FUS_HRSVA
ID FUS_HRSVA Reviewed; 574 AA.
AC P03420; P88811;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Fusion glycoprotein F0;
DE Contains:
DE RecName: Full=Fusion glycoprotein F2 {ECO:0000303|PubMed:23593008};
DE Short=F2;
DE Contains:
DE RecName: Full=p27 {ECO:0000303|PubMed:23593008};
DE AltName: Full=Intervening segment;
DE AltName: Full=Pep27;
DE AltName: Full=Peptide 27;
DE Contains:
DE RecName: Full=Fusion glycoprotein F1 {ECO:0000303|PubMed:23593008};
DE Short=F1;
DE Flags: Precursor;
GN Name=F;
OS Human respiratory syncytial virus A (strain A2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11259;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6096849; DOI=10.1073/pnas.81.24.7683;
RA Collins P.L., Huang Y.T., Wertz G.W.;
RT "Nucleotide sequence of the gene encoding the fusion (F) glycoprotein of
RT human respiratory syncytial virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:7683-7687(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=8918930; DOI=10.1006/viro.1996.0618;
RA Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R., Crowe J.E. Jr.;
RT "Nucleotide sequence analysis of the respiratory syncytial virus subgroup A
RT cold-passaged (cp) temperature sensitive (ts) cpts-248/404 live attenuated
RT virus vaccine candidate.";
RL Virology 225:419-422(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=9035372; DOI=10.1007/bf00366988;
RA Crowe J.E. Jr., Firestone C.Y., Whitehead S.S., Collins P.L., Murphy B.R.;
RT "Acquisition of the ts phenotype by a chemically mutagenized cold-passaged
RT human respiratory syncytial virus vaccine candidate results from the
RT acquisition of a single mutation in the polymerase (L) gene.";
RL Virus Genes 13:269-273(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=7747420; DOI=10.1006/viro.1995.1178;
RA Connors M., Crowe J.E. Jr., Firestone C.Y., Murphy B.R., Collins P.L.;
RT "A cold-passaged, attenuated strain of human respiratory syncytial virus
RT contains mutations in the F and L genes.";
RL Virology 208:478-484(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Cold-passage attenuated;
RX PubMed=9557743; DOI=10.1128/jvi.72.5.4467-4471.1998;
RA Whitehead S.S., Juhasz K., Firestone C.Y., Collins P.L., Murphy B.R.;
RT "Recombinant respiratory syncytial virus (RSV) bearing a set of mutations
RT from cold-passaged RSV is attenuated in chimpanzees.";
RL J. Virol. 72:4467-4471(1998).
RN [6]
RP PROTEIN SEQUENCE OF 110-117, PROTEOLYTIC CLEAVAGE (FUSION GLYCOPROTEIN F0),
RP AND MUTAGENESIS OF ARG-108; ARG-109 AND LYS-131.
RX PubMed=11493675; DOI=10.1073/pnas.151098198;
RA Gonzalez-Reyes L., Ruiz-Argueello M.B., Garcia-Barreno B., Calder L.,
RA Lopez J.A., Albar J.P., Skehel J.J., Wiley D.C., Melero J.A.;
RT "Cleavage of the human respiratory syncytial virus fusion protein at two
RT distinct sites is required for activation of membrane fusion.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9859-9864(2001).
RN [7]
RP PALMITOYLATION AT CYS-550.
RX PubMed=2732224; DOI=10.1016/s0021-9258(18)81623-4;
RA Arumugham R.G., Seid R.C. Jr., Doyle S., Hildreth S.W., Paradisio P.R.;
RT "Fatty acid acylation of the fusion glycoprotein of human respiratory
RT syncytial virus.";
RL J. Biol. Chem. 264:10339-10342(1989).
RN [8]
RP INTERACTION WITH HOST RHOA (FUSION GLYCOPROTEIN F1), INTERACTION WITH HOST
RP RHOA (FUSION GLYCOPROTEIN F2), FUNCTION (FUSION GLYCOPROTEIN F1), AND
RP FUNCTION (FUSION GLYCOPROTEIN F2).
RX PubMed=10438814; DOI=10.1128/jvi.73.9.7262-7270.1999;
RA Pastey M.K., Crowe J.E. Jr., Graham B.S.;
RT "RhoA interacts with the fusion glycoprotein of respiratory syncytial virus
RT and facilitates virus-induced syncytium formation.";
RL J. Virol. 73:7262-7270(1999).
RN [9]
RP INTERACTION WITH HOST HEPARAN SULFATE (FUSION GLYCOPROTEIN F1), INTERACTION
RP WITH HOST HEPARAN SULFATE (FUSION GLYCOPROTEIN F2), FUNCTION (FUSION
RP GLYCOPROTEIN F1), AND FUNCTION (FUSION GLYCOPROTEIN F2).
RX PubMed=10864656; DOI=10.1128/jvi.74.14.6442-6447.2000;
RA Feldman S.A., Audet S., Beeler J.A.;
RT "The fusion glycoprotein of human respiratory syncytial virus facilitates
RT virus attachment and infectivity via an interaction with cellular heparan
RT sulfate.";
RL J. Virol. 74:6442-6447(2000).
RN [10]
RP COILED COIL, DOMAIN (FUSION GLYCOPROTEIN F1), AND DOMAIN (FUSION
RP GLYCOPROTEIN F0).
RX PubMed=10846072; DOI=10.1128/jvi.74.13.5911-5920.2000;
RA Matthews J.M., Young T.F., Tucker S.P., Mackay J.P.;
RT "The core of the respiratory syncytial virus fusion protein is a trimeric
RT coiled coil.";
RL J. Virol. 74:5911-5920(2000).
RN [11]
RP PROTEOLYTIC CLEAVAGE (FUSION GLYCOPROTEIN F0).
RX PubMed=11369882; DOI=10.1099/0022-1317-82-6-1375;
RA Sugrue R.J., Brown C., Brown G., Aitken J., McL Rixon H.W.;
RT "Furin cleavage of the respiratory syncytial virus fusion protein is not a
RT requirement for its transport to the surface of virus-infected cells.";
RL J. Gen. Virol. 82:1375-1386(2001).
RN [12]
RP PROTEOLYTIC CLEAVAGE (FUSION GLYCOPROTEIN F0).
RX PubMed=11418598; DOI=10.1074/jbc.m102633200;
RA Zimmer G., Budz L., Herrler G.;
RT "Proteolytic activation of respiratory syncytial virus fusion protein.
RT Cleavage at two furin consensus sequences.";
RL J. Biol. Chem. 276:31642-31650(2001).
RN [13]
RP PROTEOLYTIC CLEAVAGE (FUSION GLYCOPROTEIN F0), AND MUTAGENESIS OF
RP 108-ARG-ARG-109.
