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Protein

Envelope glycoprotein

Gene

GP

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

Functioni

Envelope glycoprotein: Trimeric GP1,2 complexes form the virion surface spikes and mediate the viral entry processes, with GP1 acting as the receptor-binding subunit and GP2 as the membrane fusion subunit. At later times of infection, downregulates the expression of various host cell surface molecules that are essential for immune surveillance and cell adhesion. Down-modulates several integrins including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1. This decrease in cell adhesion molecules may lead to cell detachment, contributing to the disruption of blood vessel integrity and hemorrhages developed during infection (cytotoxicity). Interacts with host TLR4 and thereby stimulates the differentiation and activation of monocytes leading to bystander death of T-lymphocytes (PubMed:28542576). Downregulates as well the function of host natural killer cells (PubMed:30013549). Counteracts the antiviral effect of host BST2/tetherin that restricts release of progeny virions from infected cells. However, cooperates with VP40 and host BST2 to activate canonical NF-kappa-B pathway in a manner dependent on neddylation.6 Publications
Shed GP: Functions as a decoy for anti-GP1,2 antibodies therby contributing to viral immune evasion. Interacts and activates host macrophages and dendritic cells inducing up-regulation of cytokine transcription. This effect is mediated throught activation of host TLR4.3 Publications
GP1: 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 dendritic cells (DCs) and endothelial cells. 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.

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.

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 - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

Keywordsi

Biological processClathrin-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:
Alternative name(s):
GP1,2-delta
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
  • UP000109874 Componenti: Genome
  • UP000149419 Componenti: Genome
  • UP000150973 Componenti: Genome

Subcellular locationi

GP2 :
GP1 :
Shed GP :

Topology

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

GO - Cellular componenti

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 → A: About 50% loss of ability to counteract host BST2. 1 Publication1
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
Mutagenesisi111L → A: About 60% loss of ability to counteract host BST2. 1 Publication1
Mutagenesisi121C → G: Reduced levels of expression of GP1 and GP2. 50% loss of virus capability to enter into host cell. 1 Publication1
Mutagenesisi122L → A: About 60% loss of ability to counteract host BST2. 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
Mutagenesisi635L → V: Increased GP shedding. 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
Mutagenesisi637D → V: Decreased GP shedding. 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
Mutagenesisi660G → L: About 60% loss of viral release; when associated with L-664. 1 Publication1
Mutagenesisi664A → L: About 60% loss of viral release; when associated with L-660. 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
ChainiPRO_00004456861 – 637Shed GPAdd BLAST637
Signal peptidei1 – 32Sequence analysisAdd BLAST32
ChainiPRO_000003748533 – 676Envelope glycoproteinAdd BLAST644
ChainiPRO_000003748633 – 501GP1Add BLAST469
ChainiPRO_0000037487502 – 676GP2Add BLAST175

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi53 ↔ 609Interchain (between GP1 and GP2 chains)1 Publication
Disulfide bondi108 ↔ 135Sequence analysis
Disulfide bondi121 ↔ 147Sequence analysis
Glycosylationi204N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi228N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi238N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi257N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi268N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi296N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi317N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi333N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi346N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi386N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi413N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi436N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi454N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi462N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi511 ↔ 556Sequence analysis
Glycosylationi563N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi601 ↔ 6081 Publication
Glycosylationi618N-linked (GlcNAc...) asparagine; 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
Shed GP: Glycosylated; glycosylation is essential for the activation of dendritic cells and macrophages.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

Proteomic databases

PRIDEiQ05320

Interactioni

Subunit structurei

Envelope glycoprotein: 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. Interacts with host integrin alpha-V/ITGAV and CLEC10A. Binds also to host CD209 and CLEC4M/DC-SIGN(R), as well as host FOLR1. Interacts with host entry receptor NPC1. Interacts with BST2; this interaction inhibits the antiviral effect of BST2 and this allows viral release from infected cells. Interacts with host FCN1; this interaction enhances viral entry (PubMed:26984723). Interacts with host TLR4; this interaction induces T-lymphocyte death (PubMed:28542576). Shed GP: GP1 and GP2delta are part of GP1,2delta soluble complexes released by ectodomain shedding.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-16200230,EBI-16200230

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-62002N
ELMiQ05320
IntActiQ05320, 1 interactor

Structurei

Secondary structure

1676
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi660 – 664Important role for host BST2/tetherin antagonism1 Publication5

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

Phylogenomic databases

OrthoDBiVOG09000092

Family and domain databases

InterProiView protein in InterPro
IPR014625 GPC_FiloV
IPR002561 GPC_filovir-type_extra_dom
PfamiView protein in Pfam
PF01611 Filo_glycop, 1 hit
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

Similar proteinsi

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/P464-501[»]
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[»]
6F5UX-ray2.07A32-312[»]
B502-632[»]
6F6IX-ray2.40A32-336[»]
B502-632[»]
6F6NX-ray2.15A32-336[»]
6F6SX-ray2.29A32-336[»]
6G95X-ray2.31A32-311[»]
B502-632[»]
6G9BX-ray2.26A32-311[»]
B502-632[»]
6G9IX-ray2.19A32-311[»]
B502-632[»]
ProteinModelPortaliQ05320
SMRiQ05320
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-62002N
ELMiQ05320
IntActiQ05320, 1 interactor

Protein family/group databases

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

Proteomic databases

PRIDEiQ05320

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi911829
KEGGivg:911829

Phylogenomic databases

OrthoDBiVOG09000092

Miscellaneous databases

EvolutionaryTraceiQ05320

Family and domain databases

InterProiView protein in InterPro
IPR014625 GPC_FiloV
IPR002561 GPC_filovir-type_extra_dom
PfamiView protein in Pfam
PF01611 Filo_glycop, 1 hit
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 historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 7, 2018
This is version 131 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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