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Q05320

- VGP_EBOZM

UniProt

Q05320 - VGP_EBOZM

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Protein

Envelope glycoprotein

Gene

GP

Organism
Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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, unmasking its fusion peptide and initiating membranes fusion.
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.
GP1,2 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.
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei57 – 571Involved in receptor recognition and/or post-binding eventsSequence Analysis
Sitei63 – 631Involved in receptor recognition and/or post-binding eventsSequence Analysis
Sitei64 – 641Involved in receptor recognition and/or post-binding eventsSequence Analysis
Sitei88 – 881Involved in receptor recognition and/or post-binding eventsSequence Analysis
Sitei95 – 951Involved in receptor recognition and/or post-binding eventsSequence Analysis
Sitei170 – 1701Involved in receptor recognition and/or post-binding eventsSequence Analysis
Sitei501 – 5022Cleavage; by host furin
Sitei637 – 6382Cleavage; by host ADAM17

GO - Biological processi

  1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  3. suppression by virus of host tetherin activity Source: UniProtKB-KW
  4. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
  5. viral budding from plasma membrane Source: CACAO
  6. viral entry into host cell Source: CACAO
  7. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with 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, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell

Protein family/group databases

TCDBi1.G.12.2.2. the avian leukosis virus gp95 fusion protein (alv-gp95) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein
Alternative name(s):
GP1,2
Short name:
GP
Cleaved into the following 3 chains:
Gene namesi
Name:GP
OrganismiZaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus)
Taxonomic identifieri128952 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesFiloviridaeEbolavirus
Virus hostiEpomops franqueti (Franquet's epauleted fruit bat) [TaxID: 77231]
Homo sapiens (Human) [TaxID: 9606]
Myonycteris torquata (Little collared fruit bat) [TaxID: 77243]
ProteomesiUP000007209: Genome

Subcellular locationi

Chain GP2 : Virion membrane; Single-pass type I membrane protein. Virion membrane; Lipid-anchor. Host cell membrane; Single-pass type I membrane protein. Host cell membrane; Lipid-anchor
Note: In the cell, localizes to the plasma membrane lipid rafts, which probably represent the assembly and budding site.
Chain GP1 : Virion membrane; Peripheral membrane protein. Host cell membrane; Peripheral membrane protein
Note: GP1 is not anchored to the viral envelope, but associates with the extravirion surface through its binding to 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.
Chain GP2-delta : Secreted
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 650618ExtracellularSequence AnalysisAdd
BLAST
Transmembranei651 – 67121HelicalSequence AnalysisAdd
BLAST
Topological domaini672 – 6765CytoplasmicSequence Analysis