RX PubMed=12127793; DOI=10.1006/viro.2002.1497;
RA Begona Ruiz-Argueello M., Gonzalez-Reyes L., Calder L.J., Palomo C.,
RA Martin D., Saiz M.J., Garcia-Barreno B., Skehel J.J., Melero J.A.;
RT "Effect of proteolytic processing at two distinct sites on shape and
RT aggregation of an anchorless fusion protein of human respiratory syncytial
RT virus and fate of the intervening segment.";
RL Virology 298:317-326(2002).
RN [14]
RP FUNCTION (FUSION GLYCOPROTEIN F2).
RX PubMed=12663767; DOI=10.1128/jvi.77.8.4609-4616.2003;
RA Schlender J., Zimmer G., Herrler G., Conzelmann K.K.;
RT "Respiratory syncytial virus (RSV) fusion protein subunit F2, not
RT attachment protein G, determines the specificity of RSV infection.";
RL J. Virol. 77:4609-4616(2003).
RN [15]
RP SUBCELLULAR LOCATION (FUSION GLYCOPROTEIN F0), SUBCELLULAR LOCATION (FUSION
RP GLYCOPROTEIN F1), AND TOPOLOGY.
RX PubMed=16160180; DOI=10.1128/jvi.79.19.12528-12535.2005;
RA Brock S.C., Heck J.M., McGraw P.A., Crowe J.E. Jr.;
RT "The transmembrane domain of the respiratory syncytial virus F protein is
RT an orientation-independent apical plasma membrane sorting sequence.";
RL J. Virol. 79:12528-12535(2005).
RN [16]
RP DISULFIDE BOND, MUTAGENESIS OF CYS-37; CYS-69; CYS-212; CYS-313; CYS-322;
RP CYS-333; CYS-343; CYS-358; CYS-367; CYS-382; CYS-393; CYS-416; CYS-422 AND
RP CYS-439, SUBUNIT (FUSION GLYCOPROTEIN F1), AND SUBUNIT (FUSION GLYCOPROTEIN
RP F2).
RX PubMed=16723026; DOI=10.1186/1743-422x-3-34;
RA Day N.D., Branigan P.J., Liu C., Gutshall L.L., Luo J., Melero J.A.,
RA Sarisky R.T., Del Vecchio A.M.;
RT "Contribution of cysteine residues in the extracellular domain of the F
RT protein of human respiratory syncytial virus to its function.";
RL Virol. J. 3:34-34(2006).
RN [17]
RP FUNCTION (FUSION GLYCOPROTEIN F1), AND FUNCTION (FUSION GLYCOPROTEIN F2).
RX PubMed=18216092; DOI=10.1128/jvi.01887-07;
RA Eckardt-Michel J., Lorek M., Baxmann D., Grunwald T., Keil G.M., Zimmer G.;
RT "The fusion protein of respiratory syncytial virus triggers p53-dependent
RT apoptosis.";
RL J. Virol. 82:3236-3249(2008).
RN [18]
RP IDENTIFICATION IN A COMPLEX WITH F1; F2 AND G GLYCOPROTEIN (FUSION
RP GLYCOPROTEIN F1), AND IDENTIFICATION IN A COMPLEX WITH F1; F2 AND G
RP GLYCOPROTEIN (FUSION GLYCOPROTEIN F2).
RX PubMed=18036342; DOI=10.1016/j.bbrc.2007.11.042;
RA Low K.W., Tan T., Ng K., Tan B.H., Sugrue R.J.;
RT "The RSV F and G glycoproteins interact to form a complex on the surface of
RT infected cells.";
RL Biochem. Biophys. Res. Commun. 366:308-313(2008).
RN [19]
RP INTERACTION WITH HOST NCL (FUSION GLYCOPROTEIN F1), AND FUNCTION (FUSION
RP GLYCOPROTEIN F1).
RX PubMed=21841784; DOI=10.1038/nm.2444;
RA Tayyari F., Marchant D., Moraes T.J., Duan W., Mastrangelo P., Hegele R.G.;
RT "Identification of nucleolin as a cellular receptor for human respiratory
RT syncytial virus.";
RL Nat. Med. 17:1132-1135(2011).
RN [20]
RP REVIEW.
RX PubMed=24362685; DOI=10.1007/978-3-642-38919-1_4;
RA McLellan J.S., Ray W.C., Peeples M.E.;
RT "Structure and function of respiratory syncytial virus surface
RT glycoproteins.";
RL Curr. Top. Microbiol. Immunol. 372:83-104(2013).
RN [21]
RP CRYOELECTRON MICROSCOPY, SUBCELLULAR LOCATION (FUSION GLYCOPROTEIN F1), AND
RP SUBCELLULAR LOCATION (FUSION GLYCOPROTEIN F2).
RX PubMed=23776214; DOI=10.1073/pnas.1309070110;
RA Liljeroos L., Krzyzaniak M.A., Helenius A., Butcher S.J.;
RT "Architecture of respiratory syncytial virus revealed by electron
RT cryotomography.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11133-11138(2013).
RN [22]
RP FUNCTION (FUSION GLYCOPROTEIN F0), PROTEOLYTIC CLEAVAGE (FUSION
RP GLYCOPROTEIN F0), AND FUNCTION (FUSION GLYCOPROTEIN F1).
RX PubMed=23593008; DOI=10.1371/journal.ppat.1003309;
RA Krzyzaniak M.A., Zumstein M.T., Gerez J.A., Picotti P., Helenius A.;
RT "Host cell entry of respiratory syncytial virus involves macropinocytosis
RT followed by proteolytic activation of the F protein.";
RL PLoS Pathog. 9:E1003309-E1003309(2013).
RN [23]
RP DOMAIN (FUSION GLYCOPROTEIN F0), AND COILED COIL (FUSION GLYCOPROTEIN F2).
RX PubMed=29212939; DOI=10.1128/jvi.01323-17;
RA Bermingham I.M., Chappell K.J., Watterson D., Young P.R.;
RT "The Heptad Repeat C Domain of the Respiratory Syncytial Virus Fusion
RT Protein Plays a Key Role in Membrane Fusion.";
RL J. Virol. 92:0-0(2018).
RN [24]
RP REVIEW.
RX PubMed=30723301; DOI=10.1038/s41579-019-0149-x;
RA Battles M.B., McLellan J.S.;
RT "Respiratory syncytial virus entry and how to block it.";
RL Nat. Rev. Microbiol. 17:233-245(2019).
