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

 VGP_EBOSU               Reviewed;         676 AA.
Q7T9D9;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
22-NOV-2017, entry version 75.
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;
Sudan ebolavirus (strain Human/Uganda/Gulu/2000) (SEBOV) (Sudan Ebola
virus).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Filoviridae; Ebolavirus.
NCBI_TaxID=386033;
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).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15367603; DOI=10.1128/JVI.78.19.10370-10377.2004;
Sanchez A., Lukwiya M., Bausch D., Mahanty S., Sanchez A.J.,
Wagoner K.D., Rollin P.E.;
"Analysis of human peripheral blood samples from fatal and nonfatal
cases of Ebola (Sudan) hemorrhagic fever: cellular responses, virus
load, and nitric oxide levels.";
J. Virol. 78:10370-10377(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=15047846; DOI=10.1128/JVI.78.8.4330-4341.2004;
Towner J.S., Rollin P.E., Bausch D.G., Sanchez A., Crary S.M.,
Vincent M., Lee W.F., Spiropoulou C.F., Ksiazek T.G., Lukwiya M.,
Kaducu F., Downing R., Nichol S.T.;
"Rapid diagnosis of Ebola hemorrhagic fever by reverse transcription-
PCR in an outbreak setting and assessment of patient viral load as a
predictor of outcome.";
J. Virol. 78:4330-4341(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=16139097; DOI=10.1016/j.virusres.2005.03.028;
Sanchez A., Rollin P.E.;
"Complete genome sequence of an Ebola virus (Sudan species)
responsible for a 2000 outbreak of human disease in Uganda.";
Virus Res. 113:16-25(2005).
-!- 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
seem to enhance virus infectivity. 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, allowing its binding to
the host entry receptor NPC1 and unmasking its fusion peptide to
initiate membranes fusion. {ECO:0000250|UniProtKB:Q05320}.
-!- 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. Down-
modulates integrins ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6,
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. {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: 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=295; 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 Q7T9E0), the +2A edited RNA gives rise to the
super small secreted glycoprotein ssGP (AC P0C772).;
-!- 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; AY316199; AAP88031.1; -; Genomic_RNA.
EMBL; AY344234; AAR11463.1; -; Genomic_RNA.
EMBL; AY729654; AAU43887.1; -; Genomic_RNA.
RefSeq; YP_138523.1; NC_006432.1.
PDB; 3S88; X-ray; 3.35 A; I=32-313, J=473-637.
PDBsum; 3S88; -.
ProteinModelPortal; Q7T9D9; -.
SMR; Q7T9D9; -.
DIP; DIP-59447N; -.
GeneID; 3160774; -.
KEGG; vg:3160774; -.
OrthoDB; VOG09000092; -.
Proteomes; UP000000277; 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.
1: Evidence at protein level;
3D-structure; 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; 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 32 {ECO:0000255}.
CHAIN 33 676 Envelope glycoprotein. {ECO:0000250}.
/FTId=PRO_0000316901.
CHAIN 33 501 GP1. {ECO:0000250}.
/FTId=PRO_0000316902.
CHAIN 502 676 GP2. {ECO:0000250}.
/FTId=PRO_0000316903.
CHAIN 502 637 GP2-delta. {ECO:0000250}.
/FTId=PRO_0000316904.
TOPO_DOM 33 650 Extracellular. {ECO:0000255}.
TRANSMEM 651 671 Helical. {ECO:0000255}.
TOPO_DOM 672 676 Cytoplasmic. {ECO:0000255}.
REGION 33 185 Receptor binding. {ECO:0000255}.
REGION 305 485 Mucin-like region. {ECO:0000250}.
REGION 524 539 Fusion peptide. {ECO:0000250}.
COILED 554 595 {ECO:0000255}.
COILED 615 634 {ECO:0000255}.
SITE 57 57 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 63 63 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 88 88 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 95 95 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 170 170 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 501 502 Cleavage; by host furin. {ECO:0000250}.
SITE 637 638 Cleavage; by host ADAM17. {ECO:0000250}.
LIPID 670 670 S-palmitoyl cysteine; by host.
{ECO:0000250|UniProtKB:Q05320}.
LIPID 672 672 S-palmitoyl cysteine; by host.
