Reviewed
Aedimorphus [TaxID: 53540]; Diceromyia [TaxID: 53539]; Erythrocebus Patas (Red Guenon) (Cercopithecus Patas) [TaxID: 9538]; Homo Sapiens (Human) [TaxID: 9606]; Stegomyia [TaxID: 53541]
Not Available
♦Genome polyprotein [Cleaved into: Envelope protein E
♦ Non-structural protein 1 (NS1)
♦ Non-structural protein 2A (NS2A)
♦ Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Non-structural protein 3)] (Fragments)
♦ Non-structural protein 1 (NS1)
♦ Non-structural protein 2A (NS2A)
♦ Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Non-structural protein 3)] (Fragments)
Dengue Virus Type 2 (strain Tonga/EKB194/1974) (DENV-2)
Viruses> SsRNA Viruses> SsRNA Positive-strand Viruses> No DNA Stage> Flaviviridae> Flavivirus (arboviruses Group B)> Dengue Virus Group> Dengue Virus> Dengue Virus 2> Dengue Virus Type 2 (strain Tonga/EKB194/1974) (DENV-2)
Various pathway(s) in which protein is involved
Not Available
Not Available
MRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTDSRCPTQGEPTLNEEQDKRFVCKHSMVDRG
WGNGCGLFGKGGIVTCAMFTCKKNMEGKIVQPENLEYTVVITPHSGEEHAVGNDTGKHGKEVKITPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQ
MEDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYS
MCTGKFKIVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLDWFKKGSSIGQ
MFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVFGAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVSLVLVGIVTLYLGVMVQADSGCV
VSWKNKELKCGSGIFVTDNVHTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITSELNHILSENEVKLTIMTGDIKGIMQVGKRSLR
PQPTELRYSWKTWGKAKMLSTELHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLRLREKQDVFCDSKLMSAAIKDNRAVHADMGYWIESA
LNDTWKIEKASFIEVKSCHWPKSHTLWSNGVLESEMVIPKNFAGPVSQHNNRPGYYTQTAGPWHLGKLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASG
KLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENLVSSLVTAGHGQIDNFSLGILGMALFLEEMLRTRVGTKHAILLVAVSFVTLITGNMSFRDL
GRVMVMVGATMTDDIGMGVTYLALLAAFRVRPTFAAGLLLRKLTSKELMMTTIGIVLLSQSSIPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAIL
CVPNAVILQNAWKVSCTILAVVSVSPLLLTSSQQKADWIPLALTIKGLNPTAIFLTTLSRTSKKRAGVLWDVPSPPPVGKAELEDGAYRIKQKGILGYSQ
IGAGVYKEGTFHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFRTNTGTIGAVSLDFSPGTS
GSPIVDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLPAIVREAIKRGLRTLILAPTRVVAAEMEEAL
RGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPIRVPNYNLIIMDEAHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIMDE
EREIPERSWNSGHEWVTDFKGKTVWFVPSIKTGNDIAACLRKNGKRVIQLSRKTFDSEYVKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILT
DGEERVILAGPMPVTHSSAAQRRGRIGRNPRNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSIFEPEREKVDAIDGEYRLRGEARKTFVD
LMRRGDLPVWLAYKVAAEGINYADRRWCFDGTRNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPLALKEFKEFAAGRK
WGNGCGLFGKGGIVTCAMFTCKKNMEGKIVQPENLEYTVVITPHSGEEHAVGNDTGKHGKEVKITPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQ
MEDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYS
MCTGKFKIVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLDWFKKGSSIGQ
MFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVFGAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVSLVLVGIVTLYLGVMVQADSGCV
VSWKNKELKCGSGIFVTDNVHTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITSELNHILSENEVKLTIMTGDIKGIMQVGKRSLR
PQPTELRYSWKTWGKAKMLSTELHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLRLREKQDVFCDSKLMSAAIKDNRAVHADMGYWIESA
LNDTWKIEKASFIEVKSCHWPKSHTLWSNGVLESEMVIPKNFAGPVSQHNNRPGYYTQTAGPWHLGKLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASG
KLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENLVSSLVTAGHGQIDNFSLGILGMALFLEEMLRTRVGTKHAILLVAVSFVTLITGNMSFRDL
GRVMVMVGATMTDDIGMGVTYLALLAAFRVRPTFAAGLLLRKLTSKELMMTTIGIVLLSQSSIPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAIL
CVPNAVILQNAWKVSCTILAVVSVSPLLLTSSQQKADWIPLALTIKGLNPTAIFLTTLSRTSKKRAGVLWDVPSPPPVGKAELEDGAYRIKQKGILGYSQ
IGAGVYKEGTFHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFRTNTGTIGAVSLDFSPGTS
GSPIVDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLPAIVREAIKRGLRTLILAPTRVVAAEMEEAL
RGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPIRVPNYNLIIMDEAHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIMDE
EREIPERSWNSGHEWVTDFKGKTVWFVPSIKTGNDIAACLRKNGKRVIQLSRKTFDSEYVKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILT
DGEERVILAGPMPVTHSSAAQRRGRIGRNPRNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSIFEPEREKVDAIDGEYRLRGEARKTFVD
LMRRGDLPVWLAYKVAAEGINYADRRWCFDGTRNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPLALKEFKEFAAGRK
1683
Not Available
Not Available
01-08-1992
Evidence at protein level
| Amino Acid | Count | % Frequency | Amino Acid | Count | % Frequency |
|---|---|---|---|---|---|
| Alanine (A) | Leucine (L) | ||||
| Arginine (R) | Lysine (K) | ||||
| Asparagine (N) | Methionine (M) | ||||
| Aspartic Acid (D) | Phenylalanine (F) | ||||
| Cysteine (C) | Proline (P) | ||||
| Glutamine (Q) | Serine (S) | ||||
| Glutamic Acid (E) | Threonine (T) | ||||
| Glycine (G) | Tryptophan (W) | ||||
| Histidine (H) | Tyrosine (Y) | ||||
| Isoleucine (I) | Valine (V) |
| % Number of Residues in Helices | % Number of Residues in Strands | % Number of Residues in Coils |
|---|---|---|
♦Envelope protein E: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is inefficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion.