RN [25]
RP INTERACTION WITH HOST IGF1R (FUSION GLYCOPROTEIN F1), FUNCTION (FUSION
RP GLYCOPROTEIN F1), INTERACTION WITH HOST IGF1R (FUSION GLYCOPROTEIN F2), AND
RP FUNCTION (FUSION GLYCOPROTEIN F2).
RX PubMed=32494007; DOI=10.1038/s41586-020-2369-7;
RA Griffiths C.D., Bilawchuk L.M., McDonough J.E., Jamieson K.C., Elawar F.,
RA Cen Y., Duan W., Lin C., Song H., Casanova J.L., Ogg S., Jensen L.D.,
RA Thienpont B., Kumar A., Hobman T.C., Proud D., Moraes T.J., Marchant D.J.;
RT "IGF1R is an entry receptor for respiratory syncytial virus.";
RL Nature 583:615-619(2020).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 254-277.
RX PubMed=20098425; DOI=10.1038/nsmb.1723;
RA McLellan J.S., Chen M., Kim A., Yang Y., Graham B.S., Kwong P.D.;
RT "Structural basis of respiratory syncytial virus neutralization by
RT motavizumab.";
RL Nat. Struct. Mol. Biol. 17:248-250(2010).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 159-209 AND 482-520, COILED COIL
RP (FUSION GLYCOPROTEIN F1), AND FUNCTION (FUSION GLYCOPROTEIN F1).
RX PubMed=19966279; DOI=10.1073/pnas.0910108106;
RA Roymans D., De Bondt H.L., Arnoult E., Geluykens P., Gevers T.,
RA Van Ginderen M., Verheyen N., Kim H., Willebrords R., Bonfanti J.F.,
RA Bruinzeel W., Cummings M.D., van Vlijmen H., Andries K.;
RT "Binding of a potent small-molecule inhibitor of six-helix bundle formation
RT requires interactions with both heptad-repeats of the RSV fusion protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:308-313(2010).
RN [28] {ECO:0007744|PDB:3RRR, ECO:0007744|PDB:3RRT}
RP X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 26-109 OF 147-513, GLYCOSYLATION
RP AT ASN-500, DISULFIDE BOND, SUBUNIT (FUSION GLYCOPROTEIN F1), AND SUBUNIT
RP (FUSION GLYCOPROTEIN F2).
RX PubMed=21613394; DOI=10.1128/jvi.00555-11;
RA McLellan J.S., Yang Y., Graham B.S., Kwong P.D.;
RT "Structure of respiratory syncytial virus fusion glycoprotein in the
RT postfusion conformation reveals preservation of neutralizing epitopes.";
RL J. Virol. 85:7788-7796(2011).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-524, AND GLYCOSYLATION AT
RP ASN-27; ASN-70 AND ASN-500.
RX PubMed=21586636; DOI=10.1073/pnas.1106536108;
RA Swanson K.A., Settembre E.C., Shaw C.A., Dey A.K., Rappuoli R., Mandl C.W.,
RA Dormitzer P.R., Carfi A.;
RT "Structural basis for immunization with postfusion respiratory syncytial
RT virus fusion F glycoprotein (RSV F) to elicit high neutralizing antibody
RT titers.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9619-9624(2011).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 26-513, DOMAIN (FUSION
RP GLYCOPROTEIN F0), DOMAIN (FUSION GLYCOPROTEIN F1), SUBUNIT (FUSION
RP GLYCOPROTEIN F1), SUBUNIT (FUSION GLYCOPROTEIN F2), AND FUNCTION (FUSION
RP GLYCOPROTEIN F1).
RX PubMed=23618766; DOI=10.1126/science.1234914;
RA McLellan J.S., Chen M., Leung S., Graepel K.W., Du X., Yang Y., Zhou T.,
RA Baxa U., Yasuda E., Beaumont T., Kumar A., Modjarrad K., Zheng Z., Zhao M.,
RA Xia N., Kwong P.D., Graham B.S.;
RT "Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific
RT neutralizing antibody.";
RL Science 340:1113-1117(2013).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 26-107 AND 137-513, AND
RP GLYCOSYLATION AT ASN-500.
RX PubMed=24179220; DOI=10.1126/science.1243283;
RA McLellan J.S., Chen M., Joyce M.G., Sastry M., Stewart-Jones G.B., Yang Y.,
RA Zhang B., Chen L., Srivatsan S., Zheng A., Zhou T., Graepel K.W., Kumar A.,
RA Moin S., Boyington J.C., Chuang G.Y., Soto C., Baxa U., Bakker A.Q.,
RA Spits H., Beaumont T., Zheng Z., Xia N., Ko S.Y., Todd J.P., Rao S.,
RA Graham B.S., Kwong P.D.;
RT "Structure-based design of a fusion glycoprotein vaccine for respiratory
RT syncytial virus.";
RL Science 342:592-598(2013).
RN [32] {ECO:0007744|PDB:5C69, ECO:0007744|PDB:5C6B}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-513, SUBUNIT (FUSION
RP GLYCOPROTEIN F1), AND SUBUNIT (FUSION GLYCOPROTEIN F2).
RX PubMed=26333350; DOI=10.1038/ncomms9143;
RA Krarup A., Truan D., Furmanova-Hollenstein P., Bogaert L., Bouchier P.,
RA Bisschop I.J.M., Widjojoatmodjo M.N., Zahn R., Schuitemaker H.,
RA McLellan J.S., Langedijk J.P.M.;
RT "A highly stable prefusion RSV F vaccine derived from structural analysis
RT of the fusion mechanism.";
RL Nat. Commun. 6:8143-8143(2015).
RN [33] {ECO:0007744|PDB:5EA3, ECO:0007744|PDB:5EA4, ECO:0007744|PDB:5EA5, ECO:0007744|PDB:5EA6, ECO:0007744|PDB:5EA7, ECO:0007744|PDB:5EA8}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-513.
RX PubMed=26641933; DOI=10.1038/nchembio.1982;
RA Battles M.B., Langedijk J.P., Furmanova-Hollenstein P.,
RA Chaiwatpongsakorn S., Costello H.M., Kwanten L., Vranckx L., Vink P.,
RA Jaensch S., Jonckers T.H., Koul A., Arnoult E., Peeples M.E., Roymans D.,
RA McLellan J.S.;
RT "Molecular mechanism of respiratory syncytial virus fusion inhibitors.";
RL Nat. Chem. Biol. 12:87-93(2016).
RN [34] {ECO:0007744|PDB:5K6B, ECO:0007744|PDB:5K6C, ECO:0007744|PDB:5K6F, ECO:0007744|PDB:5K6G, ECO:0007744|PDB:5K6H, ECO:0007744|PDB:5K6I}
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 26-103 AND 145-509, AND
RP GLYCOSYLATION AT ASN-27 AND ASN-70.
