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Protein

Envelope glycoprotein

Gene

GP

Organism
Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus)
Status
Reviewed-Annotation score: 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, allowing its binding to the host entry receptor NPC1 and unmasking its fusion peptide to initiate membranes fusion (PubMed:22031933, PubMed:26516900).2 Publications
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.
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 (PubMed:26516900).1 Publication
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)DescriptionActionsGraphical viewLength
Sitei57Involved in receptor recognition and/or post-binding eventsSequence analysis1
Sitei63Involved in receptor recognition and/or post-binding eventsSequence analysis1
Sitei64Involved in receptor recognition and/or post-binding eventsSequence analysis1
Sitei88Involved in receptor recognition and/or post-binding eventsSequence analysis1
Sitei95Involved in receptor recognition and/or post-binding eventsSequence analysis1
Sitei170Involved in receptor recognition and/or post-binding eventsSequence analysis1

GO - Biological processi

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 attachment to host entry receptor, 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 virusesssRNA 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]
Proteomesi
  • UP000007209 Componenti: Genome

Subcellular locationi

GP2 :
GP1 :
GP2-delta :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini33 – 650ExtracellularSequence analysisAdd BLAST618
Transmembranei651 – 671HelicalSequence analysisAdd BLAST21
Topological domaini672 – 676CytoplasmicSequence analysis5

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • host cell cytoplasm Source: CACAO
  • host cell endoplasmic reticulum Source: CACAO
  • host cell plasma membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane raft Source: CACAO
  • viral envelope Source: UniProtKB-KW
  • virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40N → D: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi53C → G: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi55D → A: 80% loss of virus capability to enter into host cell. 1
Mutagenesisi55D → E or K: No effect on viral entry. 1
Mutagenesisi57L → A: Complete loss of virus capability to enter into host cell. 1
Mutagenesisi57L → F, I or K: 90% loss of virus capability to enter into host cell. 1
Mutagenesisi63L → A: 90% loss of virus capability to enter into host cell. 1
Mutagenesisi63L → F: Almost complete loss of virus capability to enter into host cell. 1
Mutagenesisi63L → K: Complete loss of virus capability to enter into host cell. 1
Mutagenesisi64R → A or E: Complete loss of virus capability to enter into host cell. 1
Mutagenesisi64R → K: No loss of virus capability to enter into host cell. 1
Mutagenesisi88F → A or E: Complete loss of virus capability to enter into host cell. 1
Mutagenesisi88F → I: No loss of virus capability to enter into host cell. 1
Mutagenesisi95K → A or E: 80% loss of virus capability to enter into host cell. 1
Mutagenesisi95K → R: 20% loss of virus capability to enter into host cell. 1
Mutagenesisi108C → G: Almost complete loss of expression of GP1 and GP2. Almost complete loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi121C → G: Reduced levels of expression of GP1 and GP2. 50% loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi135C → S: Almost complete loss of expression of GP1 and GP2. Complete loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi147C → S: Reduced levels of expression of GP1 and GP2. Almost complete loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi170I → A: 90% loss of virus capability to enter into host cell. 1
Mutagenesisi170I → E: Complete loss of virus capability to enter into host cell. 1
Mutagenesisi170I → F: 50% loss of virus capability to enter into host cell. 1
Mutagenesisi204N → D: No effect on GP1 and GP2 expression. No loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi238N → Y: No effect on GP1 and GP2 expression. 12% loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi257N → D: No effect on GP1 and GP2 expression. 12% loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi296N → D: No effect on GP1 and GP2 expression. 18% loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi497 – 501RRTRR → AGTAA: Almost complete loss of cleavage between GP1 and GP2. No loss of infectivity. 1 Publication5
Mutagenesisi498 – 501RTRR → ATAA: No effect on cleavage between GP1 and GP2. 1 Publication4
Mutagenesisi511C → G: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi528G → R: Reduced infectivity. 1 Publication1
Mutagenesisi529L → A or R: Reduced infectivity. 1 Publication1
Mutagenesisi532I → A: Reduced infectivity. 1 Publication1
Mutagenesisi532I → R: Almost complete loss of infectivity. No effect on transport of GP to the cell surface and incorporation onto virions. 1 Publication1
Mutagenesisi535F → A: Reduced infectivity. 1 Publication1
Mutagenesisi535F → R: Almost complete loss of infectivity. No effect on transport of GP to the cell surface and incorporation onto virions. 1 Publication1
Mutagenesisi536G → A: Almost complete loss of infectivity. No effect on transport of GP to the cell surface and incorporation onto virions. 1 Publication1
Mutagenesisi537P → R: Almost complete loss of infectivity. No effect on transport of GP to the cell surface and incorporation onto virions. 1 Publication1
Mutagenesisi556C → S: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi563N → D: Reduced levels of expression of GP, GP1 and GP2. 20% loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi601C → S: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi608C → G: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi609C → G: Induces GP1 secretion. Complete loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi618N → D: Slightly reduced levels of expression of GP1 and GP2. No loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi632D → V: No effect on release of soluble GP1,2delta. 1 Publication1
Mutagenesisi633K → R or V: No effect on release of soluble GP1,2delta. 1 Publication1
Mutagenesisi634T → I: 50% loss of release of soluble GP1,2delta. 1 Publication1
Mutagenesisi635L → V: 60% loss of release of soluble GP1,2delta. 1 Publication1
Mutagenesisi636P → A: 60% loss of release of soluble GP1,2delta. 1
Mutagenesisi637D → E: No effect on release of soluble GP1,2delta. 1 Publication1
Mutagenesisi637D → L or V: Increased release of soluble GP1,2delta. 1 Publication1
Mutagenesisi638Q → V: No effect on release of soluble GP1,2delta. 1 Publication1
Mutagenesisi639G → V: 40% loss of release of soluble GP1,2delta. 1 Publication1
Mutagenesisi640D → V: No effect on release of soluble GP1,2delta. 1 Publication1
Mutagenesisi641N → A: No effect on release of soluble GP1,2delta. 1 Publication1
Mutagenesisi642D → V: No effect on release of soluble GP1,2delta. 1 Publication1
Mutagenesisi643N → A: No effect on release of soluble GP1,2delta. 1 Publication1
Mutagenesisi670C → A: Reduced palmitoylation. No effect on GP processing and association with retrovirus particle. No loss of virus capability to enter into host cell. Loss of localization to the rafts; when associated with A-670. 3 Publications1
Mutagenesisi670C → 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. Loss of localization to the rafts; when associated with A-672. 3 Publications1
Mutagenesisi672C → A: Reduced palmitoylation. No effect on GP processing and association with retrovirus particle. No loss of virus capability to enter into host cell. 2 Publications1
Mutagenesisi672C → 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 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Sequence analysisAdd BLAST32
ChainiPRO_000003748533 – 676Envelope glycoproteinAdd BLAST644
ChainiPRO_000003748633 – 501GP1Add BLAST469
ChainiPRO_0000037487502 – 676GP2Add BLAST175
ChainiPRO_0000245066502 – 637GP2-deltaAdd BLAST136