GO - Cellular componenti

  1. cytoplasm Source: CACAO
  2. host cell endoplasmic reticulum Source: CACAO
  3. host cell plasma membrane Source: UniProtKB-KW
  4. integral component of membrane Source: UniProtKB-KW
  5. membrane raft Source: CACAO
  6. viral envelope Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Secreted, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401N → D: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi53 – 531C → G: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi55 – 551D → A: 80% loss of virus capability to enter into host cell.
Mutagenesisi55 – 551D → E or K: No effect on viral entry.
Mutagenesisi57 – 571L → A: Complete loss of virus capability to enter into host cell.
Mutagenesisi57 – 571L → F, I or K: 90% loss of virus capability to enter into host cell.
Mutagenesisi63 – 631L → A: 90% loss of virus capability to enter into host cell.
Mutagenesisi63 – 631L → F: Almost complete loss of virus capability to enter into host cell.
Mutagenesisi63 – 631L → K: Complete loss of virus capability to enter into host cell.
Mutagenesisi64 – 641R → A or E: Complete loss of virus capability to enter into host cell.
Mutagenesisi64 – 641R → K: No loss of virus capability to enter into host cell.
Mutagenesisi88 – 881F → A or E: Complete loss of virus capability to enter into host cell.
Mutagenesisi88 – 881F → I: No loss of virus capability to enter into host cell.
Mutagenesisi95 – 951K → A or E: 80% loss of virus capability to enter into host cell.
Mutagenesisi95 – 951K → R: 20% loss of virus capability to enter into host cell.
Mutagenesisi108 – 1081C → G: Almost complete loss of expression of GP1 and GP2. Almost complete loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi121 – 1211C → G: Reduced levels of expression of GP1 and GP2. 50% loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi135 – 1351C → S: Almost complete loss of expression of GP1 and GP2. Complete loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi147 – 1471C → S: Reduced levels of expression of GP1 and GP2. Almost complete loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi170 – 1701I → A: 90% loss of virus capability to enter into host cell.
Mutagenesisi170 – 1701I → E: Complete loss of virus capability to enter into host cell.
Mutagenesisi170 – 1701I → F: 50% loss of virus capability to enter into host cell.
Mutagenesisi204 – 2041N → D: No effect on GP1 and GP2 expression. No loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi238 – 2381N → Y: No effect on GP1 and GP2 expression. 12% loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi257 – 2571N → D: No effect on GP1 and GP2 expression. 12% loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi296 – 2961N → D: No effect on GP1 and GP2 expression. 18% loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi497 – 5015RRTRR → AGTAA: Almost complete loss of cleavage between GP1 and GP2. No loss of infectivity. 1 Publication
Mutagenesisi498 – 5014RTRR → ATAA: No effect on cleavage between GP1 and GP2. 1 Publication
Mutagenesisi511 – 5111C → G: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi528 – 5281G → R: Reduced infectivity. 1 Publication
Mutagenesisi529 – 5291L → A or R: Reduced infectivity. 1 Publication
Mutagenesisi532 – 5321I → A: Reduced infectivity. 1 Publication
Mutagenesisi532 – 5321I → R: Almost complete loss of infectivity. No effect on transport of GP to the cell surface and incorporation onto virions. 1 Publication
Mutagenesisi535 – 5351F → A: Reduced infectivity. 1 Publication
Mutagenesisi535 – 5351F → R: Almost complete loss of infectivity. No effect on transport of GP to the cell surface and incorporation onto virions. 1 Publication
Mutagenesisi536 – 5361G → A: Almost complete loss of infectivity. No effect on transport of GP to the cell surface and incorporation onto virions. 1 Publication
Mutagenesisi537 – 5371P → R: Almost complete loss of infectivity. No effect on transport of GP to the cell surface and incorporation onto virions. 1 Publication
Mutagenesisi556 – 5561C → S: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi563 – 5631N → D: Reduced levels of expression of GP, GP1 and GP2. 20% loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi601 – 6011C → S: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi608 – 6081C → G: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi609 – 6091C → G: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi618 – 6181N → D: Slightly reduced levels of expression of GP1 and GP2. No loss of virus capability to enter into host cell. 1 Publication
Mutagenesisi632 – 6321D → V: No effect on release of soluble GP1,2delta. 1 Publication
Mutagenesisi633 – 6331K → R or V: No effect on release of soluble GP1,2delta. 1 Publication
Mutagenesisi634 – 6341T → I: 50% loss of release of soluble GP1,2delta. 1 Publication
Mutagenesisi635 – 6351L → V: 60% loss of release of soluble GP1,2delta. 1 Publication
Mutagenesisi636 – 6361P → A: 60% loss of release of soluble GP1,2delta.
Mutagenesisi637 – 6371D → E: No effect on release of soluble GP1,2delta. 1 Publication
Mutagenesisi637 – 6371D → L or V: Increased release of soluble GP1,2delta. 1 Publication
Mutagenesisi638 – 6381Q → V: No effect on release of soluble GP1,2delta. 1 Publication
Mutagenesisi639 – 6391G → V: 40% loss of release of soluble GP1,2delta. 1 Publication
Mutagenesisi640 – 6401D → V: No effect on release of soluble GP1,2delta. 1 Publication
Mutagenesisi641 – 6411N → A: No effect on release of soluble GP1,2delta. 1 Publication
Mutagenesisi642 – 6421D → V: No effect on release of soluble GP1,2delta. 1 Publication
Mutagenesisi643 – 6431N → A: No effect on release of soluble GP1,2delta. 1 Publication
Mutagenesisi670 – 6701C → A: Reduced palmitoylation. No effect on GP processing and association with retrovirus particle. No loss of virus capability to enter into host cell. 2 Publications
Mutagenesisi670 – 6701C → F: Slightly reduced levels of expression of GP1 and GP2. Greatly reduced GP processing and association with retrovirus particle. 43% loss of virus capability to enter into host cell. 2 Publications
Mutagenesisi672 – 6721C → A: Reduced palmitoylation. No effect on GP processing and association with retrovirus particle. No loss of virus capability to enter into host cell. 2 Publications
Mutagenesisi672 – 6721C → F: Slightly reduced levels of expression of GP1 and GP2. Almost no effect on GP processing and association with retrovirus particle. 24% loss of virus capability to enter into host cell. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 676644Envelope glycoproteinPRO_0000037485Add
BLAST
Chaini33 – 501469GP1PRO_0000037486Add
BLAST
Chaini502 – 676175GP2PRO_0000037487Add
BLAST
Chaini502 – 637136GP2-deltaPRO_0000245066Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi53 ↔ 609Interchain (between GP1 and GP2 chains)1 Publication
Disulfide bondi108 ↔ 135Sequence Analysis
Disulfide bondi121 ↔ 147Sequence Analysis
Glycosylationi204 – 2041N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi228 – 2281N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi238 – 2381N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi257 – 2571N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi268 – 2681N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi296 – 2961N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi317 – 3171N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi346 – 3461N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi386 – 3861N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi413 – 4131N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi436 – 4361N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi454 – 4541N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi462 – 4621N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi511 ↔ 556Sequence Analysis
Glycosylationi563 – 5631N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi601 ↔ 6081 Publication
Glycosylationi618 – 6181N-linked (GlcNAc...); by hostSequence Analysis
Lipidationi670 – 6701S-palmitoyl cysteine; by host1 Publication
Lipidationi672 – 6721S-palmitoyl cysteine; by host1 Publication