RX PubMed=27478931; DOI=10.1038/nsmb.3267;
RA Joyce M.G., Zhang B., Ou L., Chen M., Chuang G.Y., Druz A., Kong W.P.,
RA Lai Y.T., Rundlet E.J., Tsybovsky Y., Yang Y., Georgiev I.S., Guttman M.,
RA Lees C.R., Pancera M., Sastry M., Soto C., Stewart-Jones G.B.E.,
RA Thomas P.V., Van Galen J.G., Baxa U., Lee K.K., Mascola J.R., Graham B.S.,
RA Kwong P.D.;
RT "Iterative structure-based improvement of a fusion-glycoprotein vaccine
RT against RSV.";
RL Nat. Struct. Mol. Biol. 23:811-820(2016).
RN [35] {ECO:0007744|PDB:5U68}
RP X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 1-513.
RX PubMed=28134915; DOI=10.1038/nmicrobiol.2016.272;
RA Wen X., Mousa J.J., Bates J.T., Lamb R.A., Crowe J.E. Jr., Jardetzky T.S.;
RT "Structural basis for antibody cross-neutralization of respiratory
RT syncytial virus and human metapneumovirus.";
RL Nat. Microbiol. 2:16272-16272(2017).
RN [36] {ECO:0007744|PDB:5TOJ, ECO:0007744|PDB:5TOK}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-516, AND GLYCOSYLATION AT
RP ASN-500.
RX PubMed=28194013; DOI=10.1038/ncomms14158;
RA Rossey I., Gilman M.S., Kabeche S.C., Sedeyn K., Wrapp D., Kanekiyo M.,
RA Chen M., Mas V., Spitaels J., Melero J.A., Graham B.S., Schepens B.,
RA McLellan J.S., Saelens X.;
RT "Potent single-domain antibodies that arrest respiratory syncytial virus
RT fusion protein in its prefusion state.";
RL Nat. Commun. 8:14158-14158(2017).
RN [37] {ECO:0007744|PDB:5KWW}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-513 IN COMPLEX WITH THE FUSION
RP INHIBITOR JNJ-53718678.
RX PubMed=28761099; DOI=10.1038/s41467-017-00170-x;
RA Roymans D., Alnajjar S.S., Battles M.B., Sitthicharoenchai P.,
RA Furmanova-Hollenstein P., Rigaux P., Berg J.V.D., Kwanten L.,
RA Ginderen M.V., Verheyen N., Vranckx L., Jaensch S., Arnoult E.,
RA Voorzaat R., Gallup J.M., Larios-Mora A., Crabbe M., Huntjens D.,
RA Raboisson P., Langedijk J.P., Ackermann M.R., McLellan J.S., Vendeville S.,
RA Koul A.;
RT "Therapeutic efficacy of a respiratory syncytial virus fusion inhibitor.";
RL Nat. Commun. 8:167-167(2017).
RN [38] {ECO:0007744|PDB:5W23}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 1-513.
RX PubMed=29187732; DOI=10.1038/s41467-017-01858-w;
RA Tian D., Battles M.B., Moin S.M., Chen M., Modjarrad K., Kumar A.,
RA Kanekiyo M., Graepel K.W., Taher N.M., Hotard A.L., Moore M.L., Zhao M.,
RA Zheng Z.Z., Xia N.S., McLellan J.S., Graham B.S.;
RT "Structural basis of respiratory syncytial virus subtype-dependent
RT neutralization by an antibody targeting the fusion glycoprotein.";
RL Nat. Commun. 8:1877-1877(2017).
RN [39] {ECO:0007744|PDB:5UDC}
RP X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 1-513 IN COMPLEX WITH MANNOSE,
RP AND GLYCOSYLATION AT ASN-70.
RX PubMed=28469033; DOI=10.1126/scitranslmed.aaj1928;
RA Zhu Q., McLellan J.S., Kallewaard N.L., Ulbrandt N.D., Palaszynski S.,
RA Zhang J., Moldt B., Khan A., Svabek C., McAuliffe J.M., Wrapp D.,
RA Patel N.K., Cook K.E., Richter B.W.M., Ryan P.C., Yuan A.Q., Suzich J.A.;
RT "A highly potent extended half-life antibody as a potential RSV vaccine
RT surrogate for all infants.";
RL Sci. Transl. Med. 9:0-0(2017).
RN [40] {ECO:0007744|PDB:6APB, ECO:0007744|PDB:6APD}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-513.
RX PubMed=29396163; DOI=10.1016/j.immuni.2018.01.005;
RA Goodwin E., Gilman M.S.A., Wrapp D., Chen M., Ngwuta J.O., Moin S.M.,
RA Bai P., Sivasubramanian A., Connor R.I., Wright P.F., Graham B.S.,
RA McLellan J.S., Walker L.M.;
RT "Infants Infected with Respiratory Syncytial Virus Generate Potent
RT Neutralizing Antibodies that Lack Somatic Hypermutation.";
RL Immunity 48:339-349.e5(2018).
RN [41] {ECO:0007744|PDB:6NTX}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 159-209, AND COILED COIL.
RX PubMed=31268705; DOI=10.1021/jacs.9b04615;
RA Outlaw V.K., Bottom-Tanzer S., Kreitler D.F., Gellman S.H., Porotto M.,
RA Moscona A.;
RT "Dual Inhibition of Human Parainfluenza Type 3 and Respiratory Syncytial
RT Virus Infectivity with a Single Agent.";
RL J. Am. Chem. Soc. 141:12648-12656(2019).
RN [42] {ECO:0007744|PDB:6OE4, ECO:0007744|PDB:6OE5}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-513.
RX PubMed=31068578; DOI=10.1038/s41467-019-09807-5;
RA Gilman M.S.A., Furmanova-Hollenstein P., Pascual G., van 't Wout A.B.,
RA Langedijk J.P.M., McLellan J.S.;
RT "Transient opening of trimeric prefusion RSV F proteins.";
RL Nat. Commun. 10:2105-2105(2019).
RN [43] {ECO:0007744|PDB:6OUS}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 26-109 AND 137-513.
RX PubMed=31515478; DOI=10.1038/s41467-019-12137-1;
RA Tang A., Chen Z., Cox K.S., Su H.P., Callahan C., Fridman A., Zhang L.,
RA Patel S.B., Cejas P.J., Swoyer R., Touch S., Citron M.P., Govindarajan D.,
RA Luo B., Eddins M., Reid J.C., Soisson S.M., Galli J., Wang D., Wen Z.,
RA Heidecker G.J., Casimiro D.R., DiStefano D.J., Vora K.A.;
RT "A potent broadly neutralizing human RSV antibody targets conserved site IV
RT of the fusion glycoprotein.";
RL Nat. Commun. 10:4153-4153(2019).
