FUS_PIV5
ID FUS_PIV5 Reviewed; 529 AA.
AC P04849;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 146.
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 Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Mammalian orthorubulavirus 5.
OX NCBI_TaxID=11208;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6093114; DOI=10.1073/pnas.81.21.6706;
RA Paterson R.G., Harris T.J.R., Lamb R.A.;
RT "Fusion protein of the paramyxovirus simian virus 5: nucleotide sequence of
RT mRNA predicts a highly hydrophobic glycoprotein.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6706-6710(1984).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 122-185 AND 440-477.
RX PubMed=10198633; DOI=10.1016/s1097-2765(00)80458-x;
RA Baker K.A., Dutch R.E., Lamb R.A., Jardetzky T.S.;
RT "Structural basis for paramyxovirus-mediated membrane fusion.";
RL Mol. Cell 3:309-319(1999).
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.
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.
CC -!- SIMILARITY: Belongs to the paramyxoviruses fusion glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; K02253; AAA47881.1; -; Genomic_RNA.
DR EMBL; AF052755; AAC95515.1; -; Genomic_RNA.
DR PIR; A21688; VGNZSP.
DR PDB; 1SVF; X-ray; 1.40 A; A/C=122-185, B/D=440-477.
DR PDB; 2B9B; X-ray; 2.85 A; A/B/C=20-475.
DR PDB; 4GIP; X-ray; 2.00 A; A/B/C=20-100, D/E/F=103-477.
DR PDB; 4WSG; X-ray; 3.00 A; A/B/C=23-477.
DR PDBsum; 1SVF; -.
DR PDBsum; 2B9B; -.
DR PDBsum; 4GIP; -.
DR PDBsum; 4WSG; -.
DR SMR; P04849; -.
DR EvolutionaryTrace; P04849; -.
DR Proteomes; UP000007232; Genome.
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:0046761; P:viral budding from plasma membrane; IDA:UniProtKB.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..529
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000039378"
FT CHAIN 20..102
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000039379"
FT CHAIN 103..529
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000039380"
FT TOPO_DOM 20..487
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 509..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 103..127
FT /note="Fusion peptide"
FT COILED 128..156
FT /evidence="ECO:0000255"
FT COILED 452..477
FT /evidence="ECO:0000255"
FT SITE 102..103
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 64..185
FT /note="Interchain (between F2 and F1 chains)"
FT /evidence="ECO:0000250"
FT DISULFID 324..333
FT /evidence="ECO:0000250"
FT DISULFID 348..356
FT /evidence="ECO:0000250"
FT DISULFID 380..385
FT /evidence="ECO:0000250"
FT DISULFID 387..410
FT /evidence="ECO:0000250"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:4GIP"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 30..52
FT /evidence="ECO:0007829|PDB:4GIP"
FT HELIX 67..93
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:4GIP"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4GIP"
FT HELIX 123..174
FT /evidence="ECO:0007829|PDB:1SVF"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:1SVF"
FT HELIX 185..203
FT /evidence="ECO:0007829|PDB:4GIP"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:4GIP"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:4WSG"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:4GIP"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4GIP"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:4GIP"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:4GIP"
FT TURN 264..267
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 268..291
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:4GIP"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:4GIP"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:4GIP"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:4GIP"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:4GIP"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:4GIP"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:4GIP"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:4GIP"
FT HELIX 450..475
FT /evidence="ECO:0007829|PDB:1SVF"
SQ SEQUENCE 529 AA; 56597 MW; 3152C37B1AEA2C7E CRC64;
MGTIIQFLVV SCLLAGAGSL DPAALMQIGV IPTNVRQLMY YTEASSAFIV VKLMPTIDSP
ISGCNITSIS SYNATVTKLL QPIGENLETI RNQLIPTRRR RRFAGVVIGL AALGVATAAQ
VTAAVALVKA NENAAAILNL KNAIQKTNAA VADVVQATQS LGTAVQAVQD HINSVVSPAI
TAANCKAQDA IIGSILNLYL TELTTIFHNQ ITNPALSPIT IQALRILLGS TLPTVVEKSF
NTQISAAELL SSGLLTGQIV GLDLTYMQMV IKIELPTLTV QPATQIIDLA TISAFINNQE
VMAQLPTRVM VTGSLIQAYP ASQCTITPNT VYCRYNDAQV LSDDTMACLQ GNLTRCTFSP
VVGSFLTRFV LFDGIVYANC RSMLCKCMQP AAVILQPSSS PVTVIDMYKC VSLQLDNLRF
TITQLANVTY NSTIKLESSQ ILSIDPLDIS QNLAAVNKSL SDALQHLAQS DTYLSAITSA
TTTSVLSIIA ICLGSLGLIL IILLSVVVWK LLTIVVANRN RMENFVYHK