Post-translational modificationi

The signal peptide region modulates GP's high mannose glycosylation, thereby determining the efficiency of the interactions with DC-SIGN(R).1 Publication
N-glycosylated.1 Publication
O-glycosylated in the mucin-like region.1 Publication
Palmitoylation of GP2 is not required for its function.1 Publication
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).5 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Interactioni

Subunit structurei

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 FOLR1.5 Publications

Structurei

Secondary structure

1
676
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 395Combined sources
Beta strandi42 – 465Combined sources
Beta strandi48 – 503Combined sources
Helixi60 – 623Combined sources
Beta strandi63 – 697Combined sources
Helixi70 – 734Combined sources
Helixi79 – 835Combined sources
Beta strandi86 – 927Combined sources
Beta strandi96 – 983Combined sources
Beta strandi100 – 1034Combined sources
Beta strandi105 – 11410Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi120 – 1223Combined sources
Beta strandi135 – 14410Combined sources
Beta strandi149 – 1546Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi163 – 1697Combined sources
Beta strandi175 – 18511Combined sources
Beta strandi216 – 22914Combined sources
Beta strandi231 – 2344Combined sources
Beta strandi240 – 2434Combined sources
Helixi250 – 26314Combined sources
Beta strandi268 – 2703Combined sources
Beta strandi273 – 2764Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi515 – 5206Combined sources
Turni528 – 5314Combined sources
Beta strandi532 – 5365Combined sources
Beta strandi541 – 5488Combined sources
Helixi560 – 59435Combined sources
Helixi595 – 5973Combined sources
Helixi600 – 6045Combined sources
Helixi605 – 6095Combined sources
Helixi616 – 62813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBOX-ray1.90A/B/C557-630[»]
2RLJNMR-A524-539[»]
3CSYX-ray3.40I/K/M/O32-311[»]
J/L/N/P502-632[»]
ProteinModelPortaliQ05320.
SMRiQ05320. Positions 32-310, 502-634.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05320.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 201148Receptor-bindingSequence AnalysisAdd
BLAST
Regioni305 – 485181Mucin-like regionAdd
BLAST
Regioni524 – 53916Fusion peptideCuratedAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili554 – 59542Sequence AnalysisAdd
BLAST
Coiled coili615 – 63420Sequence AnalysisAdd
BLAST

Domaini

The mucin-like region seems to be involved in the cytotoxic function. This region is also involved in binding to human CLEC10A.
The coiled coil regions play a role in oligomerization and fusion activity.

