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VGP_EBOSB
ID   VGP_EBOSB               Reviewed;         676 AA.
AC   Q66814;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Envelope glycoprotein;
DE   AltName: Full=GP1,2;
DE            Short=GP;
DE   Contains:
DE     RecName: Full=GP1;
DE   Contains:
DE     RecName: Full=GP2;
DE   Contains:
DE     RecName: Full=Shed GP;
DE     AltName: Full=GP1,2-delta;
DE   Flags: Precursor;
GN   Name=GP;
OS   Sudan ebolavirus (strain Boniface-76) (SEBOV) (Sudan Ebola virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX   NCBI_TaxID=128948;
OH   NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RX   PubMed=8622982; DOI=10.1073/pnas.93.8.3602;
RA   Sanchez A., Trappier S.G., Mahy B.W.J., Peters C.J., Nichol S.T.;
RT   "The virion glycoproteins of Ebola viruses are encoded in two reading
RT   frames and are expressed through transcriptional editing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:3602-3607(1996).
RN   [2]
RP   INTERACTION WITH HUMAN CLEC10A.
RX   PubMed=14990712; DOI=10.1128/jvi.78.6.2943-2947.2004;
RA   Takada A., Fujioka K., Tsuiji M., Morikawa A., Higashi N., Ebihara H.,
RA   Kobasa D., Feldmann H., Irimura T., Kawaoka Y.;
RT   "Human macrophage C-type lectin specific for galactose and N-
RT   acetylgalactosamine promotes filovirus entry.";
RL   J. Virol. 78:2943-2947(2004).
RN   [3]
RP   SIGNAL PEPTIDE (ENVELOPE GLYCOPROTEIN), AND GLYCOSYLATION (ENVELOPE
RP   GLYCOPROTEIN).
RX   PubMed=16775318; DOI=10.1128/jvi.02545-05;
RA   Marzi A., Akhavan A., Simmons G., Gramberg T., Hofmann H., Bates P.,
RA   Lingappa V.R., Poehlmann S.;
RT   "The signal peptide of the ebolavirus glycoprotein influences interaction
RT   with the cellular lectins DC-SIGN and DC-SIGNR.";
RL   J. Virol. 80:6305-6317(2006).
CC   -!- FUNCTION: [Envelope glycoprotein]: Trimeric GP1,2 complexes form the
CC       virion surface spikes and mediate the viral entry processes, with GP1
CC       acting as the receptor-binding subunit and GP2 as the membrane fusion
CC       subunit. At later times of infection, down-regulates the expression of
CC       various host cell surface molecules that are essential for immune
CC       surveillance and cell adhesion. Down-modulates several integrins
CC       including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1.
CC       This decrease in cell adhesion molecules may lead to cell detachment,
CC       contributing to the disruption of blood vessel integrity and
CC       hemorrhages developed during infection (cytotoxicity). Interacts with
CC       host TLR4 and thereby stimulates the differentiation and activation of
CC       monocytes leading to bystander death of T-lymphocytes. Down-regulates
CC       as well the function of host natural killer cells. Counteracts the
CC       antiviral effect of host BST2/tetherin that restricts release of
CC       progeny virions from infected cells. However, cooperates with VP40 and
CC       host BST2 to activate canonical NF-kappa-B pathway in a manner
CC       dependent on neddylation. {ECO:0000250|UniProtKB:Q05320}.
CC   -!- FUNCTION: [Shed GP]: Functions as a decoy for anti-GP1,2 antibodies
CC       thereby contributing to viral immune evasion. Interacts and activates
CC       host macrophages and dendritic cells inducing up-regulation of cytokine
CC       transcription. This effect is mediated throught activation of host
CC       TLR4. {ECO:0000250|UniProtKB:Q05320}.