RN [44] {ECO:0007744|PDB:6CXC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 26-526.
RX PubMed=30730999; DOI=10.1371/journal.pone.0210749;
RA Xie Q., Wang Z., Ni F., Chen X., Ma J., Patel N., Lu H., Liu Y., Tian J.H.,
RA Flyer D., Massare M.J., Ellingsworth L., Glenn G., Smith G., Wang Q.;
RT "Structure basis of neutralization by a novel site II/IV antibody against
RT respiratory syncytial virus fusion protein.";
RL PLoS ONE 14:e0210749-e0210749(2019).
RN [45] {ECO:0007744|PDB:6DC3, ECO:0007744|PDB:6DC5}
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 1-513.
RX PubMed=31306469; DOI=10.1371/journal.ppat.1007944;
RA Jones H.G., Battles M.B., Lin C.C., Bianchi S., Corti D., McLellan J.S.;
RT "Alternative conformations of a major antigenic site on RSV F.";
RL PLoS Pathog. 15:e1007944-e1007944(2019).
CC -!- FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved
CC at two sites by a furin-like protease to give rise to the mature F1 and
CC F2 fusion glycoproteins. {ECO:0000269|PubMed:23593008}.
CC -!- FUNCTION: [Fusion glycoprotein F1]: Class I viral fusion protein
CC (PubMed:23618766). Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state (PubMed:23618766).
CC During viral and plasma cell membrane fusion, the coiled coil regions
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain
CC (PubMed:23618766, PubMed:19966279). The formation of this structure
CC appears to drive apposition and subsequent fusion of viral and cellular
CC membranes leading to delivery of the nucleocapsid into the cytoplasm
CC (PubMed:23593008, PubMed:23618766). This fusion is pH independent and
CC occurs at the plasma or endosomal membrane (Probable). The trimer of
CC F1-F2 (F protein) also facilitates the attachment to host cell by
CC binding to host heparan sulfate (PubMed:10864656). F protein is
CC involved in the entry into the host cell through the interaction with
CC host IGFR1 (PubMed:32494007). This interaction activates PRKCZ/PKCzeta
CC that recruits host NCL/nucleolin to the apical cell surface where it
CC can bind fusion glycoprotein F1 (PubMed:32494007, PubMed:21841784).
CC Later in infection, F protein expressed at the plasma membrane of
CC infected cells can mediate fusion with adjacent cells to form syncytia,
CC a cytopathic effect that could lead to tissue necrosis
CC (PubMed:10438814). F protein may trigger p53-dependent apoptosis
CC (PubMed:18216092). {ECO:0000269|PubMed:10438814,
CC ECO:0000269|PubMed:10864656, ECO:0000269|PubMed:18216092,
CC ECO:0000269|PubMed:19966279, ECO:0000269|PubMed:21841784,
CC ECO:0000269|PubMed:23593008, ECO:0000269|PubMed:23618766,
CC ECO:0000269|PubMed:32494007, ECO:0000305|PubMed:23593008,
CC ECO:0000305|PubMed:30723301}.
CC -!- FUNCTION: [Fusion glycoprotein F2]: Major determinant of the species
CC specificity of RSV infection (PubMed:12663767). The trimer of F1-F2 (F
CC protein) also facilitates the attachment to host cell by binding to
CC host heparan sulfate (PubMed:10864656). F protein is involved in the
CC entry into the host cell through the interaction with host IGFR1
CC (PubMed:32494007). This interaction activates PRKCZ/PKCzeta that
CC recruits host NCL/nucleolin to the apical cell surface where it can
CC bind fusion glycoprotein F1 (PubMed:32494007). Later in infection, F
CC protein expressed at the plasma membrane of infected cells can mediate
CC fusion with adjacent cells to form syncytia, a cytopathic effect that
CC could lead to tissue necrosis (PubMed:10438814). F protein seems to
CC trigger p53-dependent apoptosis (PubMed:18216092).
CC {ECO:0000269|PubMed:10438814, ECO:0000269|PubMed:10864656,
CC ECO:0000269|PubMed:12663767, ECO:0000269|PubMed:18216092,
CC ECO:0000269|PubMed:32494007}.
CC -!- SUBUNIT: [Fusion glycoprotein F1]: Homotrimer (PubMed:23618766,
CC PubMed:26333350). Heterodimer with fusion protein F2; disulfide-linked
CC (PubMed:16723026, PubMed:21613394). Interacts with host NCL; this
CC interaction plays a role in viral entry into the host cell
CC (PubMed:21841784). As a heterodimer with F2, interacts with host
CC heparan sulfate (PubMed:10864656). As a heterodimer with F2, interacts
CC with host IGFR1; this interaction activates PRKCZ/PKCzeta that recruits
CC NCL/nucleolin from the host nucleus to the plasma membrane
CC (PubMed:32494007). Part of a complex composed of F1, F2 and G
CC glycoproteins (PubMed:18036342). As a heterodimer with F2, interacts
CC with host RHOA; this interaction facilitates virus-induced syncytium
CC formation (PubMed:10438814). {ECO:0000269|PubMed:10438814,
CC ECO:0000269|PubMed:10864656, ECO:0000269|PubMed:16723026,
CC ECO:0000269|PubMed:18036342, ECO:0000269|PubMed:21613394,
CC ECO:0000269|PubMed:21841784, ECO:0000269|PubMed:23618766,
CC ECO:0000269|PubMed:26333350, ECO:0000269|PubMed:32494007}.
CC -!- SUBUNIT: [Fusion glycoprotein F2]: Homotrimer (PubMed:26333350,
CC PubMed:23618766). Heterodimer with fusion protein F1; disulfide-linked
CC (PubMed:26333350, PubMed:16723026, PubMed:21613394). As a heterodimer
CC with F1, interacts with host heparan sulfate (PubMed:10864656). As a
CC heterodimer with F1, interacts with host IGFR1; this interaction
CC activates PRKCZ/PKCzeta that recruits NCL/nucleolin from the host
CC nucleus to the plasma membrane (PubMed:32494007). Part of a complex
CC composed of F1, F2 and G glycoproteins (PubMed:18036342). As a
CC heterodimer with F1, interacts with host RHOA; this interaction
CC facilitates virus-induced syncytium formation (PubMed:10438814).
CC {ECO:0000269|PubMed:10438814, ECO:0000269|PubMed:10864656,
CC ECO:0000269|PubMed:16723026, ECO:0000269|PubMed:18036342,
CC ECO:0000269|PubMed:21613394, ECO:0000269|PubMed:23618766,
CC ECO:0000269|PubMed:26333350, ECO:0000269|PubMed:32494007}.