♦ Non-structural protein 1: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).
♦ Non-structural protein 1: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease.
♦ Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.
♦ Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).
♦ Serine protease NS3: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
♦ Non-structural protein 1: Involved in immune evasion, pathogenesis and viral replication. Once cleaved off the polyprotein, is targeted to three destinations: the viral replication cycle, the plasma membrane and the extracellular compartment. Essential for viral replication. Required for formation of the replication complex and recruitment of other non-structural proteins to the ER-derived membrane structures. Excreted as a hexameric lipoparticle that plays a role against host immune response. Antagonizing the complement function. Binds to the host macrophages and dendritic cells. Inhibits signal transduction originating from Toll-like receptor 3 (TLR3).
♦ Non-structural protein 1: Disrupts the host endothelial glycocalyx layer of host pulmonary microvascular endothelial cells, inducing degradation of sialic acid and shedding of heparan sulfate proteoglycans. NS1 induces expression of sialidases, heparanase, and activates cathepsin L, which activates heparanase via enzymatic cleavage. These effects are probably linked to the endothelial hyperpermeability observed in severe dengue disease.
♦ Non-structural protein 2A: Component of the viral RNA replication complex that functions in virion assembly and antagonizes the host immune response.
♦ Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3. May have membrane-destabilizing activity and form viroporins (By similarity).
♦ Serine protease NS3: Displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction.
3.4.21.91 , 3.6.1.15 , 3.6.4.13
GO:0003724 ; GO:0003725 ; GO:0005524 ; GO:0005576 ; GO:0008026 ;
GO:0008236 ; GO:0016021 ; GO:0019013 ; GO:0019031 ; GO:0019062 ;
GO:0039654 ; GO:0044167 ; GO:0046983 ; GO:0055036 ; GO:0075512
GO:0008236 ; GO:0016021 ; GO:0019013 ; GO:0019031 ; GO:0019062 ;
GO:0039654 ; GO:0044167 ; GO:0046983 ; GO:0055036 ; GO:0075512
♦ Envelope protein E: Virion membrane
♦ Multi-pass membrane protein . Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein .
♦ Non-structural protein 1: Secreted . Host endoplasmic reticulum membrane
♦ Peripheral membrane protein
♦ Lumenal side . Note=Located in RE-derived vesicles hosting the replication complex. Q6P4.
♦ Non-structural protein 2A: Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein .
♦ Serine protease NS3: Host endoplasmic reticulum membrane PROSITE-ProRule:PRU00860
♦ Peripheral membrane protein PROSITE-ProRule:PRU00860
♦ Cytoplasmic side PROSITE-ProRule:PRU00860. Note=Remains non-covalently associated to serine protease subunit NS2B. PROSITE-ProRule:PRU00860.
♦ Multi-pass membrane protein . Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein .
♦ Non-structural protein 1: Secreted . Host endoplasmic reticulum membrane
♦ Peripheral membrane protein
♦ Lumenal side . Note=Located in RE-derived vesicles hosting the replication complex. Q6P4.
♦ Non-structural protein 2A: Host endoplasmic reticulum membrane
♦ Multi-pass membrane protein .
♦ Serine protease NS3: Host endoplasmic reticulum membrane PROSITE-ProRule:PRU00860
♦ Peripheral membrane protein PROSITE-ProRule:PRU00860
♦ Cytoplasmic side PROSITE-ProRule:PRU00860. Note=Remains non-covalently associated to serine protease subunit NS2B. PROSITE-ProRule:PRU00860.
♦DOMAIN 1066 1243 Peptidase S7.
♦ DOMAIN 1245 1401 Helicase ATP-binding.
♦ DOMAIN 1411 1582 Helicase C-terminal.
♦ DOMAIN 1245 1401 Helicase ATP-binding.
♦ DOMAIN 1411 1582 Helicase C-terminal.
MOTIF 1349 1352 DEAH box.
X-ray crystallography (1); Electron microscopy (1)
♦ACT_SITE 1116 1116 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 1140 1140 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 1200 1200 Charge relay system
♦ for serine protease NS3 activity.
♦ for serine protease NS3 activity.
♦ ACT_SITE 1140 1140 Charge relay system
♦ for serine protease NS3 activity.
♦ ACT_SITE 1200 1200 Charge relay system
♦ for serine protease NS3 activity.
Protein couldn't be modeled using I-Tasser and Raptor X because of length constraints of the software.