CC   -!- FUNCTION: [GP1]: Responsible for binding to the receptor(s) on target
CC       cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as
CC       cofactors for virus entry into dendritic cells (DCs) and endothelial
CC       cells. Binding to the macrophage specific lectin CLEC10A also seem to
CC       enhance virus infectivity (PubMed:14990712). Interaction with
CC       FOLR1/folate receptor alpha may be a cofactor for virus entry in some
CC       cell types, although results are contradictory (By similarity). Members
CC       of the Tyro3 receptor tyrosine kinase family also seem to be cell entry
CC       factors in filovirus infection (By similarity). Once attached, the
CC       virions are internalized through clathrin-dependent endocytosis and/or
CC       macropinocytosis. After internalization of the virus into the endosomes
CC       of the host cell, proteolysis of GP1 by two cysteine proteases,
CC       CTSB/cathepsin B and CTSL/cathepsin L removes the glycan cap and allows
CC       GP1 binding to the host entry receptor NPC1. NPC1-binding, Ca(2+) and
CC       acidic pH induce a conformational change of GP2, which unmasks its
CC       fusion peptide and permit membranes fusion (By similarity).
CC       {ECO:0000250|UniProtKB:O11457, ECO:0000250|UniProtKB:Q05320,
CC       ECO:0000269|PubMed:14990712}.
CC   -!- FUNCTION: [GP2]: Acts as a class I viral fusion protein. Under the
CC       current model, the protein has at least 3 conformational states: pre-
CC       fusion native state, pre-hairpin intermediate state, and post-fusion
CC       hairpin state. During viral and target cell membrane fusion, the coiled
CC       coil regions (heptad repeats) assume a trimer-of-hairpins structure,
CC       positioning the fusion peptide in close proximity to the C-terminal
CC       region of the ectodomain. The formation of this structure appears to
CC       drive apposition and subsequent fusion of viral and target cell
CC       membranes. Responsible for penetration of the virus into the cell
CC       cytoplasm by mediating the fusion of the membrane of the endocytosed
CC       virus particle with the endosomal membrane. Low pH in endosomes induces
CC       an irreversible conformational change in GP2, releasing the fusion
CC       hydrophobic peptide. {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBUNIT: [Envelope glycoprotein]: Homotrimer; each monomer consists of
CC       a GP1 and a GP2 subunit linked by disulfide bonds. The resulting
CC       peplomers (GP1,2) protrude from the virus surface as spikes. Interacts
CC       with host integrin alpha-V/ITGAV. Interacts with host CLEC10A. Binds
CC       also to host CD209 and CLEC4M/DC-SIGN(R). Interacts with host FOLR1.
CC       Interacts with BST2; this interaction inhibits the antiviral effect of
CC       BST2 and this allows viral release from infected cells. Interacts with
CC       host FCN1; this interaction enhances viral entry. Interacts with host
CC       TLR4; this interaction induces T-lymphocyte death.
CC       {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBUNIT: [GP1]: Interacts with host entry receptor NPC1.
CC       {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBUNIT: [Shed GP]: GP1 and GP2delta are part of GP1,2delta soluble
CC       complexes released by ectodomain shedding.
CC       {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBCELLULAR LOCATION: [GP2]: Virion membrane
CC       {ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane protein
CC       {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:Q05320};
CC       Single-pass type I membrane protein {ECO:0000255}. Note=In the cell,
CC       localizes to the plasma membrane lipid rafts, which probably represent
CC       the assembly and budding site. {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBCELLULAR LOCATION: [GP1]: Virion membrane
CC       {ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q05320}. Host cell membrane
CC       {ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q05320}. Note=GP1 is not anchored to the viral
CC       envelope, but forms a disulfid-linked complex with the extravirion
CC       surface GP2. In the cell, both GP1 and GP2 localize to the plasma
CC       membrane lipid rafts, which probably represent the assembly and budding
CC       site. GP1 can also be shed after proteolytic processing.
CC       {ECO:0000250|UniProtKB:Q05320}.