CC -!- INTERACTION:
CC P03420; P03420: F; NbExp=8; IntAct=EBI-10042897, EBI-10042897;
CC -!- SUBCELLULAR LOCATION: [Fusion glycoprotein F0]: Host Golgi apparatus
CC membrane {ECO:0000305|PubMed:16160180}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16160180}.
CC -!- SUBCELLULAR LOCATION: [Fusion glycoprotein F1]: Virion membrane
CC {ECO:0000269|PubMed:23776214}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16160180}. Host cell membrane
CC {ECO:0000269|PubMed:16160180}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16160180}. Note=Localized at the host apical
CC membrane. {ECO:0000269|PubMed:16160180}.
CC -!- SUBCELLULAR LOCATION: [Fusion glycoprotein F2]: Virion membrane
CC {ECO:0000269|PubMed:23776214}. Host cell membrane {ECO:0000305}.
CC Note=Localized at the host apical membrane. {ECO:0000305}.
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 by host furin (PubMed:23618766). The coiled coil (heptad
CC repeat) regions are probably involved in homotrimerization,
CC heterodimerization and in the formation of a fusion-active hairpin
CC structure (PubMed:10846072, PubMed:29212939).
CC {ECO:0000250|UniProtKB:P11209, ECO:0000269|PubMed:10846072,
CC ECO:0000269|PubMed:23618766, ECO:0000269|PubMed:29212939}.
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 by host furin (PubMed:23618766). The coiled coil (heptad
CC repeat) regions are probably involved in homotrimerization,
CC heterodimerization and in the formation of a fusion-active hairpin
CC structure (PubMed:10846072). {ECO:0000250|UniProtKB:P11209,
CC ECO:0000269|PubMed:10846072, ECO:0000269|PubMed:23618766}.
CC -!- PTM: [Fusion glycoprotein F0]: The F glycoprotein is synthesized as a
CC F0 inactive precursor that is heavily N-glycosylated and processed at
CC two sites by a host furin-like protease probably in the Golgi
CC (PubMed:11493675, PubMed:11369882, PubMed:23593008, PubMed:11418598).
CC The cleavage site between p27 and F1 may occur after endocytosis to
CC yield the mature F1 and F2 proteins (Probable). Both cleavages are
CC required for membrane fusion and p27 is released from the processed
CC protein (PubMed:11493675, PubMed:23593008, PubMed:12127793).
CC {ECO:0000269|PubMed:11369882, ECO:0000269|PubMed:11418598,
CC ECO:0000269|PubMed:11493675, ECO:0000269|PubMed:12127793,
CC ECO:0000269|PubMed:23593008, ECO:0000305|PubMed:23593008}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; M11486; AAB59858.1; -; Genomic_RNA.
DR EMBL; U50362; AAB86664.1; -; Genomic_RNA.
DR EMBL; U50363; AAB86676.1; -; Genomic_RNA.
DR EMBL; AF035006; AAC14902.1; -; Genomic_RNA.
DR EMBL; U63644; AAC55970.1; -; Genomic_RNA.
DR PIR; A04035; VGNZA2.
DR PIR; B28929; B28929.
DR PDB; 2MDP; NMR; -; A=1-85.
DR PDB; 3IXT; X-ray; 2.75 A; C/P=254-277.
DR PDB; 3KPE; X-ray; 1.47 A; A=159-209, B=482-520.
DR PDB; 3O41; X-ray; 1.95 A; C/P=423-436.
DR PDB; 3O45; X-ray; 2.87 A; C/P=423-438.
DR PDB; 3RKI; X-ray; 3.20 A; A/B/C=1-524.
DR PDB; 3RRR; X-ray; 2.82 A; A/C/E/G/I/M=26-109, B/D/F/H/L/N=147-513.
DR PDB; 3RRT; X-ray; 3.20 A; A/C/E=26-109, B/D/F=147-513.
DR PDB; 4CCF; X-ray; 2.65 A; A/B/C/D/E/F=1-574.
DR PDB; 4JHW; X-ray; 3.60 A; F=26-513.
DR PDB; 4MMQ; X-ray; 3.25 A; A=26-107, B=137-513.
DR PDB; 4MMR; X-ray; 3.10 A; A=26-107, B=137-513.
DR PDB; 4MMS; X-ray; 2.40 A; A/C/E=26-107, B/D/F=137-513.
DR PDB; 4MMT; X-ray; 3.05 A; A=26-107, B=137-513.
DR PDB; 4MMU; X-ray; 3.00 A; A=26-107, B=137-513.
DR PDB; 4MMV; X-ray; 2.81 A; A=26-107, B=137-513.
DR PDB; 4ZYP; X-ray; 5.50 A; A/B/C=26-513.
DR PDB; 5C69; X-ray; 2.30 A; A=26-513.
DR PDB; 5C6B; X-ray; 2.40 A; F=26-108, F=113-513.
DR PDB; 5EA3; X-ray; 2.75 A; F=1-513.
DR PDB; 5EA4; X-ray; 2.30 A; F=1-513.
DR PDB; 5EA5; X-ray; 3.05 A; F=1-513.
DR PDB; 5EA6; X-ray; 2.75 A; F=1-513.
DR PDB; 5EA7; X-ray; 2.85 A; F=1-513.
DR PDB; 5EA8; X-ray; 2.60 A; F=1-513.
DR PDB; 5J3D; X-ray; 4.08 A; E/G/J=26-98, F/I/K=147-513.
DR PDB; 5K6B; X-ray; 2.98 A; F=26-105, F=145-509.
DR PDB; 5K6C; X-ray; 3.58 A; F=26-103, F=145-509.
DR PDB; 5K6F; X-ray; 2.59 A; F=26-101, F=145-509.
DR PDB; 5K6G; X-ray; 2.90 A; F=26-96, F=145-509.
DR PDB; 5K6H; X-ray; 2.65 A; F=26-103, F=145-509.
DR PDB; 5K6I; X-ray; 2.92 A; F=26-101, F=145-509.
DR PDB; 5KWW; X-ray; 2.50 A; F=1-513.
DR PDB; 5TOJ; X-ray; 3.30 A; A/B/C=1-513.
DR PDB; 5TOK; X-ray; 3.80 A; A/B/C=1-513.
DR PDB; 5TPN; X-ray; 3.14 A; A=27-108, A=113-513.
DR PDB; 5U68; X-ray; 3.08 A; A/B/C=1-513.
DR PDB; 5UDC; X-ray; 3.45 A; A/D/F=1-513.
DR PDB; 5W23; X-ray; 3.40 A; A/B/C=1-513.
DR PDB; 6APB; X-ray; 3.00 A; A/B/C=1-513.
