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Envelope glycoprotein (GP1,2) (GP) [Cleaved into: GP1; GP2; GP2-delta]

 VGP_EBORR               Reviewed;         677 AA.
Q66799; Q5UAK8; Q8JPX8;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 109.
RecName: Full=Envelope glycoprotein;
AltName: Full=GP1,2;
Short=GP;
Contains:
RecName: Full=GP1;
Contains:
RecName: Full=GP2;
Contains:
RecName: Full=GP2-delta;
Flags: Precursor;
Name=GP;
Reston ebolavirus (strain Reston-89) (REBOV) (Reston Ebola virus).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Filoviridae; Ebolavirus.
NCBI_TaxID=386032;
NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
PubMed=8622982; DOI=10.1073/pnas.93.8.3602;
Sanchez A., Trappier S.G., Mahy B.W.J., Peters C.J., Nichol S.T.;
"The virion glycoproteins of Ebola viruses are encoded in two reading
frames and are expressed through transcriptional editing.";
Proc. Natl. Acad. Sci. U.S.A. 93:3602-3607(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Volchkov V.E.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=12191779; DOI=10.1016/S0168-1702(02)00087-4;
Groseth A., Stroeher U., Theriault S., Feldmann H.;
"Molecular characterization of an isolate from the 1989/90 epizootic
of Ebola virus Reston among macaques imported into the United
States.";
Virus Res. 87:155-163(2002).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate Pennsylvania-89;
PubMed=15661171; DOI=10.1016/j.virol.2004.11.018;
Boehmann Y., Enterlein S., Randolf A., Muehlberger E.I.;
"A reconstituted replication and transcription system for Ebola virus
Reston and comparison with Ebola virus Zaire.";
Virology 332:406-417(2005).
[5]
DOWN-MODULATION OF HOST MHC-I; ALPHA/BETA INTEGRINS AND EGFR.
PubMed=11836430; DOI=10.1128/jvi.76.5.2518-2528.2002;
Simmons G., Wool-Lewis R.J., Baribaud F., Netter R.C., Bates P.;
"Ebola virus glycoproteins induce global surface protein down-
modulation and loss of cell adherence.";
J. Virol. 76:2518-2528(2002).
-!- FUNCTION: GP1 is responsible for binding to the receptor(s) on
target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR
which act as cofactors for virus entry into the host cell. Binding
to CD209 and CLEC4M, which are respectively found on dendritic
cells (DCs), and on endothelial cells of liver sinusoids and lymph
node sinuses, facilitate infection of macrophages and endothelial
cells. These interactions not only facilitate virus cell entry,
but also allow capture of viral particles by DCs and subsequent
transmission to susceptible cells without DCs infection (trans
infection). Binding to the macrophage specific lectin CLEC10A also
seems to enhance virus infectivity, also this effect is much less
pronounced in Reston than in Zaire, Sudan or Cote d'Ivoire
strains. Interaction with FOLR1/folate receptor alpha may be a
cofactor for virus entry in some cell types, although results are
contradictory. Members of the Tyro3 receptor tyrosine kinase
family also seem to be cell entry factors in filovirus infection.
Once attached, the virions are internalized through clathrin-
dependent endocytosis and/or macropinocytosis. After
internalization of the virus into the endosomes of the host cell,
proteolysis of GP1 by two cysteine proteases, CTSB/cathepsin B and
CTSL/cathepsin L presumably induces a conformational change of
GP2, unmasking its fusion peptide and initiating membranes fusion
(By similarity). {ECO:0000250}.
-!- FUNCTION: GP2 acts as a class I viral fusion protein. Under the
current model, the protein has at least 3 conformational states:
pre-fusion native state, pre-hairpin intermediate state, and post-
fusion hairpin state. During viral and target cell membrane
fusion, the coiled coil regions (heptad repeats) assume a trimer-
of-hairpins structure, positioning the fusion peptide in close
proximity to the C-terminal region of the ectodomain. The
formation of this structure appears to drive apposition and
subsequent fusion of viral and target cell membranes. Responsible
for penetration of the virus into the cell cytoplasm by mediating
the fusion of the membrane of the endocytosed virus particle with
the endosomal membrane. Low pH in endosomes induces an
irreversible conformational change in GP2, releasing the fusion
hydrophobic peptide. {ECO:0000250|UniProtKB:Q05320}.
-!- FUNCTION: Envelope glycoprotein: GP1,2 which is the disulfid-
linked complex of GP1 and GP2, mediates endothelial cell
activation and decreases endothelial barrier function. Mediates
activation of primary macrophages. At terminal stages of the viral
infection, when its expression is high, GP1,2 down-modulates the
expression of various host cell surface molecules that are
essential for immune surveillance and cell adhesion. This
phenomenon is however much less pronounced in Reston than in
Zaire, Sudan or Cote d'Ivoire strains. Down-modulates integrins
ITGA1, ITGAV and ITGB1. GP1,2 alters the cellular recycling of the
dimer alpha-V/beta-3 via a dynamin-dependent pathway. Decrease in
the host cell surface expression of various adhesion molecules may
lead to cell detachment, contributing to the disruption of blood
vessel integrity and hemorrhages developed during Ebola virus
infection (cytotoxicity). This cytotoxicity appears late in the
infection, only after the massive release of viral particles by
infected cells. Down-modulation of host MHC-I, leading to altered
recognition by immune cells, may explain the immune suppression
and inflammatory dysfunction linked to Ebola infection. Also down-
modulates EGFR surface expression. Counteracts the antiviral
effect of host tetherin (By similarity).