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi53 ↔ 609Interchain (between GP1 and GP2 chains)1 Publication
Disulfide bondi108 ↔ 135Sequence analysis
Disulfide bondi121 ↔ 147Sequence analysis
Glycosylationi204N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi228N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi238N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi257N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi268N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi296N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi317N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi333N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi346N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi386N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi413N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi436N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi454N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi462N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi511 ↔ 556Sequence analysis
Glycosylationi563N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi601 ↔ 6081 Publication
Glycosylationi618N-linked (GlcNAc...); by hostSequence analysis1
Lipidationi670S-palmitoyl cysteine; by host1 Publication1
Lipidationi672S-palmitoyl cysteine; by host1 Publication1

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 (PubMed:9576958, PubMed:9614872) (PubMed:9882347). The cleavage site corresponds to the furin optimal cleavage sequence [KR]-X-[KR]-R (PubMed:9576958). This cleavage does not seem to be required for function (PubMed:9576958). 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 (PubMed:16571833). This cleaved 19-kDa GP1 can then bind to the host entry receptor NPC1 (PubMed:21866103). 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) (PubMed:15103332).7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei501 – 502Cleavage; by host furin1 Publication2
Sitei637 – 638Cleavage; by host ADAM171 Publication2

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. Interacts with host entry receptor NPC1.6 Publications

Protein-protein interaction databases

DIPiDIP-62002N.