Sequence similaritiesi

Belongs to the filoviruses glycoprotein family.Curated

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR014625. GPC_FiloV.
IPR002561. GPC_filovir-type_extra_dom.
[Graphical view]
PfamiPF01611. Filo_glycop. 1 hit.
[Graphical view]
PIRSFiPIRSF036874. GPC_FiloV. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q05320-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVTGILQLP RDRFKRTSFF LWVIILFQRT FSIPLGVIHN STLQVSDVDK
60 70 80 90 100
LVCRDKLSST NQLRSVGLNL EGNGVATDVP SATKRWGFRS GVPPKVVNYE
110 120 130 140 150
AGEWAENCYN LEIKKPDGSE CLPAAPDGIR GFPRCRYVHK VSGTGPCAGD
160 170 180 190 200
FAFHKEGAFF LYDRLASTVI YRGTTFAEGV VAFLILPQAK KDFFSSHPLR
210 220 230 240 250
EPVNATEDPS SGYYSTTIRY QATGFGTNET EYLFEVDNLT YVQLESRFTP
260 270 280 290 300
QFLLQLNETI YTSGKRSNTT GKLIWKVNPE IDTTIGEWAF WETKKNLTRK
310 320 330 340 350
IRSEELSFTV VSNGAKNISG QSPARTSSDP GTNTTTEDHK IMASENSSAM
360 370 380 390 400
VQVHSQGREA AVSHLTTLAT ISTSPQSLTT KPGPDNSTHN TPVYKLDISE
410 420 430 440 450
ATQVEQHHRR TDNDSTASDT PSATTAAGPP KAENTNTSKS TDFLDPATTT
460 470 480 490 500
SPQNHSETAG NNNTHHQDTG EESASSGKLG LITNTIAGVA GLITGGRRTR
510 520 530 540 550
REAIVNAQPK CNPNLHYWTT QDEGAAIGLA WIPYFGPAAE GIYIEGLMHN
560 570 580 590 600
QDGLICGLRQ LANETTQALQ LFLRATTELR TFSILNRKAI DFLLQRWGGT
610 620 630 640 650
CHILGPDCCI EPHDWTKNIT DKIDQIIHDF VDKTLPDQGD NDNWWTGWRQ
660 670
WIPAGIGVTG VIIAVIALFC ICKFVF
Length:676
Mass (Da):74,464
Last modified:February 1, 1994 - v1
Checksum:iBE8AB3B339F63261
GO

Sequence cautioni

The sequence AAA96744.1 differs from that shown. Reason: Frameshift at position 296. Curated

RNA editingi

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 P60170), the +2A edited RNA gives rise to the super small secreted glycoprotein ssGP (AC Q9YMG2).

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651S → P in strain: Isolate mouse-adapted.
Natural varianti246 – 2461S → P in strain: Isolate mouse-adapted.
Natural varianti544 – 5441I → T.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11365 Genomic RNA. Translation: AAB81004.1.
U31033 Genomic RNA. Translation: AAA96744.1. Frameshift.
U23187 Genomic RNA. Translation: AAC54887.1.
AF272001 Genomic RNA. Translation: AAG40168.1.
AY142960 Genomic RNA. Translation: AAN37507.1.
AF086833 Genomic RNA. Translation: AAD14585.1.
AF499101 Genomic RNA. Translation: AAM76034.1.
PIRiS23155.
RefSeqiNP_066246.1. NC_002549.1.