{ECO:0000250|UniProtKB:Q05320}.
-!- FUNCTION: GP2delta is part of the complex GP1,2delta released by
host ADAM17 metalloprotease. This secreted complex may play a role
in the pathogenesis of the virus by efficiently blocking the
neutralizing antibodies that would otherwise neutralize the virus
surface glycoproteins GP1,2. Might therefore contribute to the
lack of inflammatory reaction seen during infection in spite the
of extensive necrosis and massive virus production. GP1,2delta
does not seem to be involved in activation of primary macrophages
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Homotrimer; each monomer consists of a GP1 and a GP2
subunit linked by disulfide bonds. The resulting peplomers (GP1,2)
protrude from the virus surface as spikes. GP1 and GP2delta are
part of GP1,2delta soluble complexes released by ectodomain
shedding. GP1,2 interacts with host integrin ITGAV/alpha-V and
CLEC10A. Also binds human CD209 and CLEC4M (collectively referred
to as DC-SIGN(R)), as well as human FOLR1. Interacts with host
entry receptor NPC1. {ECO:0000250|UniProtKB:Q05320}.
-!- SUBCELLULAR LOCATION: GP2: Virion membrane
{ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane
protein {ECO:0000255}. Host cell membrane
{ECO:0000250|UniProtKB:Q05320}; Single-pass type I membrane
protein {ECO:0000255}. Note=In the cell, localizes to the plasma
membrane lipid rafts, which probably represent the assembly and
budding site. {ECO:0000250|UniProtKB:Q05320}.
-!- SUBCELLULAR LOCATION: GP1: Virion membrane
{ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q05320}. Host cell membrane
{ECO:0000250|UniProtKB:Q05320}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q05320}. Note=GP1 is not anchored to the
viral envelope, but forms a disulfid-linked complex with the
extravirion surface GP2. In the cell, both GP1 and GP2 localize to
the plasma membrane lipid rafts, which probably represent the
assembly and budding site. GP1 can also be shed after proteolytic
processing. {ECO:0000250|UniProtKB:Q05320}.
-!- SUBCELLULAR LOCATION: GP2-delta: Secreted
{ECO:0000250|UniProtKB:Q05320}. Note=GP2-delta bound to GP1
(GP1,2-delta) is produced by proteolytic cleavage of GP1,2 by host
ADAM17 and shed by the virus. {ECO:0000250|UniProtKB:Q05320}.
-!- DOMAIN: The mucin-like region seems to be involved in the
cytotoxic function. This region is also involved in binding to
human CLEC10A (By similarity). {ECO:0000250}.
-!- DOMAIN: The coiled coil regions play a role in oligomerization and
fusion activity. {ECO:0000250}.
-!- PTM: The signal peptide region modulates GP's high mannose
glycosylation, thereby determining the efficiency of the
interactions with DC-SIGN(R). {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: O-glycosylated in the mucin-like region. {ECO:0000250}.
-!- PTM: Palmitoylation of GP2 is not required for its function.
{ECO:0000250}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
The precursor is processed into GP1 and GP2 by host cell furin in
the trans Golgi, and maybe by other host proteases, to yield the
mature GP1 and GP2 proteins. The cleavage site corresponds to the
furin optimal cleavage sequence [KR]-X-[KR]-R. This cleavage does
not seem to be required for function. After the internalization of
the virus into cell endosomes, GP1 C-terminus is removed by the
endosomal proteases cathepsin B, cathepsin L, or both, leaving a
19-kDa N-terminal fragment which is further digested by cathepsin
B. Proteolytic processing of GP1,2 by host ADAM17 can remove the
transmembrane anchor of GP2 and leads to shedding of complexes
consisting in GP1 and truncated GP2 (GP1,2delta) (By similarity).
{ECO:0000250}.
-!- RNA EDITING: Modified_positions=296 {ECO:0000269|PubMed:8622982};
Note=Partially edited. RNA editing at this position consists of an
insertion of one or two adenine nucleotides. The sequence
displayed here is the full-length transmembrane glycoprotein GP,
derived from the +1A edited RNA. The unedited RNA gives rise to
the small secreted glycoprotein sGP (AC Q66800), the +2A edited
RNA gives rise to the super small secreted glycoprotein ssGP (AC
P0C771).;
-!- MISCELLANEOUS: Filoviruses entry requires functional lipid rafts
at the host cell surface. {ECO:0000250}.