Structurei

Secondary structure

1676
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 39Combined sources4
Beta strandi42 – 45Combined sources4
Turni48 – 50Combined sources3
Helixi60 – 62Combined sources3
Beta strandi63 – 69Combined sources7
Helixi70 – 73Combined sources4
Helixi79 – 83Combined sources5
Beta strandi86 – 91Combined sources6
Beta strandi96 – 98Combined sources3
Beta strandi100 – 103Combined sources4
Beta strandi105 – 114Combined sources10
Beta strandi116 – 118Combined sources3
Beta strandi120 – 122Combined sources3
Beta strandi135 – 144Combined sources10
Beta strandi149 – 154Combined sources6
Beta strandi159 – 161Combined sources3
Beta strandi163 – 169Combined sources7
Beta strandi176 – 185Combined sources10
Beta strandi216 – 224Combined sources9
Beta strandi227 – 229Combined sources3
Beta strandi231 – 237Combined sources7
Beta strandi240 – 243Combined sources4
Helixi250 – 263Combined sources14
Beta strandi269 – 271Combined sources3
Beta strandi273 – 277Combined sources5
Turni290 – 292Combined sources3
Beta strandi307 – 310Combined sources4
Beta strandi515 – 520Combined sources6
Turni528 – 531Combined sources4
Turni533 – 535Combined sources3
Helixi539 – 541Combined sources3
Beta strandi543 – 548Combined sources6
Helixi551 – 553Combined sources3
Helixi560 – 594Combined sources35
Helixi595 – 597Combined sources3
Helixi600 – 604Combined sources5
Helixi605 – 609Combined sources5
Helixi616 – 628Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EBOX-ray1.90A/B/C557-630[»]
2RLJNMR-A524-539[»]
3CSYX-ray3.40I/K/M/O32-311[»]
J/L/N/P502-632[»]
5FHCX-ray6.70J502-599[»]
K1-308[»]
K490-501[»]
5HJ3X-ray3.30C/G/K/O32-194[»]
5JQ3X-ray2.23A32-501[»]
B502-632[»]
5JQ7X-ray2.69A32-501[»]
B502-632[»]
5JQBX-ray2.68A32-501[»]
B502-632[»]
5KELelectron microscopy4.30A/E/F33-501[»]
B/G/I502-637[»]
5KEMelectron microscopy5.50A/F53-284[»]
5KENelectron microscopy4.30A/E/K33-308[»]
B/F/M503-615[»]
ProteinModelPortaliQ05320.
SMRiQ05320.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05320.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni54 – 201Receptor-bindingSequence analysisAdd BLAST148
Regioni305 – 485Mucin-like regionAdd BLAST181
Regioni524 – 539Fusion peptideCuratedAdd BLAST16

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili554 – 595Sequence analysisAdd BLAST42
Coiled coili615 – 634Sequence analysisAdd BLAST20

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 differs from that shown. Reason: Frameshift at position 296.Curated

RNA editingi

Edited at position 295.2 Publications
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)DescriptionActionsGraphical viewLength
Natural varianti65S → P in strain: Isolate mouse-adapted. 1
Natural varianti246S → P in strain: Isolate mouse-adapted. 1
Natural varianti544I → T.1

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.
KEGGivg:911829.

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.
PIRiS23155.
RefSeqiNP_066246.1. NC_002549.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EBOX-ray1.90A/B/C557-630[»]
2RLJNMR-A524-539[»]
3CSYX-ray3.40I/K/M/O32-311[»]
J/L/N/P502-632[»]
5FHCX-ray6.70J502-599[»]
K1-308[»]
K490-501[»]
5HJ3X-ray3.30C/G/K/O32-194[»]
5JQ3X-ray2.23A32-501[»]
B502-632[»]
5JQ7X-ray2.69A32-501[»]
B502-632[»]
5JQBX-ray2.68A32-501[»]
B502-632[»]
5KELelectron microscopy4.30A/E/F33-501[»]
B/G/I502-637[»]
5KEMelectron microscopy5.50A/F53-284[»]
5KENelectron microscopy4.30A/E/K33-308[»]
B/F/M503-615[»]
ProteinModelPortaliQ05320.
SMRiQ05320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-62002N.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi911829.
KEGGivg:911829.

Miscellaneous databases

EvolutionaryTraceiQ05320.

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.
ProtoNetiSearch...

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 2, 2016
This is version 119 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.