Genome annotation databases

GeneIDi911829.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L11365 Genomic RNA. Translation: AAB81004.1 .
U31033 Genomic RNA. Translation: AAA96744.1 . Frameshift.
U23187 Genomic RNA. Translation: AAC54887.1 .
AF272001 Genomic RNA. Translation: AAG40168.1 .
AY142960 Genomic RNA. Translation: AAN37507.1 .
AF086833 Genomic RNA. Translation: AAD14585.1 .
AF499101 Genomic RNA. Translation: AAM76034.1 .
PIRi S23155.
RefSeqi NP_066246.1. NC_002549.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EBO X-ray 1.90 A/B/C 557-630 [» ]
2RLJ NMR - A 524-539 [» ]
3CSY X-ray 3.40 I/K/M/O 32-311 [» ]
J/L/N/P 502-632 [» ]
ProteinModelPortali Q05320.
SMRi Q05320. Positions 32-310, 502-634.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

TCDBi 1.G.12.2.2. the avian leukosis virus gp95 fusion protein (alv-gp95) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 911829.

Miscellaneous databases

EvolutionaryTracei Q05320.

Family and domain databases

InterProi IPR014625. GPC_FiloV.
IPR002561. GPC_filovir-type_extra_dom.
[Graphical view ]
Pfami PF01611. Filo_glycop. 1 hit.
[Graphical view ]
PIRSFi PIRSF036874. GPC_FiloV. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Sequence analysis of the Ebola virus genome: organization, genetic elements, and comparison with the genome of Marburg virus."
    Sanchez A., Kiley M.P., Holloway B.P., Auperin D.D.
    Virus Res. 29:215-240(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases."
    Volchkov V.E., Becker S., Volchkova V.A., Ternovoj V.A., Kotov A.N., Netesov S.V., Klenk H.-D.
    Virology 214:421-430(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA], RNA EDITING.
  3. "The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing."
    Sanchez A., Trappier S.G., Mahy B.W.J., Peters C.J., Nichol S.T.
    Proc. Natl. Acad. Sci. U.S.A. 93:3602-3607(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], RNA EDITING.
  4. "Molecular characterization of guinea pig-adapted variants of Ebola virus."
    Volchkov V.E., Chepurnov A.A., Volchkova V.A., Ternovoj V.A., Klenk H.D.
    Virology 277:147-155(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate guinea pig-adapted.
  5. Volchkov V.E.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  6. Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate mouse-adapted.
  7. "The envelope glycoprotein of Ebola virus contains an immunosuppressive-like domain similar to oncogenic retroviruses."
    Volchkov V.E., Blinov V.M., Netesov S.V.
    FEBS Lett. 305:181-184(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 359-676.
  8. "Processing of the Ebola virus glycoprotein by the proprotein convertase furin."
    Volchkov V.E., Feldmann H., Volchkova V.A., Klenk H.-D.
    Proc. Natl. Acad. Sci. U.S.A. 95:5762-5767(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF ENVELOPE GLYCOPROTEIN.
  9. "Release of viral glycoproteins during Ebola virus infection."
    Volchkov V.E., Volchkova V.A., Slenczka W., Klenk H.-D., Feldmann H.
    Virology 245:110-119(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF ENVELOPE GLYCOPROTEIN.
  10. "Phosphatidylinositol-dependent membrane fusion induced by a putative fusogenic sequence of Ebola virus."
    Ruiz-Arguello M.B., Goni F.M., Pereira F.B., Nieva J.L.
    J. Virol. 72:1775-1781(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN FUSION PEPTIDE.
  11. "Mutational analysis of the putative fusion domain of Ebola virus glycoprotein."
    Ito H., Watanabe S., Sanchez A., Whitt M.A., Kawaoka Y.
    J. Virol. 73:8907-8912(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN FUSION PEPTIDE, MUTAGENESIS OF GLY-528; LEU-529; ILE-532; PHE-535; GLY-536 AND PRO-537.
  12. "Endoproteolytic processing of the ebola virus envelope glycoprotein: cleavage is not required for function."
    Wool-Lewis R.J., Bates P.