-!- MISCELLANEOUS: Essential for infectivity, as it is the sole viral
protein expressed at the virion surface.
-!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U23152; AAC54885.1; -; Genomic_RNA.
EMBL; AF034645; AAC24346.1; -; Genomic_RNA.
EMBL; AF522874; AAN04455.1; -; Genomic_RNA.
EMBL; AY769362; AAV48577.1; -; Genomic_RNA.
RefSeq; NP_690583.1; NC_004161.1.
ProteinModelPortal; Q66799; -.
SMR; Q66799; -.
GeneID; 955190; -.
KEGG; vg:955190; -.
OrthoDB; VOG09000092; -.
Proteomes; UP000007207; Genome.
Proteomes; UP000138664; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039587; P:suppression by virus of host tetherin activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR014625; GPC_FiloV.
InterPro; IPR002561; GPC_filovir-type_extra_dom.
Pfam; PF01611; Filo_glycop; 1.
PIRSF; PIRSF036874; GPC_FiloV; 1.
3: Inferred from homology;
Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Coiled coil; Complete proteome;
Disulfide bond; Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Host-virus interaction;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host tetherin by virus; Lipoprotein; Membrane;
Palmitate; Reference proteome; RNA editing; Secreted; Signal;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral attachment to host entry receptor; Viral envelope protein;
Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
SIGNAL 1 33 {ECO:0000255}.
CHAIN 34 677 Envelope glycoprotein.
/FTId=PRO_0000037470.
CHAIN 34 502 GP1. {ECO:0000250}.
/FTId=PRO_0000037471.
CHAIN 503 677 GP2. {ECO:0000250}.
/FTId=PRO_0000037472.
CHAIN 503 638 GP2-delta. {ECO:0000250}.
/FTId=PRO_0000245061.
TOPO_DOM 34 651 Extracellular. {ECO:0000255}.
TRANSMEM 652 672 Helical. {ECO:0000255}.
TOPO_DOM 673 677 Cytoplasmic. {ECO:0000255}.
REGION 55 202 Receptor-binding. {ECO:0000250}.
REGION 306 486 Mucin-like region. {ECO:0000250}.
REGION 525 540 Fusion peptide. {ECO:0000250}.
COILED 555 596 {ECO:0000255}.
COILED 616 635 {ECO:0000255}.
SITE 58 58 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 64 64 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 89 89 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 96 96 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 171 171 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 502 503 Cleavage; by host furin. {ECO:0000250}.
SITE 638 639 Cleavage; by host ADAM17. {ECO:0000250}.
LIPID 671 671 S-palmitoyl cysteine; by host.
{ECO:0000250|UniProtKB:Q05320}.
LIPID 673 673 S-palmitoyl cysteine; by host.
{ECO:0000250|UniProtKB:Q05320}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 339 339 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 420 420 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 435 435 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 463 463 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 564 564 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 619 619 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 54 610 Interchain (between GP1 and GP2 chains).
{ECO:0000250}.
DISULFID 109 136 {ECO:0000255}.
DISULFID 122 148 {ECO:0000255}.
DISULFID 512 557 {ECO:0000255}.
DISULFID 602 609 {ECO:0000250|UniProtKB:O11457}.
VARIANT 312 312 L -> P.
SEQUENCE 677 AA; 74433 MW; 3D22C37CF856F8BA CRC64;
MGSGYQLLQL PRERFRKTSF LVWVIILFQR AISMPLGIVT NSTLKATEID QLVCRDKLSS
TSQLKSVGLN LEGNGIATDV PSATKRWGFR SGVPPKVVSY EAGEWAENCY NLEIKKSDGS
ECLPLPPDGV RGFPRCRYVH KVQGTGPCPG DLAFHKNGAF FLYDRLASTV IYRGTTFAEG
VVAFLILSEP KKHFWKATPA HEPVNTTDDS TSYYMTLTLS YEMSNFGGNE SNTLFKVDNH
TYVQLDRPHT PQFLVQLNET LRRNNRLSNS TGRLTWTLDP KIEPDVGEWA FWETKKNFSQ
QLHGENLHFQ ILSTHTNNSS DQSPAGTVQG KISYHPPANN SELVPTDSPP VVSVLTAGRT
EEMSTQGLTN GETITGFTAN PMTTTIAPSP TMTSEVDNNV PSEQPNNTAS IEDSPPSASN
ETIYHSEMDP IQGSNNSAQS PQTKTTPAPT TSPMTQDPQE TANSSKPGTS PGSAAGPSQP
GLTINTVSKV ADSLSPTRKQ KRSVRQNTAN KCNPDLYYWT AVDEGAAVGL AWIPYFGPAA
EGIYIEGVMH NQNGLICGLR QLANETTQAL QLFLRATTEL RTYSLLNRKA IDFLLQRWGG
TCRILGPSCC IEPHDWTKNI TDEINQIKHD FIDNPLPDHG DDLNLWTGWR QWIPAGIGII
GVIIAIIALL CICKILC


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