2000).
[17]
THREE-DIMENSIONAL RECONSTRUCTION (16 ANGSTROMS) OF 26-500 BY ELECTRON
CRYOMICROSCOPY.
PubMed=12881411; DOI=10.1093/emboj/cdg385;
Ludwig K., Baljinnyam B., Herrmann A., Boettcher C.;
"The 3D structure of the fusion primed Sendai F-protein determined by
electron cryomicroscopy.";
EMBO J. 22:3761-3771(2003).
-!- 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) interacts
with HN tetramer 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.
-!- SUBUNIT: Homotrimer of disulfide-linked F1-F2. Interacts with HN
and M proteins. {ECO:0000269|PubMed:10578061,
ECO:0000269|PubMed:11040121, ECO:0000269|PubMed:8151783,
ECO:0000269|PubMed:8709235, ECO:0000269|PubMed:9603994}.
-!- 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}.
Note=Folded in the endoplasmic reticulum by the human CANX and
HSPA5 chaperones.
-!- DOMAIN: The cytoplasmic region mediates the interaction with HN
and M proteins. {ECO:0000269|PubMed:9398274}.
-!- PTM: In natural infection, inactive F0 is matured into F1 and F2
outside the cell by one or more trypsin-like, arginine-specific
endoprotease secreted by the bronchial epithelial cells. One
identified protease that may be involved in this process is
tryptase Clara. Unlike most paramyxoviruses, Sendai F0 processing
occurs on the cell surface and induces a conformational change in
the protein that unmasks the fusion peptide. F0 maturation is a
primary determinant for organ tropism and pathogenicity. F1 and F2
display interchain and intrachain disulfide bonds, that are
necessary for correct folding and intracellular transport.
-!- PTM: N-glycosylated; glycans consist of a mixture of high mannose-
type oligosaccharides and of complex-type oligosaccharides.
Glycosylation at Asn-245 is essential for membrane localization
and F0 cleavage. {ECO:0000269|PubMed:10876159,
ECO:0000269|PubMed:6263875}.
-!- MISCELLANEOUS: Sendai virus or recombinant F protein are widely
used in cellular biology to fuse cells.
-!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein
family. {ECO:0000305}.
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EMBL; M12396; AAA47809.1; -; Genomic_RNA.
EMBL; X03614; CAA27275.1; -; Genomic_RNA.
EMBL; M30202; AAB06281.1; -; Genomic_RNA.
EMBL; M30203; AAB06287.1; -; Genomic_RNA.
EMBL; M30204; AAB06199.1; -; Genomic_RNA.
EMBL; M69046; AAB06293.1; -; Genomic_RNA.
EMBL; M55564; AAA47804.1; -; Genomic_RNA.
EMBL; U86411; AAC82291.1; -; Genomic_DNA.
EMBL; U86412; AAC82292.1; -; Genomic_DNA.
EMBL; U86413; AAC82293.1; -; Genomic_DNA.
EMBL; U86414; AAC82294.1; -; Genomic_DNA.
EMBL; U86415; AAC82295.1; -; Genomic_DNA.
EMBL; U86416; AAC82296.1; -; Genomic_DNA.
EMBL; U86417; AAC82297.1; -; Genomic_DNA.
EMBL; U86418; AAC82298.1; -; Genomic_DNA.
EMBL; U86419; AAC82299.1; -; Genomic_DNA.
EMBL; U86420; AAC82300.1; -; Genomic_DNA.
EMBL; U86421; AAC82301.1; -; Genomic_DNA.
EMBL; U86422; AAC82302.1; -; Genomic_DNA.
EMBL; U86423; AAC82303.1; -; Genomic_DNA.
EMBL; M76993; AAB06520.1; -; Genomic_RNA.
EMBL; M76994; AAB06512.1; -; Genomic_RNA.
EMBL; M76995; AAB06513.1; -; Genomic_RNA.
EMBL; M76996; AAB06514.1; -; Genomic_RNA.
EMBL; M76997; AAB06515.1; -; Genomic_RNA.
EMBL; M76998; AAB06516.1; -; Genomic_RNA.
EMBL; M76999; AAB06517.1; -; Genomic_RNA.
EMBL; M77000; AAB06518.1; -; Genomic_RNA.
EMBL; M77001; AAB06519.1; -; Genomic_RNA.
EMBL; M77002; AAB06830.1; -; Genomic_RNA.
EMBL; X00087; CAA24948.1; -; Genomic_RNA.
EMBL; AF001283; AAC82320.1; -; Genomic_RNA.
PIR; A04036; VGNZSV.
PIR; A24516; VGNZSH.
ProteinModelPortal; P04855; -.
