FUS_NIPAV
ID FUS_NIPAV Reviewed; 546 AA.
AC Q9IH63; Q5K4D9; Q8QU00;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Fusion glycoprotein F0;
DE Short=Protein F;
DE Contains:
DE RecName: Full=Fusion glycoprotein F2;
DE Contains:
DE RecName: Full=Fusion glycoprotein F1;
DE Flags: Precursor;
GN Name=F;
OS Nipah virus.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Henipavirus.
OX NCBI_TaxID=121791;
OH NCBI_TaxID=58060; Cynopterus brachyotis (Lesser short-nosed fruit bat) (Pachysoma brachyotis).
OH NCBI_TaxID=58065; Eonycteris spelaea (Lesser dawn bat) (Macroglossus spelaeus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9405; Pteropus hypomelanus (Island flying fox) (Variable flying fox).
OH NCBI_TaxID=132908; Pteropus vampyrus (Large flying fox).
OH NCBI_TaxID=153297; Scotophilus kuhlii (Lesser asiatic yellow bat).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10860887; DOI=10.1006/viro.2000.0340;
RA Harcourt B.H., Tamin A., Rollin P.E., Ksiazek T.G., Anderson L.J.,
RA Bellini W.J., Rota P.A.;
RT "Molecular characterization of Nipah virus, a newly emergent
RT paramyxovirus.";
RL Virology 271:334-349(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10827955; DOI=10.1126/science.288.5470.1432;
RA Chua K.B., Bellini W.J., Rota P.A., Harcourt B.H., Tamin A., Lam S.K.,
RA Ksiazek T.G., Rollin P.E., Zaki S.R., Shieh W., Goldsmith C.S.,
RA Gubler D.J., Roehrig J.T., Eaton B., Gould A.R., Olson J., Field H.,
RA Daniels P., Ling A.E., Peters C.J., Anderson L.J., Mahy B.W.;
RT "Nipah virus: a recently emergent deadly paramyxovirus.";
RL Science 288:1432-1435(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate UMMC1, and Isolate UMMC2;
RX PubMed=11514724; DOI=10.1099/0022-1317-82-9-2151;
RA Chan Y.P., Chua K.B., Koh C.L., Lim M.E., Lam S.K.;
RT "Complete nucleotide sequences of Nipah virus isolates from Malaysia.";
RL J. Gen. Virol. 82:2151-2155(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Malaysian flying-fox;
RX PubMed=11880045; DOI=10.1016/s1286-4579(01)01522-2;
RA Chua K.B., Koh C.L., Hooi P.S., Wee K.F., Khong J.H., Chua B.H., Chan Y.P.,
RA Lim M.E., Lam S.K.;
RT "Isolation of Nipah virus from Malaysian island flying-foxes.";
RL Microbes Infect. 4:145-151(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate NV/MY/99/UM-0128, Isolate NV/MY/99/VRI-1413, and
RC Isolate NV/MY/99/VRI-2794;
RX PubMed=15663869; DOI=10.3201/eid1012.040452;
RA Abubakar S., Chang L.Y., Mohdali A.R., Sharifah S.H., Yusoff K., Zamrod Z.;
RT "Isolation and molecular identification of Nipah virus from pigs.";
RL Emerg. Infect. Dis. 10:2228-2230(2004).
RN [6]
RP FUNCTION.
RX PubMed=25275126; DOI=10.1128/jvi.01632-14;
RA Landowski M., Dabundo J., Liu Q., Nicola A.V., Aguilar H.C.;
RT "Nipah virion entry kinetics, composition, and conformational changes
RT determined by enzymatic virus-like particles and new flow virometry
RT tools.";
RL J. Virol. 88:14197-14206(2014).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26059400; DOI=10.1016/j.ejcb.2015.05.005;
RA Weis M., Maisner A.;
RT "Nipah virus fusion protein: Importance of the cytoplasmic tail for
RT endosomal trafficking and bioactivity.";
RL Eur. J. Cell Biol. 94:316-322(2015).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF TYR-525 AND LEU-528.