CC   -!- SUBCELLULAR LOCATION: [Shed GP]: Secreted
CC       {ECO:0000250|UniProtKB:Q05320}. Note=GP2-delta bound to GP1 (GP1,2-
CC       delta) is produced by proteolytic cleavage of GP1,2 by host ADAM17 and
CC       shed by the virus. {ECO:0000250|UniProtKB:Q05320}.
CC   -!- DOMAIN: The mucin-like region seems to be involved in the cytotoxic
CC       function. This region is also involved in binding to human CLEC10A (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The coiled coil regions play a role in oligomerization and
CC       fusion activity. {ECO:0000250}.
CC   -!- PTM: [Envelope glycoprotein]: The signal peptide region modulates GP's
CC       high mannose glycosylation, thereby determining the efficiency of the
CC       interactions with DC-SIGN(R). {ECO:0000269|PubMed:16775318}.
CC   -!- PTM: [Envelope glycoprotein]: N-glycosylated.
CC       {ECO:0000305|PubMed:16775318}.
CC   -!- PTM: O-glycosylated in the mucin-like region. {ECO:0000250}.
CC   -!- PTM: Palmitoylation of GP2 is not required for its function.
CC       {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC       precursor is processed into GP1 and GP2 by host cell furin in the trans
CC       Golgi, and maybe by other host proteases, to yield the mature GP1 and
CC       GP2 proteins. The cleavage site corresponds to the furin optimal
CC       cleavage sequence [KR]-X-[KR]-R. This cleavage does not seem to be
CC       required for function. After the internalization of the virus into cell
CC       endosomes, GP1 C-terminus is removed by the endosomal proteases
CC       cathepsin B, cathepsin L, or both, leaving a 19-kDa N-terminal fragment
CC       which is further digested by cathepsin B. Proteolytic processing of
CC       GP1,2 by host ADAM17 can remove the transmembrane anchor of GP2 and
CC       leads to shedding of complexes consisting in GP1 and truncated GP2
CC       (GP1,2delta) (By similarity). {ECO:0000250}.
CC   -!- RNA EDITING: Modified_positions=295 {ECO:0000269|PubMed:8622982};
CC       Note=Partially edited. RNA editing at this position consists of an
CC       insertion of one adenine nucleotide. The sequence displayed here is the
CC       full-length transmembrane glycoprotein, derived from the edited RNA.
CC       The unedited RNA gives rise to the small secreted glycoprotein (AC
CC       P60172).;
CC   -!- MISCELLANEOUS: Filoviruses entry requires functional lipid rafts at the
CC       host cell surface. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Essential for infectivity, as it is the sole viral
CC       protein expressed at the virion surface.
CC   -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; U28134; AAB37096.1; -; Genomic_RNA.
DR   PDB; 3VE0; X-ray; 3.35 A; I=33-313, J=473-637.
DR   PDBsum; 3VE0; -.
DR   SMR; Q66814; -.
DR   ABCD; Q66814; 2 sequenced antibodies.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039587; P:suppression by virus of host tetherin activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR014625; GPC_FiloV.
DR   InterPro; IPR002561; GPC_filovir-type_extra_dom.
DR   Pfam; PF01611; Filo_glycop; 1.