SMR; P04855; -.
TCDB; 1.G.2.1.2; the viral pore-forming membrane fusion protein-2 (vmfp2) family.
iPTMnet; P04855; -.
UniCarbKB; P04855; -.
OrthoDB; VOG0900006Q; -.
SABIO-RK; P04855; -.
Proteomes; UP000006560; Genome.
Proteomes; UP000110830; Genome.
Proteomes; UP000163956; Genome.
Proteomes; UP000169749; Genome.
Proteomes; UP000181310; 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.
InterPro; IPR000776; Fusion_F0_Paramyxovir.
Pfam; PF00523; Fusion_gly; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Direct protein sequencing;
Disulfide bond; Fusion of virus membrane with host cell membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Membrane; Reference proteome;
Signal; Transmembrane; Transmembrane helix; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
SIGNAL 1 25
CHAIN 26 565 Fusion glycoprotein F0.
/FTId=PRO_0000039375.
CHAIN 26 116 Fusion glycoprotein F2.
/FTId=PRO_0000039376.
CHAIN 117 565 Fusion glycoprotein F1.
/FTId=PRO_0000039377.
TOPO_DOM 26 500 Extracellular.
TRANSMEM 501 521 Helical.
TOPO_DOM 522 565 Cytoplasmic.
REGION 117 141 Fusion peptide.
REGION 278 306 Leucine-zipper. {ECO:0000255}.
COILED 142 170 {ECO:0000255}.
COILED 466 491 {ECO:0000255}.
SITE 116 117 Cleavage; by arginine-specific
endoprotease.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000269|PubMed:10876159,
ECO:0000269|PubMed:6263875}.
CARBOHYD 245 245 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000269|PubMed:10876159,
ECO:0000269|PubMed:6263875}.
CARBOHYD 449 449 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000269|PubMed:10876159,
ECO:0000269|PubMed:6263875}.
DISULFID 70 199 Interchain (between F2 and F1 chains).
DISULFID 338 347
DISULFID 362 370
DISULFID 394 399 {ECO:0000250}.
DISULFID 401 424 {ECO:0000250}.
VARIANT 38 39 IV -> TA (in strain: Mutant KD-22 in
Mutant KD-22M).
VARIANT 47 47 I -> V (in Mutant KD-21 and Mutant KD-
52).
VARIANT 56 56 I -> L (in strain: Mutant KD-41).
VARIANT 63 63 G -> V (in strain: Mutant F1-R, Mutant
F1-R / T-5 revertant and Mutant ts-f1).
VARIANT 65 67 DFE -> HFD (in strain: Mutant KD-32).
VARIANT 67 67 E -> Q (in strain: Mutant KD-22M and
Mutant KD-32M).
VARIANT 79 79 K -> N (in strain: Mutant KD-62).
VARIANT 84 84 R -> M (in strain: Mutant BF-41, Mutant
BF-53, Mutant BF-82 and Mutant BF-132).
VARIANT 90 90 R -> S (in strain: Mutant KD-51 and
Mutant KD-51M).
VARIANT 91 91 D -> V (in strain: Mutant KD-51M).
VARIANT 104 104 N -> S (in strain: Mutant F1-R, Mutant
F1-R / T-5 revertant and Mutant ts-f1).
VARIANT 105 106 DT -> AP (in strain: Mutant KD-11 and
Mutant KD-11M).
VARIANT 109 109 N -> L (in strain: Mutant KD-31 and
Mutant KD-61).
VARIANT 115 116 SR -> AT (in strain: Mutant KD-52M).
VARIANT 115 116 SR -> PK (in strain: Mutant F1-R and
Mutant ts-f1).
VARIANT 116 116 R -> I (in strain: Mutant KD-21 and
Mutant KD-62).
VARIANT 116 116 R -> K (in strain: Mutant F1-R / T-5
revertant).
VARIANT 129 129 V -> A (in strain: Mutant KD-22M).
VARIANT 196 196 E -> D (in strain: Mutant KD-32 and KD-
32M).
VARIANT 200 200 E -> G (in strain: Mutant KD-32 and KD-
32M).
VARIANT 250 250 M -> I (in strain: Mutant BY-4 and Mutant
BY-13).
VARIANT 254 254 K -> R (in strain: wild-type, Mutant F1-
R, Mutant F1-R / T-5 revertant and Mutant
ts-f1).
VARIANT 279 279 E -> K (in strain: Mutant F1-R, Mutant
F1-R / T-5 revertant and Mutant ts-f1).
VARIANT 318 318 T -> H (in strain: Mutant BY-4, Mutant
BY-5 and Mutant BY-13).
VARIANT 319 319 V -> A.