DR PDB; 6APD; X-ray; 4.10 A; A/B/C=1-513.
DR PDB; 6CXC; EM; 3.90 A; A/B/C/D/E/F=26-526.
DR PDB; 6DC3; X-ray; 3.50 A; F=1-513.
DR PDB; 6DC5; X-ray; 3.50 A; A/D/G=1-513.
DR PDB; 6EAD; X-ray; 2.80 A; F=1-513.
DR PDB; 6EAE; X-ray; 2.90 A; F=1-513.
DR PDB; 6EAF; X-ray; 3.00 A; A/B/C=1-513.
DR PDB; 6EAG; X-ray; 3.30 A; F=1-513.
DR PDB; 6EAH; X-ray; 3.00 A; A/B/C=1-513.
DR PDB; 6EAI; X-ray; 2.80 A; A/B/C=1-513.
DR PDB; 6EAJ; X-ray; 2.85 A; F=1-513.
DR PDB; 6EAK; X-ray; 2.60 A; F=1-513.
DR PDB; 6EAL; X-ray; 2.75 A; F=1-513.
DR PDB; 6EAM; X-ray; 2.74 A; F=1-513.
DR PDB; 6EAN; X-ray; 2.90 A; F=1-513.
DR PDB; 6NTX; X-ray; 2.20 A; A/B=159-209.
DR PDB; 6OE4; X-ray; 3.30 A; A/D=1-513.
DR PDB; 6OE5; X-ray; 4.10 A; A=1-513.
DR PDB; 6OJ7; X-ray; 1.45 A; A=159-209.
DR PDB; 6OUS; X-ray; 3.40 A; A/C/E/G/I/K=26-109, B/D/F/H/J/L=137-513.
DR PDB; 6VKC; X-ray; 2.60 A; F=1-513.
DR PDB; 6VKD; X-ray; 2.50 A; F=1-513.
DR PDB; 6VKE; X-ray; 2.10 A; F=1-513.
DR PDB; 6W52; X-ray; 3.74 A; A=26-107.
DR PDB; 7LUE; EM; 2.90 A; A/B/C=26-513.
DR PDB; 7LVW; X-ray; 2.10 A; A/B/C/D/E/F=26-513.
DR PDB; 7MMN; X-ray; 3.57 A; A/C/J=26-97, B/I/K=137-516.
DR PDBsum; 2MDP; -.
DR PDBsum; 3IXT; -.
DR PDBsum; 3KPE; -.
DR PDBsum; 3O41; -.
DR PDBsum; 3O45; -.
DR PDBsum; 3RKI; -.
DR PDBsum; 3RRR; -.
DR PDBsum; 3RRT; -.
DR PDBsum; 4CCF; -.
DR PDBsum; 4JHW; -.
DR PDBsum; 4MMQ; -.
DR PDBsum; 4MMR; -.
DR PDBsum; 4MMS; -.
DR PDBsum; 4MMT; -.
DR PDBsum; 4MMU; -.
DR PDBsum; 4MMV; -.
DR PDBsum; 4ZYP; -.
DR PDBsum; 5C69; -.
DR PDBsum; 5C6B; -.
DR PDBsum; 5EA3; -.
DR PDBsum; 5EA4; -.
DR PDBsum; 5EA5; -.
DR PDBsum; 5EA6; -.
DR PDBsum; 5EA7; -.
DR PDBsum; 5EA8; -.
DR PDBsum; 5J3D; -.
DR PDBsum; 5K6B; -.
DR PDBsum; 5K6C; -.
DR PDBsum; 5K6F; -.
DR PDBsum; 5K6G; -.
DR PDBsum; 5K6H; -.
DR PDBsum; 5K6I; -.
DR PDBsum; 5KWW; -.
DR PDBsum; 5TOJ; -.
DR PDBsum; 5TOK; -.
DR PDBsum; 5TPN; -.
DR PDBsum; 5U68; -.
DR PDBsum; 5UDC; -.
DR PDBsum; 5W23; -.
DR PDBsum; 6APB; -.
DR PDBsum; 6APD; -.
DR PDBsum; 6CXC; -.
DR PDBsum; 6DC3; -.
DR PDBsum; 6DC5; -.
DR PDBsum; 6EAD; -.
DR PDBsum; 6EAE; -.
DR PDBsum; 6EAF; -.
DR PDBsum; 6EAG; -.
DR PDBsum; 6EAH; -.
DR PDBsum; 6EAI; -.
DR PDBsum; 6EAJ; -.
DR PDBsum; 6EAK; -.
DR PDBsum; 6EAL; -.
DR PDBsum; 6EAM; -.
DR PDBsum; 6EAN; -.
DR PDBsum; 6NTX; -.
DR PDBsum; 6OE4; -.
DR PDBsum; 6OE5; -.
DR PDBsum; 6OJ7; -.
DR PDBsum; 6OUS; -.
DR PDBsum; 6VKC; -.
DR PDBsum; 6VKD; -.
DR PDBsum; 6VKE; -.
DR PDBsum; 6W52; -.
DR PDBsum; 7LUE; -.
DR PDBsum; 7LVW; -.
DR PDBsum; 7MMN; -.
DR SMR; P03420; -.
DR DIP; DIP-48772N; -.
DR ELM; P03420; -.
DR IntAct; P03420; 2.
DR BindingDB; P03420; -.
DR ChEMBL; CHEMBL3856166; -.
DR DrugCentral; P03420; -.
DR TCDB; 1.G.2.1.3; the viral pore-forming membrane fusion protein-2 (vmfp2) family.
DR ABCD; P03420; 28 sequenced antibodies.
DR EvolutionaryTrace; P03420; -.
DR Proteomes; UP000007678; Genome.
DR Proteomes; UP000134464; Genome.
DR Proteomes; UP000181145; Genome.
DR Proteomes; UP000181262; Genome.
