FUS_PI3H4
ID FUS_PI3H4 Reviewed; 539 AA.
AC P06828; Q86987;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Fusion glycoprotein F0;
DE Contains:
DE RecName: Full=Fusion glycoprotein F2;
DE Contains:
DE RecName: Full=Fusion glycoprotein F1;
DE Flags: Precursor;
GN Name=F;
OS Human parainfluenza 3 virus (strain Wash/47885/57) (HPIV-3) (Human
OS parainfluenza 3 virus (strain NIH 47885)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11217;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3012869; DOI=10.1016/0042-6822(86)90388-0;
RA Spriggs M.K., Olmsted R.A., Venkatesan S., Coligan J.E., Collins P.L.;
RT "Fusion glycoprotein of human parainfluenza virus type 3: nucleotide
RT sequence of the gene, direct identification of the cleavage-activation
RT site, and comparison with other paramyxoviruses.";
RL Virology 152:241-251(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3033123; DOI=10.1099/0022-1317-68-4-1003;
RA Cote M.J., Storey D.G., Kang C.Y., Dimock K.;
RT "Nucleotide sequence of the coding and flanking regions of the human
RT parainfluenza virus type 3 fusion glycoprotein gene.";
RL J. Gen. Virol. 68:1003-1010(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2825443; DOI=10.1016/0168-1702(87)90016-5;
RA Galinski M.S., Mink M.A., Pons M.W.;
RT "Molecular cloning and sequence analysis of the human parainfluenza 3 virus
RT genes encoding the surface glycoproteins, F and HN.";
RL Virus Res. 8:205-215(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1311137; DOI=10.1016/0168-1702(92)90089-r;
RA Prinoski K., Cote M.J., Kang C.Y., Dimock K.;
RT "Evolution of the fusion protein gene of human parainfluenza virus 3.";
RL Virus Res. 22:55-69(1992).
CC -!- FUNCTION: Class I viral fusion protein. Under the current model, the
CC protein has at least 3 conformational states: pre-fusion native state,
CC pre-hairpin intermediate state, and post-fusion hairpin state. During
CC viral and plasma cell membrane fusion, the heptad repeat (HR) regions
CC assume a trimer-of-hairpins structure, positioning the fusion peptide
CC in close proximity to the C-terminal region of the ectodomain. The
CC formation of this structure appears to drive apposition and subsequent
CC fusion of viral and plasma cell membranes. Directs fusion of viral and
CC cellular membranes leading to delivery of the nucleocapsid into the
CC cytoplasm. This fusion is pH independent and occurs directly at the
CC outer cell membrane. The trimer of F1-F2 (F protein) probably interacts
CC with HN at the virion surface. Upon HN binding to its cellular
CC receptor, the hydrophobic fusion peptide is unmasked and interacts with
CC the cellular membrane, inducing the fusion between cell and virion
CC membranes. Later in infection, F proteins expressed at the plasma
CC membrane of infected cells could mediate fusion with adjacent cells to
CC form syncytia, a cytopathic effect that could lead to tissue necrosis
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer of disulfide-linked F1-F2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- PTM: The inactive precursor F0 is glycosylated and proteolytically
CC cleaved into F1 and F2 to be functionally active. The cleavage is
CC mediated by cellular proteases during the transport and maturation of
CC the polypeptide (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; X05303; CAA28932.1; -; Genomic_RNA.
DR EMBL; D00016; BAA00012.1; -; mRNA.
DR EMBL; M21649; AAA46852.1; -; Genomic_RNA.
DR EMBL; S82195; AAB21447.1; -; Genomic_RNA.
DR PIR; A26764; VGNZH3.
DR PIR; A47610; A47610.
DR PDB; 1ZTM; X-ray; 3.05 A; A/B/C=19-493.
DR PDB; 6NRO; X-ray; 1.75 A; A/C/E=139-189, B/D/F=449-484.
DR PDB; 6NTX; X-ray; 2.20 A; C/D=449-484.
DR PDB; 6NYX; X-ray; 1.85 A; A/B/C/D/E/F/H/J/L=139-189, G/I/K/M/N/O/P/Q/T=449-484.
DR PDB; 6O40; X-ray; 1.20 A; A=139-189, B=449-484.
DR PDB; 6OJ7; X-ray; 1.45 A; C=449-484.
DR PDB; 6PRL; X-ray; 1.87 A; A/C/E=139-189, B/D/F=449-484.