    J. Virol. 73:1419-1426(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF ENVELOPE GLYCOPROTEIN, MUTAGENESIS OF 498-ARG--ARG-501.
  13. "Identification of the Ebola virus glycoprotein as the main viral determinant of vascular cell cytotoxicity and injury."
    Yang Z.-Y., Duckers H.J., Sullivan N.J., Sanchez A., Nabel E.G., Nabel G.J.
    Nat. Med. 6:886-889(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN MUCIN/LIKE REGION.
  14. "Downregulation of beta1 integrins by Ebola virus glycoprotein: implication for virus entry."
    Takada A., Watanabe S., Ito H., Okazaki K., Kida H., Kawaoka Y.
    Virology 278:20-26(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-MODULATION OF HOST ITGB1/BETA-1 INTEGRIN.
  15. "Ebola virus glycoprotein: proteolytic processing, acylation, cell tropism, and detection of neutralizing antibodies."
    Ito H., Watanabe S., Takada A., Kawaoka Y.
    J. Virol. 75:1576-1580(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF ENVELOPE GLYCOPROTEIN, PALMITOYLATION, MUTAGENESIS OF 497-ARG--ARG-501; CYS-670 AND CYS-672.
  16. "Functional importance of the coiled-coil of the Ebola virus glycoprotein."
    Watanabe S., Takada A., Watanabe T., Ito H., Kida H., Kawaoka Y.
    J. Virol. 74:10194-10201(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: COILED-COIL DOMAIN.
  17. "Folate receptor-alpha is a cofactor for cellular entry by Marburg and Ebola viruses."
    Chan S.Y., Empig C.J., Welte F.J., Speck R.F., Schmaljohn A., Kreisberg J.F., Goldsmith M.A.
    Cell 106:117-126(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN FOLR1.
  18. "Covalent modifications of the ebola virus glycoprotein."
    Jeffers S.A., Sanders D.A., Sanchez A.
    J. Virol. 76:12463-12472(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, GLYCOSYLATION, MUTAGENESIS OF ASN-40; CYS-53; CYS-108; CYS-121; CYS-135; CYS-147; ASN-204; ASN-238; ASN-257; ASN-296; CYS-511; CYS-556; ASN-563; CYS-601; CYS-608; CYS-609; ASN-618; CYS-670 AND CYS-672.
  19. "Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence."
    Simmons G., Wool-Lewis R.J., Baribaud F., Netter R.C., Bates P.
    J. Virol. 76:2518-2528(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-MODULATION OF HOST MHC-I; ALPHA/BETA INTEGRINS AND EGFR.
  20. "Lipid raft microdomains: a gateway for compartmentalized trafficking of Ebola and Marburg viruses."
    Bavari S., Bosio C.M., Wiegand E., Ruthel G., Will A.B., Geisbert T.W., Hevey M., Schmaljohn C., Schmaljohn A., Aman M.J.
    J. Exp. Med. 195:593-602(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  21. "C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans."
    Alvarez C.P., Lasala F., Carrillo J., Muniz O., Corbi A.L., Delgado R.
    J. Virol. 76:6841-6844(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN CD209 AND CLEC4M, ROLE IN TRANS INFECTION.
  22. "Folate receptor alpha and caveolae are not required for Ebola virus glycoprotein-mediated viral infection."
    Simmons G., Rennekamp A.J., Chai N., Vandenberghe L.H., Riley J.L., Bates P.
    J. Virol. 77:13433-13438(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PUTATIVE ROLE OF FOLR1 IN VIRUS ENTRY INTO THE CELL.
  23. "DC-SIGN and DC-SIGNR bind ebola glycoproteins and enhance infection of macrophages and endothelial cells."
    Simmons G., Reeves J.D., Grogan C.C., Vandenberghe L.H., Baribaud F., Whitbeck J.C., Burke E., Buchmeier M.J., Soilleux E.J., Riley J.L., Doms R.W., Bates P., Poehlmann S.
    Virology 305:115-123(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN CD209 AND CLEC4M.
  24. Cited for: CLEAVAGE BY HOST ADAM17, MUTAGENESIS OF ASP-632; LYS-633; THR-634; LEU-635; ASP-637; GLN-638; GLY-639; ASP-640; ASN-641; ASP-642 AND ASN-643.
  25. "Human macrophage C-type lectin specific for galactose and N-acetylgalactosamine promotes filovirus entry."