DR Proteomes; UP000181559; Genome.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0060141; P:positive regulation of syncytium formation by virus; 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 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Coiled coil;
KW Direct protein sequencing; 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;
KW Host-virus interaction; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Syncytium formation induced by viral infection;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral attachment to host entry receptor; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..574
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039234"
FT CHAIN 26..109
FT /note="Fusion glycoprotein F2"
FT /evidence="ECO:0000269|PubMed:21613394"
FT /id="PRO_0000039235"
FT PEPTIDE 110..136
FT /note="p27"
FT /evidence="ECO:0000269|PubMed:11493675"
FT /id="PRO_0000432664"
FT CHAIN 137..574
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039236"
FT TOPO_DOM 26..524
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:16160180"
FT TRANSMEM 525..550
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:16160180"
FT TOPO_DOM 551..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16160180"
FT REGION 137..157
FT /note="Fusion peptide"
FT /evidence="ECO:0000250|UniProtKB:P11209"
FT COILED 76..96
FT /evidence="ECO:0000269|PubMed:10846072,
FT ECO:0000269|PubMed:29212939"
FT COILED 158..209
FT /evidence="ECO:0000269|PubMed:19966279,
FT ECO:0000269|PubMed:31268705, ECO:0000305|PubMed:10846072"
FT COILED 481..516
FT /evidence="ECO:0000269|PubMed:19966279,
FT ECO:0000305|PubMed:10846072"
FT SITE 109..110
FT /note="Cleavage; by host furin-like protease"
FT /evidence="ECO:0000269|PubMed:11493675,
FT ECO:0000269|PubMed:12127793"
FT SITE 136..137
FT /note="Cleavage; by host furin-like protease"
FT /evidence="ECO:0000269|PubMed:11369882,
FT ECO:0000269|PubMed:12127793"
FT LIPID 550
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:2732224"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:21586636"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:21586636,
FT ECO:0000269|PubMed:28469033"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:21586636,
FT ECO:0000269|PubMed:24179220"
FT DISULFID 37..439
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000269|PubMed:21613394,
FT ECO:0000305|PubMed:16723026"
FT DISULFID 69..212
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000305|PubMed:16723026"
FT DISULFID 313..343
FT /evidence="ECO:0000269|PubMed:21613394"
FT DISULFID 322..333
FT /evidence="ECO:0000269|PubMed:21613394"
FT DISULFID 358..367
FT /evidence="ECO:0000269|PubMed:21613394"
FT DISULFID 382..393
FT /evidence="ECO:0000269|PubMed:21613394"
FT DISULFID 416..422
FT /evidence="ECO:0000305|PubMed:16723026,
FT ECO:0000305|PubMed:21613394"
FT VARIANT 102
FT /note="P -> A (in strain: Cold-passage attenuated)"
FT VARIANT 218
FT /note="E -> A (in strain: Cold-passage attenuated)"
FT VARIANT 379
FT /note="I -> V (in strain: Cold-passage attenuated)"
FT VARIANT 447
FT /note="M -> V (in strain: Cold-passage attenuated)"
FT VARIANT 523
FT /note="T -> I (in strain: Cold-passage attenuated)"
FT MUTAGEN 37
FT /note="C->S: Impairs translation or folding of the F
FT protein."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 69
FT /note="C->S: Impairs translation or folding of the F
FT protein."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 108..109
FT /note="RR->NN: Complete loss of cleavage between F2 and
FT p27."
FT /evidence="ECO:0000269|PubMed:11493675,
FT ECO:0000269|PubMed:12127793"
FT MUTAGEN 108
FT /note="R->N: Complete loss of cleavage between F2 and p27."
FT /evidence="ECO:0000269|PubMed:11493675"
FT MUTAGEN 109
FT /note="R->N: Complete loss of cleavage between F2 and p27."
FT /evidence="ECO:0000269|PubMed:11493675"
FT MUTAGEN 131
FT /note="K->Q: No effect on cleavage between F2 and p27."
FT /evidence="ECO:0000269|PubMed:11493675"
FT MUTAGEN 212
FT /note="C->S: No effect on F1 and F2 structure and
FT glycosylation."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 313
FT /note="C->S: Impairs translation or folding of the F
FT protein."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 322
FT /note="C->S: Impairs translation or folding of the F
FT protein."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 333
FT /note="C->S: Impairs translation or folding of the F
FT protein."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 343
FT /note="C->S: Impairs translation or folding of the F
FT protein."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 358
FT /note="C->S: Impairs translation or folding of the F
FT protein."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 367
FT /note="C->S: Impairs translation or folding of the F
FT protein."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 382
FT /note="C->S: No effect on F1 and F2 structure and
FT glycosylation."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 393
FT /note="C->S: Impairs translation or folding of the F
FT protein."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 416
FT /note="C->S: Impairs translation or folding of the F
FT protein."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 422
FT /note="C->S: No effect on F1 and F2 structure and
FT glycosylation."
FT /evidence="ECO:0000269|PubMed:16723026"
FT MUTAGEN 439
FT /note="C->S: Impairs translation or folding of the F
FT protein."
FT /evidence="ECO:0000269|PubMed:16723026"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:6VKE"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 38..49
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5UDC"
FT HELIX 74..96
FT /evidence="ECO:0007829|PDB:6VKE"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:5K6F"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:6VKE"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:5K6H"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:6VKE"
FT HELIX 160..203
FT /evidence="ECO:0007829|PDB:6OJ7"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3KPE"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:7LVW"
FT HELIX 217..238
FT /evidence="ECO:0007829|PDB:6VKE"
FT TURN 239..242
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:6VKE"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:6VKE"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:6VKE"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:6VKE"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 308..318
FT /evidence="ECO:0007829|PDB:6VKE"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:5K6F"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:6VKE"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6VKE"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:6VKE"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:3RKI"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 409..416
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:6VKE"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 437..446
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 449..452
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:6VKE"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:6VKE"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:6VKE"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:6VKE"
FT HELIX 487..514
FT /evidence="ECO:0007829|PDB:3KPE"
SQ SEQUENCE 574 AA; 63453 MW; A4066D9DC98933AA CRC64;
MELLILKANA ITTILTAVTF CFASGQNITE EFYQSTCSAV SKGYLSALRT GWYTSVITIE
LSNIKENKCN GTDAKVKLIK QELDKYKNAV TELQLLMQST PPTNNRARRE LPRFMNYTLN
NAKKTNVTLS KKRKRRFLGF LLGVGSAIAS GVAVSKVLHL EGEVNKIKSA LLSTNKAVVS
LSNGVSVLTS KVLDLKNYID KQLLPIVNKQ SCSISNIETV IEFQQKNNRL LEITREFSVN
AGVTTPVSTY MLTNSELLSL INDMPITNDQ KKLMSNNVQI VRQQSYSIMS IIKEEVLAYV
VQLPLYGVID TPCWKLHTSP LCTTNTKEGS NICLTRTDRG WYCDNAGSVS FFPQAETCKV
QSNRVFCDTM NSLTLPSEIN LCNVDIFNPK YDCKIMTSKT DVSSSVITSL GAIVSCYGKT
KCTASNKNRG IIKTFSNGCD YVSNKGMDTV SVGNTLYYVN KQEGKSLYVK GEPIINFYDP
LVFPSDEFDA SISQVNEKIN QSLAFIRKSD ELLHNVNAGK STTNIMITTI IIVIIVILLS
LIAVGLLLYC KARSTPVTLS KDQLSGINNI AFSN