RX PubMed=28250132; DOI=10.1128/jvi.02150-16;
RA Johnston G.P., Contreras E.M., Dabundo J., Henderson B.A., Matz K.M.,
RA Ortega V., Ramirez A., Park A., Aguilar H.C.;
RT "Cytoplasmic Motifs in the Nipah Virus Fusion Protein Modulate Virus
RT Particle Assembly and Egress.";
RL J. Virol. 91:0-0(2017).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 137-178 AND 187-205.
RA Xu Y., Liu Y., Lou Z., Su N., Bai Z., Gao G.F., Rao Z.;
RT "Crystal structure of Nipah Virus fusion core.";
RL Submitted (AUG-2004) to the PDB data bank.
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 137-178 AND 188-205.
RA Liu J., Lu M.;
RT "Molecular Basis of the Inhibition of Henipa Viruses.";
RL Submitted (MAY-2010) to the PDB data bank.
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.37 ANGSTROMS) OF 1-488, GLYCOSYLATION AT ASN-99;
RP ASN-414 AND ASN-464, AND SUBUNIT.
RX PubMed=26646856; DOI=10.1371/journal.ppat.1005322;
RA Xu K., Chan Y.P., Bradel-Tretheway B., Akyol-Ataman Z., Zhu Y., Dutta S.,
RA Yan L., Feng Y., Wang L.F., Skiniotis G., Lee B., Zhou Z.H., Broder C.C.,
RA Aguilar H.C., Nikolov D.B.;
RT "Crystal structure of the pre-fusion nipah virus fusion glycoprotein
RT reveals a novel hexamer-of-trimers assembly.";
RL PLoS Pathog. 11:1005322-1005322(2015).
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 G at the virion surface. Upon G binding to its cellular receptor,
CC the hydrophobic fusion peptide is unmasked and interacts with the
CC 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 {ECO:0000269|PubMed:25275126, ECO:0000269|PubMed:26059400,
CC ECO:0000269|PubMed:28250132}.
CC -!- SUBUNIT: Homotrimer of disulfide-linked F1-F2.
CC {ECO:0000269|PubMed:26646856}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:26059400};
CC Single-pass type I membrane protein. Host cell membrane
CC {ECO:0000269|PubMed:26059400}; Single-pass membrane protein.
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; AF238466; AAF73956.1; -; mRNA.
DR EMBL; AF212302; AAK29087.1; -; Genomic_RNA.
DR EMBL; AY029767; AAK50544.1; -; Genomic_RNA.
DR EMBL; AY029768; AAK50553.1; -; Genomic_RNA.
DR EMBL; AF376747; AAM13405.1; -; Genomic_RNA.
DR EMBL; AJ564621; CAD92350.1; -; Genomic_RNA.
DR EMBL; AJ564622; CAD92356.1; -; Genomic_RNA.
DR EMBL; AJ564623; CAD92362.1; -; Genomic_RNA.
DR EMBL; AJ627196; CAF25496.1; -; Genomic_RNA.
DR RefSeq; NP_112026.1; NC_002728.1.
DR PDB; 1WP7; X-ray; 2.20 A; A/B/C=137-178, A/B/C=453-485.
DR PDB; 3N27; X-ray; 1.80 A; A/B/C=137-178.
DR PDB; 5EVM; X-ray; 3.37 A; A/B/C/D/E/F=1-488.
DR PDB; 6T3F; X-ray; 3.20 A; F=26-482.
DR PDB; 6TYS; EM; 3.50 A; A/B/E=1-495.
DR PDB; 7KI4; EM; 2.90 A; A/B/E=1-487.
DR PDBsum; 1WP7; -.
DR PDBsum; 3N27; -.
DR PDBsum; 5EVM; -.