{ECO:0000250|UniProtKB:Q05320}.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 208 208 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 238 238 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 257 257 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 314 314 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 366 366 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 463 463 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 563 563 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 618 618 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 53 609 Interchain (between GP1 and GP2 chains).
{ECO:0000250}.
DISULFID 108 135 {ECO:0000255}.
DISULFID 121 147 {ECO:0000255}.
DISULFID 511 556 {ECO:0000255}.
DISULFID 601 608 {ECO:0000250|UniProtKB:O11457}.
STRAND 35 39 {ECO:0000244|PDB:3S88}.
STRAND 42 47 {ECO:0000244|PDB:3S88}.
HELIX 60 62 {ECO:0000244|PDB:3S88}.
STRAND 63 70 {ECO:0000244|PDB:3S88}.
HELIX 71 73 {ECO:0000244|PDB:3S88}.
HELIX 79 82 {ECO:0000244|PDB:3S88}.
TURN 83 85 {ECO:0000244|PDB:3S88}.
STRAND 86 91 {ECO:0000244|PDB:3S88}.
STRAND 96 98 {ECO:0000244|PDB:3S88}.
STRAND 100 103 {ECO:0000244|PDB:3S88}.
STRAND 105 111 {ECO:0000244|PDB:3S88}.
STRAND 120 122 {ECO:0000244|PDB:3S88}.
STRAND 135 141 {ECO:0000244|PDB:3S88}.
STRAND 149 154 {ECO:0000244|PDB:3S88}.
STRAND 159 161 {ECO:0000244|PDB:3S88}.
STRAND 163 169 {ECO:0000244|PDB:3S88}.
STRAND 176 186 {ECO:0000244|PDB:3S88}.
STRAND 216 219 {ECO:0000244|PDB:3S88}.
STRAND 225 229 {ECO:0000244|PDB:3S88}.
STRAND 233 237 {ECO:0000244|PDB:3S88}.
STRAND 240 243 {ECO:0000244|PDB:3S88}.
HELIX 250 262 {ECO:0000244|PDB:3S88}.
STRAND 515 519 {ECO:0000244|PDB:3S88}.
TURN 533 535 {ECO:0000244|PDB:3S88}.
HELIX 539 541 {ECO:0000244|PDB:3S88}.
STRAND 544 548 {ECO:0000244|PDB:3S88}.
HELIX 552 575 {ECO:0000244|PDB:3S88}.
STRAND 579 581 {ECO:0000244|PDB:3S88}.
HELIX 584 597 {ECO:0000244|PDB:3S88}.
SEQUENCE 676 AA; 74594 MW; 3852217579859E84 CRC64;
MGGLSLLQLP RDKFRKSSFF VWVIILFQKA FSMPLGVVTN STLEVTEIDQ LVCKDHLAST
DQLKSVGLNL EGSGVSTDIP SATKRWGFRS GVPPKVVSYE AGEWAENCYN LEIKKPDGSE
CLPPPPDGVR GFPRCRYVHK AQGTGPCPGD YAFHKDGAFF LYDRLASTVI YRGVNFAEGV
IAFLILAKPK ETFLQSPPIR EAVNYTENTS SYYATSYLEY EIENFGAQHS TTLFKIDNNT
FVRLDRPHTP QFLFQLNDTI HLHQQLSNTT GRLIWTLDAN INADIGEWAF WENKKNLSEQ
LRGEELSFEA LSLNETEDDD AASSRITKGR ISDRATRKYS DLVPKNSPGM VPLHIPEGET
TLPSQNSTEG RRVGVNTQET ITETAATIIG TNGNHMQIST IGIRPSSSQI PSSSPTTAPS
PEAQTPTTHT SGPSVMATEE PTTPPGSSPG PTTEAPTLTT PENITTAVKT VLPQESTSNG
LITSTVTGIL GSLGLRKRSR RQTNTKATGK CNPNLHYWTA QEQHNAAGIA WIPYFGPGAE
GIYTEGLMHN QNALVCGLRQ LANETTQALQ LFLRATTELR TYTILNRKAI DFLLRRWGGT
CRILGPDCCI EPHDWTKNIT DKINQIIHDF IDNPLPNQDN DDNWWTGWRQ WIPAGIGITG
IIIAIIALLC VCKLLC


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