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 27-MAR-2024, entry version 151. 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; OC Orthopneumovirus hominis. 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 IGF1R (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 IGF1R 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 IGF1R; 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 IGF1R; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7MPG; EM; 3.40 A; A/B/C=26-513. DR PDB; 8DG9; EM; 2.24 A; A/B/C=1-516. 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 PDBsum; 7MPG; -. DR PDBsum; 8DG9; -. DR EMDB; EMD-23521; -. DR EMDB; EMD-2392; -. DR EMDB; EMD-2393; -. DR EMDB; EMD-23933; -. DR SMR; P03420; -. DR DIP; DIP-48772N; -. DR ELM; P03420; -. DR IntAct; P03420; 2. DR BindingDB; P03420; -. DR ChEMBL; CHEMBL3856166; -. DR DrugBank; DB16258; Nirsevimab. DR DrugCentral; P03420; -. DR TCDB; 1.G.2.1.3; the viral pore-forming membrane fusion protein-2 (vmfp2) family. DR GlyCosmos; P03420; 6 sites, No reported glycans. DR iPTMnet; P03420; -. 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:0016020; C: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 Gene3D; 1.10.287.2480; -; 2. DR Gene3D; 6.10.250.1160; -; 1. DR Gene3D; 6.20.370.50; -; 1. DR InterPro; IPR000776; Fusion_F0_Paramyxovir. DR Pfam; PF00523; Fusion_gly; 1. DR SUPFAM; SSF58069; Virus ectodomain; 2. 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; Signal; KW Syncytium formation induced by viral infection; Transmembrane; KW 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 //