DR PDBsum; 6T3F; -.
DR PDBsum; 6TYS; -.
DR PDBsum; 7KI4; -.
DR SMR; Q9IH63; -.
DR IntAct; Q9IH63; 18.
DR MINT; Q9IH63; -.
DR ABCD; Q9IH63; 2 sequenced antibodies.
DR GeneID; 920954; -.
DR KEGG; vg:920954; -.
DR EvolutionaryTrace; Q9IH63; -.
DR Proteomes; UP000002330; Genome.
DR Proteomes; UP000007527; Genome.
DR Proteomes; UP000008676; Genome.
DR Proteomes; UP000100567; Genome.
DR Proteomes; UP000110983; Genome.
DR Proteomes; UP000130871; Genome.
DR Proteomes; UP000170143; 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:0039663; P:membrane fusion involved in viral entry into host cell; IDA:CAFA.
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; Coiled coil; 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 membrane; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..546
FT /note="Fusion glycoprotein F0"
FT /id="PRO_0000236005"
FT CHAIN 27..109
FT /note="Fusion glycoprotein F2"
FT /id="PRO_0000236006"
FT CHAIN 110..546
FT /note="Fusion glycoprotein F1"
FT /id="PRO_0000236007"
FT TOPO_DOM 27..497
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 64
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0007744|PDB:5EVM"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0007744|PDB:5EVM"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0007744|PDB:5EVM"
FT DISULFID 71..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 VARIANT 250
FT /note="T -> I (in strain: Isolate NiV/MY/99/VRI-0626)"
FT VARIANT 348
FT /note="M -> T (in strain: Isolate Malaysian flying-fox)"
FT MUTAGEN 525
FT /note="Y->A: Significant decrease of virus particle
FT budding."
FT /evidence="ECO:0000269|PubMed:28250132"
FT MUTAGEN 528
FT /note="L->A: Significant decrease of virus particle
FT budding."
FT /evidence="ECO:0000269|PubMed:28250132"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:7KI4"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 38..60
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:7KI4"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6T3F"
FT HELIX 75..98
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:6TYS"
FT HELIX 140..174
FT /evidence="ECO:0007829|PDB:3N27"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 188..205
FT /evidence="ECO:0007829|PDB:3N27"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:6TYS"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:7KI4"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 275..298
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:7KI4"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:7KI4"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:6T3F"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:7KI4"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:7KI4"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:7KI4"
FT HELIX 453..480
FT /evidence="ECO:0007829|PDB:7KI4"
SQ SEQUENCE 546 AA; 60282 MW; 3C78F4D1127EFD0E CRC64;
MVVILDKRCY CNLLILILMI SECSVGILHY EKLSKIGLVK GVTRKYKIKS NPLTKDIVIK
MIPNVSNMSQ CTGSVMENYK TRLNGILTPI KGALEIYKNN THDLVGDVRL AGVIMAGVAI
GIATAAQITA GVALYEAMKN ADNINKLKSS IESTNEAVVK LQETAEKTVY VLTALQDYIN
TNLVPTIDKI SCKQTELSLD LALSKYLSDL LFVFGPNLQD PVSNSMTIQA ISQAFGGNYE
TLLRTLGYAT EDFDDLLESD SITGQIIYVD LSSYYIIVRV YFPILTEIQQ AYIQELLPVS
FNNDNSEWIS IVPNFILVRN TLISNIEIGF CLITKRSVIC NQDYATPMTN NMRECLTGST
EKCPRELVVS SHVPRFALSN GVLFANCISV TCQCQTTGRA ISQSGEQTLL MIDNTTCPTA
VLGNVIISLG KYLGSVNYNS EGIAIGPPVF TDKVDISSQI SSMNQSLQQS KDYIKEAQRL
LDTVNPSLIS MLSMIILYVL SIASLCIGLI TFISFIIVEK KRNTYSRLED RRVRPTSSGD
LYYIGT