DR PDB; 6PYQ; X-ray; 1.79 A; B/D/F=449-484.
DR PDB; 6PZ6; X-ray; 1.70 A; A/C/E=139-189, B/D/F=449-484.
DR PDB; 6V3V; X-ray; 2.17 A; A/C/E=139-189, B/D/F=449-484.
DR PDB; 6VAS; X-ray; 1.49 A; A/C=139-189, B/D=449-484.
DR PDB; 6VJO; X-ray; 2.00 A; A=449-484, B=139-189.
DR PDBsum; 1ZTM; -.
DR PDBsum; 6NRO; -.
DR PDBsum; 6NTX; -.
DR PDBsum; 6NYX; -.
DR PDBsum; 6O40; -.
DR PDBsum; 6OJ7; -.
DR PDBsum; 6PRL; -.
DR PDBsum; 6PYQ; -.
DR PDBsum; 6PZ6; -.
DR PDBsum; 6V3V; -.
DR PDBsum; 6VAS; -.
DR PDBsum; 6VJO; -.
DR SMR; P06828; -.
DR EvolutionaryTrace; P06828; -.
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:0019064; P:fusion of virus membrane with host plasma membrane; 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 Disulfide bond; Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Membrane; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..539
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039345"
FT CHAIN 19..109
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039346"
FT CHAIN 110..539
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039347"
FT TOPO_DOM 19..493
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 515..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 110..134
FT /note="Fusion peptide"
FT /evidence="ECO:0000250"
FT COILED 135..163
FT /evidence="ECO:0000255"
FT COILED 459..484
FT /evidence="ECO:0000255"
FT SITE 109..110
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 63..192
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250"
FT DISULFID 331..340
FT /evidence="ECO:0000250"
FT DISULFID 355..363
FT /evidence="ECO:0000250"
FT DISULFID 387..392
FT /evidence="ECO:0000250"
FT DISULFID 394..417
FT /evidence="ECO:0000250"
FT CONFLICT 35
FT /note="P -> S (in Ref. 1; BAA00012)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="T -> A (in Ref. 1; BAA00012)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="R -> K (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="V -> I (in Ref. 2; CAA28932)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="K -> T (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="A -> S (in Ref. 2; CAA28932)"
FT /evidence="ECO:0000305"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 36..54
FT /evidence="ECO:0007829|PDB:1ZTM"
FT HELIX 65..93
FT /evidence="ECO:0007829|PDB:1ZTM"
FT HELIX 141..181
FT /evidence="ECO:0007829|PDB:6O40"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:6O40"
FT TURN 215..219
FT /evidence="ECO:0007829|PDB:1ZTM"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:1ZTM"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:1ZTM"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1ZTM"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:1ZTM"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 275..287
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:1ZTM"
FT HELIX 350..357
FT /evidence="ECO:0007829|PDB:1ZTM"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:1ZTM"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:1ZTM"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:1ZTM"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:1ZTM"
FT HELIX 453..482
FT /evidence="ECO:0007829|PDB:6O40"
SQ SEQUENCE 539 AA; 60060 MW; E94F4BDB1E658BE5 CRC64;
MPTSILLIIT TMIMASFCQI DITKLQHVGV LVNSPKGMKI SQNFETRYLI LSLIPKIEDS
NSCGDQQIKQ YKRLLDRLII PLYDGLRLQK DVIVSNQESN ENTDPRTKRF FGGVIGTIAL
GVATSAQITA AVALVEAKQA RSDIEKLKEA IRDTNKAVQS VQSSIGNLIV AIKSVQDYVN
KEIVPSIARL GCEAAGLQLG IALTQHYSEL TNIFGDNIGS LQEKGIKLQG IASLYRTNIT
EIFTTSTVDK YDIYDLLFTE SIKVRVIDVD LNDYSITLQV RLPLLTRLLN TQIYRVDSIS
YNIQNREWYI PLPSHIMTKG AFLGGADVKE CIEAFSSYIC PSDPGFVLNH EMESCLSGNI
SQCPRTVVKS DIVPRYAFVN GGVVANCITT TCTCNGIGNR INQPPDQGVK IITHKECNTI
GINGMLFNTN KEGTLAFYTP NDITLNNSVA LDPIDISIEL NKAKSDLEES KEWIRRSNQK
LDSIGNWHQS STTIIIVLIM IIILFIINVT IIIIAVKYYR IQKRNRVDQN DKPYVLTNK
