ID   Q84850_HRSV             Unreviewed;       574 AA.
AC   Q84850;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Fusion glycoprotein F0 {ECO:0000256|ARBA:ARBA00016586};
DE   Flags: Precursor;
OS   Human respiratory syncytial virus.
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus;
OC   Orthopneumovirus hominis.
OX   NCBI_TaxID=11250 {ECO:0000313|EMBL:CAA26143.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:CAA26143.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2987829; DOI=10.1093/nar/13.5.1559;
RA   Elango N., Satake M., Coligan J.E., Norrby E., Camargo E., Venkatesan S.;
RT   "Respiratory syncytial virus fusion glycoprotein: nucleotide sequence of
RT   mRNA, identification of cleavage activation site and amino acid sequence of
RT   N-terminus of F1 subunit.";
RL   Nucleic Acids Res. 13:1559-1574(1985).
RN   [2] {ECO:0007829|PDB:3RRR}
RP   X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 26-109, GLYCOSYLATION AT ASN-70,
RP   AND DISULFIDE BONDS.
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).
CC   -!- FUNCTION: Inactive precursor that is cleaved at two sites by a furin-
CC       like protease to give rise to the mature F1 and F2 fusion
CC       glycoproteins. {ECO:0000256|ARBA:ARBA00035608}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Host
CC       Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004152}; Single-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004152}. Host cell membrane
CC       {ECO:0000256|ARBA:ARBA00004178}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004178}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}. Virion membrane
CC       {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004563}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC       {ECO:0000256|ARBA:ARBA00008211}.
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DR   EMBL; X02221; CAA26143.1; -; mRNA.
DR   PIR; B28929; B28929.
DR   PDB; 3RRR; X-ray; 2.82 A; A/C/E/G/I/M=26-109.
DR   PDBsum; 3RRR; -.
DR   SMR; Q84850; -.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
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   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 {ECO:0007829|PDB:3RRR};
KW   Fusion of virus membrane with host cell membrane
KW   {ECO:0000256|ARBA:ARBA00022521};
KW   Fusion of virus membrane with host membrane
KW   {ECO:0000256|ARBA:ARBA00022521};
KW   Host Golgi apparatus {ECO:0000256|ARBA:ARBA00022812};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Syncytium formation induced by viral infection
KW   {ECO:0000256|ARBA:ARBA00023213}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Viral attachment to host entry receptor {ECO:0000256|ARBA:ARBA00022587};
KW   Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022521};
KW   Virion {ECO:0000256|ARBA:ARBA00022587};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00022521}.
FT   TRANSMEM        525..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   CARBOHYD        70
FT                   /note="N-acetyl-D-glucosamine"
FT                   /evidence="ECO:0007829|PDB:3RRR"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007829|PDB:3RRR"
FT   DISULFID        37
FT                   /note="Interchain (with C-439 in P03420)"
FT                   /evidence="ECO:0007829|PDB:3RRR"
FT   DISULFID        69
FT                   /note="Interchain (with C-212 in P03420)"
FT                   /evidence="ECO:0007829|PDB:3RRR"
SQ   SEQUENCE   574 AA;  63365 MW;  7777F459F0FBC7C4 CRC64;
     MELLILKANA ITTILTAVTF CFASGQNITE EFYQSTCSAV SKGYLSALRT GWYTSVITIE
     LSNIKENKCN GTDAKVKLIK QELDKYKNAV TELQLLMQST PATNNRARRE LPRFMNYTLN
     NAKKTNVTLS KKRKRRFLGF LLGVGSAIAS GVAVSKVLHL EGEVNKIKSA LLSTNKAVVS
     LSNGVSVLTS KVLDLKNYID KQLLPIVNKQ SCSISNIETV IEFQQKNNRL LEITREFSVN
     AGVTTPVSTY MLTNSELLSL INDMPITNDQ KKLMSNNVQI VRQQSYSIMS IIKEEVLAYV
     VQLPLYGVID TPCWKLHTSP LCTTNTKEGS NICLTRTDRG WFCDNAGSVS FFPQAETCKV
     QSNRVFCDTM NSLTLPSEVN LCNVDIFNPK YDCKIMTSKT DVSSSVITSL GAIVSCYGKT
     KCTASNKNRG IIKTFSNGCD YVSNKGVDTV SVGNTLYYVN KQEGKSLYVK GEPIINFYDP
     LVFPSDEFDA SISQVNEKIN QSLAFIRKSD ELLHNVNAGK STTNIMITTI IIVIIVILLS
     LIAVGLLLYC KARSTPVTLS KDQLSGINNI AFSN
//