FUS_HENDH
ID FUS_HENDH Reviewed; 546 AA.
AC O89342; Q66761;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 101.
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 Hendra virus (isolate Horse/Autralia/Hendra/1994).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Henipavirus.
OX NCBI_TaxID=928303;
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9402; Pteropus alecto (Black flying fox).
OH NCBI_TaxID=9403; Pteropus poliocephalus (Grey-headed flying fox).
OH NCBI_TaxID=94117; Pteropus scapulatus (Little red flying fox).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8822631; DOI=10.1016/0168-1702(96)01308-1;
RA Gould A.R.;
RT "Comparison of the deduced matrix and fusion protein sequences of equine
RT morbillivirus with cognate genes of the Paramyxoviridae.";
RL Virus Res. 43:17-31(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11024125; DOI=10.1128/jvi.74.21.9972-9979.2000;
RA Wang L.-F., Yu M., Hansson E., Pritchard L.I., Shiell B., Michalski W.P.,
RA Eaton B.T.;
RT "The exceptionally large genome of Hendra virus: support for creation of a
RT new genus within the family Paramyxoviridae.";
RL J. Virol. 74:9972-9979(2000).
RN [3]
RP FUNCTION.
RX PubMed=28468881; DOI=10.1128/jvi.00152-17;
RA Cifuentes-Munoz N., Sun W., Ray G., Schmitt P.T., Webb S., Gibson K.,
RA Dutch R.E., Schmitt A.P.;
RT "Mutations in the Transmembrane Domain and Cytoplasmic Tail of Hendra Virus
RT Fusion Protein Disrupt Virus-Like-Particle Assembly.";
RL J. Virol. 91:0-0(2017).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 137-178 AND 187-205.
RX PubMed=16972940; DOI=10.1111/j.1742-4658.2006.05459.x;
RA Lou Z., Xu Y., Xiang K., Su N., Qin L., Li X., Gao G.F., Bartlam M.,
RA Rao Z.;
RT "Crystal structures of Nipah and Hendra virus fusion core proteins.";
RL FEBS J. 273:4538-4547(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 26-495, AND GLYCOSYLATION AT
RP ASN-67; ASN-99; ASN-414 AND ASN-464.
RX PubMed=26712026; DOI=10.1073/pnas.1523303113;
RA Wong J.J., Paterson R.G., Lamb R.A., Jardetzky T.S.;
RT "Structure and stabilization of the Hendra virus F glycoprotein in its
RT prefusion form.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:1056-1061(2016).
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 (By similarity). {ECO:0000250|UniProtKB:Q9IH63,
CC ECO:0000269|PubMed:28468881}.
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; U49404; AAB39505.1; -; Genomic_RNA.
DR EMBL; AF017149; AAC83192.2; -; Genomic_RNA.
DR PIR; T08210; T08210.
DR RefSeq; NP_047111.2; NC_001906.3.
DR PDB; 1WP8; X-ray; 2.20 A; A/B/C=137-178, A/B/C=453-485.
DR PDB; 5EJB; X-ray; 3.20 A; A/B/C/D/E/F=26-482.
DR PDB; 6ILF; X-ray; 2.70 A; C=177-185.
DR PDB; 6J2F; X-ray; 1.90 A; C/F=177-185.
DR PDB; 7KI6; EM; 2.80 A; A/B/E=1-487.
DR PDBsum; 1WP8; -.
DR PDBsum; 5EJB; -.
DR PDBsum; 6ILF; -.
DR PDBsum; 6J2F; -.
DR PDBsum; 7KI6; -.
DR SMR; O89342; -.
DR PRIDE; O89342; -.
DR ABCD; O89342; 1 sequenced antibody.
DR GeneID; 1446467; -.
DR KEGG; vg:1446467; -.
DR EvolutionaryTrace; O89342; -.
DR Proteomes; UP000008771; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044228; C:host cell surface; IDA:CACAO.
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; 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_0000236002"
FT CHAIN 27..109
FT /note="Fusion glycoprotein F2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000236003"
FT CHAIN 110..546
FT /note="Fusion glycoprotein F1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000236004"
FT TOPO_DOM 27..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..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:0000305"
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:0007744|PDB:5EJB"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0007744|PDB:5EJB"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0007744|PDB:5EJB"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0007744|PDB:5EJB"
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 CONFLICT 208..213
FT /note="SDLLFV -> LICSC (in Ref. 1; AAB39505)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="A -> T (in Ref. 1; AAB39505)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="G -> R (in Ref. 1; AAB39505)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="G -> P (in Ref. 1; AAB39505)"
FT /evidence="ECO:0000305"
FT CONFLICT 437..452
FT /note="NYNSESIAVGPPVYTD -> KLQVLRALLLGHQSIQT (in Ref. 1;
FT AAB39505)"
FT /evidence="ECO:0000305"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 38..60
FT /evidence="ECO:0007829|PDB:5EJB"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 75..100
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 144..174
FT /evidence="ECO:0007829|PDB:1WP8"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:5EJB"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 190..205
FT /evidence="ECO:0007829|PDB:1WP8"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:5EJB"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:5EJB"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 275..298
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:5EJB"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:5EJB"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:5EJB"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:5EJB"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:5EJB"
FT TURN 436..440
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 453..469
FT /evidence="ECO:0007829|PDB:5EJB"
FT TURN 470..475
FT /evidence="ECO:0007829|PDB:5EJB"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:5EJB"
FT HELIX 483..490
FT /evidence="ECO:0007829|PDB:5EJB"
SQ SEQUENCE 546 AA; 59795 MW; ED80E2C158D6D0B6 CRC64;
MATQEVRLKC LLCGIIVLVL SLEGLGILHY EKLSKIGLVK GITRKYKIKS NPLTKDIVIK
MIPNVSNVSK CTGTVMENYK SRLTGILSPI KGAIELYNNN THDLVGDVKL AGVVMAGIAI
GIATAAQITA GVALYEAMKN ADNINKLKSS IESTNEAVVK LQETAEKTVY VLTALQDYIN
TNLVPTIDQI SCKQTELALD LALSKYLSDL LFVFGPNLQD PVSNSMTIQA ISQAFGGNYE
TLLRTLGYAT EDFDDLLESD SIAGQIVYVD LSSYYIIVRV YFPILTEIQQ AYVQELLPVS
FNNDNSEWIS IVPNFVLIRN TLISNIEVKY CLITKKSVIC NQDYATPMTA SVRECLTGST
DKCPRELVVS SHVPRFALSG GVLFANCISV TCQCQTTGRA ISQSGEQTLL MIDNTTCTTV
VLGNIIISLG KYLGSINYNS ESIAVGPPVY TDKVDISSQI SSMNQSLQQS KDYIKEAQKI
LDTVNPSLIS MLSMIILYVL SIAALCIGLI TFISFVIVEK KRGNYSRLDD RQVRPVSNGD
LYYIGT