DR   PIRSF; PIRSF036874; GPC_FiloV; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Clathrin-mediated endocytosis of virus by host;
KW   Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein;
KW   Host cell membrane; Host membrane; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host tetherin by virus; Lipoprotein; Membrane; Palmitate;
KW   RNA editing; Secreted; Signal; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral attachment to host entry receptor;
KW   Viral envelope protein; Viral immunoevasion;
KW   Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW   Virus entry into host cell.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..676
FT                   /note="Envelope glycoprotein"
FT                   /id="PRO_0000037476"
FT   CHAIN           33..501
FT                   /note="GP1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037477"
FT   CHAIN           502..676
FT                   /note="GP2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037478"
FT   CHAIN           502..637
FT                   /note="Shed GP"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000245063"
FT   TOPO_DOM        33..650
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        651..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        672..676
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          54..201
FT                   /note="Receptor-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          305..485
FT                   /note="Mucin-like region"
FT                   /evidence="ECO:0000250"
FT   REGION          313..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..539
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000250"
FT   COILED          554..595
FT                   /evidence="ECO:0000255"
FT   COILED          615..634
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        318..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            57
FT                   /note="Involved in receptor recognition and/or post-binding
FT                   events"
FT                   /evidence="ECO:0000255"
FT   SITE            63
FT                   /note="Involved in receptor recognition and/or post-binding
FT                   events"
FT                   /evidence="ECO:0000255"
FT   SITE            88
FT                   /note="Involved in receptor recognition and/or post-binding
FT                   events"
FT                   /evidence="ECO:0000255"
FT   SITE            170
FT                   /note="Involved in receptor recognition and/or post-binding
FT                   events"
FT                   /evidence="ECO:0000255"
FT   SITE            501..502
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250"
FT   SITE            637..638
FT                   /note="Cleavage; by host ADAM17"
FT                   /evidence="ECO:0000250"
FT   LIPID           670
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q05320"
FT   LIPID           672
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q05320"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        463
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        563
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        618
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..609
FT                   /note="Interchain (between GP1 and GP2 chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        108..135
FT                   /evidence="ECO:0000255"
FT   DISULFID        121..147
FT                   /evidence="ECO:0000255"
FT   DISULFID        511..556
FT                   /evidence="ECO:0000255"
FT   DISULFID        601..608
FT                   /evidence="ECO:0000250|UniProtKB:O11457"
FT   STRAND          34..39
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          45..49
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   HELIX           71..73
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   HELIX           79..83
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          86..91
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          96..98
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          100..103
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          105..114
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          135..143
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          163..169
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          176..189
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          216..221
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          223..226
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          236..239
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   HELIX           250..254
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   TURN            259..262
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          515..520
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          524..526
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          528..532
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   TURN            533..535
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   TURN            539..542
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          543..548
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   HELIX           552..575
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          579..581
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   HELIX           584..594
FT                   /evidence="ECO:0007829|PDB:3VE0"
FT   STRAND          606..608
FT                   /evidence="ECO:0007829|PDB:3VE0"
SQ   SEQUENCE   676 AA;  74987 MW;  700029BFD67F5E9A CRC64;
     MEGLSLLQLP RDKFRKSSFF VWVIILFQKA FSMPLGVVTN STLEVTEIDQ LVCKDHLAST
     DQLKSVGLNL EGSGVSTDIP SATKRWGFRS GVPPQVVSYE AGEWAENCYN LEIKKPDGSE
     CLPPPPDGVR GFPRCRYVHK AQGTGPCPGD YAFHKDGAFF LYDRLASTVI YRGVNFAEGV
     IAFLILAKPK ETFLQSPPIR EAANYTENTS SYYATSYLEY EIENFGAQHS TTLFKINNNT
     FVLLDRPHTP QFLFQLNDTI QLHQQLSNTT GKLIWTLDAN INADIGEWAF WENKKNLSEQ
     LRGEELSFET LSLNETEDDD ATSSRTTKGR ISDRATRKYS DLVPKDSPGM VSLHVPEGET
     TLPSQNSTEG RRVDVNTQET ITETTATIIG TNGNNMQIST IGTGLSSSQI LSSSPTMAPS
     PETQTSTTYT PKLPVMTTEE STTPPRNSPG STTEAPTLTT PENITTAVKT VWPQESTSNG
     LITSTVTGIL GSLGLRKRSR RQVNTRATGK CNPNLHYWTA QEQHNAAGIA WIPYFGPGAE
     GIYTEGLMHN QNALVCGLRQ LANETTQALQ LFLRATTELR TYTILNRKAI DFLLRRWGGT
     CRILGPDCCI EPHDWTKNIT DKINQIIHDF IDNPLPNQDN DDNWWTGWRQ WIPAGIGITG
     IIIAIIALLC VCKLLC
 
 
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