    Takada A., Fujioka K., Tsuiji M., Morikawa A., Higashi N., Ebihara H., Kobasa D., Feldmann H., Irimura T., Kawaoka Y.
    J. Virol. 78:2943-2947(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN CLEC10A.
  26. "Effects of Ebola virus glycoproteins on endothelial cell activation and barrier function."
    Wahl-Jensen V.M., Afanasieva T.A., Seebach J., Stroeher U., Feldmann H., Schnittler H.J.
    J. Virol. 79:10442-10450(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOTHELIAL CELLS ACTIVATION.
  27. "Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection."
    Chandran K., Sullivan N.J., Felbor U., Whelan S.P., Cunningham J.M.
    Science 308:1643-1645(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYSIS OF GP1.
  28. "Role of Ebola virus secreted glycoproteins and virus-like particles in activation of human macrophages."
    Wahl-Jensen V., Kurz S.K., Hazelton P.R., Schnittler H.J., Stroeher U., Burton D.R., Feldmann H.
    J. Virol. 79:2413-2419(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF GP1,2DELTA.
  29. "Ebola virus glycoprotein toxicity is mediated by a dynamin-dependent protein-trafficking pathway."
    Sullivan N.J., Peterson M., Yang Z.-Y., Kong W.-P., Duckers H., Nabel E., Nabel G.J.
    J. Virol. 79:547-553(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-MODULATION OF HOST INTEGRIN DIMER ALPHA-V/BETA-3, INTERACTION WITH HUMAN INTEGRIN ITGAV.
  30. "Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein."
    Schornberg K., Matsuyama S., Kabsch K., Delos S., Bouton A., White J.
    J. Virol. 80:4174-4178(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYSIS OF GP1.
  31. "Ebola virus glycoprotein GP is not cytotoxic when expressed constitutively at a moderate level."
    Alazard-Dany N., Volchkova V., Reynard O., Carbonnelle C., Dolnik O., Ottmann M., Khromykh A., Volchkov V.E.
    J. Gen. Virol. 87:1247-1257(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  32. "The signal peptide of the ebolavirus glycoprotein influences interaction with the cellular lectins DC-SIGN and DC-SIGNR."
    Marzi A., Akhavan A., Simmons G., Gramberg T., Hofmann H., Bates P., Lingappa V.R., Poehlmann S.
    J. Virol. 80:6305-6317(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF SIGNAL PEPTIDE.
  33. "Conserved receptor-binding domains of Lake Victoria marburgvirus and Zaire ebolavirus bind a common receptor."
    Kuhn J.H., Radoshitzky S.R., Guth A.C., Warfield K.L., Li W., Vincent M.J., Towner J.S., Nichol S.T., Bavari S., Choe H., Aman M.J., Farzan M.
    J. Biol. Chem. 281:15951-15958(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECEPTOR-BINDING REGION.
  34. "Cellular entry of ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes."
    Saeed M.F., Kolokoltsov A.A., Albrecht T., Davey R.A.
    PLoS Pathog. 6:0-0(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  35. "Ebola virus uses clathrin-mediated endocytosis as an entry pathway."
    Bhattacharyya S., Warfield K.L., Ruthel G., Bavari S., Aman M.J., Hope T.J.
    Virology 401:18-28(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  36. "Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolution."
    Malashkevich V.N., Schneider B.J., McNally M.L., Milhollen M.A., Pang J.X., Kim P.S.
    Proc. Natl. Acad. Sci. U.S.A. 96:2662-2667(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 557-630.

Entry informationi

Entry nameiVGP_EBOZM
AccessioniPrimary (citable) accession number: Q05320
Secondary accession number(s): Q66818
, Q77LU5, Q8B9S1, Q8JS62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 26, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Filoviruses entry requires functional lipid rafts at the host cell surface.
Essential for infectivity, as it is the sole viral protein expressed at the virion surface.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3