VARIANT 387 387 N -> Y (in strain: Mutant KD-61).
VARIANT 395 395 I -> S (in strain: Mutant KD-61).
VARIANT 399 399 C -> F (in strain: Mutant KD-52M).
VARIANT 400 400 T -> P (in strain: Mutant KD-61).
VARIANT 423 423 N -> H (in strain: Mutant KD-52M).
VARIANT 456 456 I -> V (in strain: Mutant KD-51 and
Mutant KD-51M).
VARIANT 461 461 I -> V (in strain: wild-type, Mutant F1-
R, Mutant F1-R / T-5 revertant and Mutant
ts-f1).
VARIANT 480 480 E -> G (in strain: Mutant KD-22).
VARIANT 488 488 L -> I (in strain: Mutant KD-51 and
Mutant KD-51M).
VARIANT 555 555 N -> K (in strain: Mutant F1-R, Mutant
F1-R / T-5 revertant and Mutant ts-f1).
MUTAGEN 70 70 C->S: Inhibits transport of F and HN to
the cell surface.
{ECO:0000269|PubMed:9603994}.
MUTAGEN 104 104 N->G: Loss of glycosylation, enhances
cell fusion activity.
{ECO:0000269|PubMed:10876159}.
MUTAGEN 199 199 C->S: Inhibits transport of F and HN to
the cell surface.
{ECO:0000269|PubMed:9603994}.
MUTAGEN 245 245 N->G: Loss of glycosylation, cell surface
transport and F0 cleavage.
{ECO:0000269|PubMed:10876159}.
MUTAGEN 338 338 C->S: Inhibits transport of F and HN to
the cell surface.
{ECO:0000269|PubMed:9603994}.
MUTAGEN 347 347 C->S: Inhibits transport of F and HN to
the cell surface.
{ECO:0000269|PubMed:9603994}.
MUTAGEN 362 362 C->S: Inhibits transport of F and HN to
the cell surface.
{ECO:0000269|PubMed:9603994}.
MUTAGEN 370 370 C->S: Inhibits transport of F and HN to
the cell surface.
{ECO:0000269|PubMed:9603994}.
MUTAGEN 394 394 C->S: Inhibits transport of F and HN to
the cell surface.
{ECO:0000269|PubMed:9603994}.
MUTAGEN 399 399 C->S: Inhibits transport of F and HN to
the cell surface.
{ECO:0000269|PubMed:9603994}.
MUTAGEN 401 401 C->S: Inhibits transport of F and HN to
the cell surface.
{ECO:0000269|PubMed:9603994}.
MUTAGEN 424 424 C->S: Inhibits transport of F and HN to
the cell surface.
{ECO:0000269|PubMed:9603994}.
MUTAGEN 449 449 N->G: Loss of glycosylation.
{ECO:0000269|PubMed:10876159}.
CONFLICT 261 261 Y -> S (in Ref. 2). {ECO:0000305}.
SEQUENCE 565 AA; 61644 MW; 2EC5AA4DF96BC621 CRC64;
MTAYIQRSQC ISTSLLVVLT TLVSCQIPRD RLSNIGVIVD EGKSLKIAGS HESRYIVLSL
VPGVDFENGC GTAQVIQYKS LLNRLLIPLR DALDLQEALI TVTNDTTQNA GAPQSRFFGA
VIGTIALGVA TSAQITAGIA LAEAREAKRD IALIKESMTK THKSIELLQN AVGEQILALK
TLQDFVNDEI KPAISELGCE TAALRLGIKL TQHYSELLTA FGSNFGTIGE KSLTLQALSS
LYSANITEIM TTIKTGQSNI YDVIYTEQIK GTVIDVDLER YMVTLSVKIP ILSEVPGVLI
HKASSISYNI DGEEWYVTVP SHILSRASFL GGADITDCVE SRLTYICPRD PAQLIPDSQQ
KCILGDTTRC PVTKVVDSLI PKFAFVNGGV VANCIASTCT CGTGRRPISQ DRSKGVVFLT
HDNCGLIGVN GVELYANRRG HDATWGVQNL TVGPAIAIRP IDISLNLADA TNFLQDSKAE
LEKARKILSE VGRWYNSRET VITIIVVMVV ILVVIIVIII VLYRLRRSML MGNPDDRIPR
DTYTLEPKIR HMYTNGGFDA MAEKR


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EIAAB38219 CNSA1,EEN,EEN fusion partner of MLL,Endophilin-2,Endophilin-A2,Extra eleven-nineteen leukemia fusion gene protein,Homo sapiens,Human,SH3 domain protein 2B,SH3 domain-containing GRB2-like protein 1,SH3


 

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