Protein C
     (Core protein)
     (Capsid protein)
prM
Peptide pr
Small envelope protein M
     (Matrix protein)
Envelope protein E
Non-structural protein 1
     (NS1)
Non-structural protein 2A
     (NS2A)
Non-structural protein 2A-alpha
     (NS2A-alpha)
Serine protease subunit NS2B
     (Non-structural protein 2B)
Serine protease subunit NS3
     (EC 3.4.21.91)
     (Non-structural protein 3)
Non-structural protein 4A
     (NS4A)
Peptide 2k
Non-structural protein 4B
     (NS4B)
RNA-directed RNA polymerase NS5
     (EC 2.7.7.48)
     (EC 2.1.1.56)
     (Non-structural protein 5)

Gene name

None

From

Dengue virus type 3 (strain Philippines/H87/1956) (DENV-3)

[TaxID: 408870]

Taxonomy

Viruses; ssRNA positive-strand viruses, no DNA stage; Flaviviridae; Flavivirus; Dengue virus group.

Virus hosts

Aedimorphus [TaxID: 53540]
Diceromyia [TaxID: 53539]
Erythrocebus patas (Red guenon) (Cercopithecus patas) [TaxID: 9538]
Homo sapiens (Human) [TaxID: 9606]
Stegomyia [TaxID: 53541]

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND PARTIAL PROTEIN SEQUENCE. DOI=10.1016/0042-6822(90)90037-R; PubMed=2345967 [NCBI, ExPASy, EBI, Israel, Japan] Osatomi K., Sumiyoshi H.; "Complete nucleotide sequence of dengue type 3 virus genome RNA."; Virology 176:643-647(1990).
[2]	X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 281-672. DOI=10.1128/JVI.79.2.1223-1231.2005; PubMed=15613349 [NCBI, ExPASy, EBI, Israel, Japan] Modis Y., Ogata S., Clements D., Harrison S.C.; "Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein."; J. Virol. 79:1223-1231(2005).

Comments

FUNCTION: The small proteins NS2A, NS4A and NS4B are hydrophobic, suggesting a possible membrane-related function. NS5 may play a role in the viral RNA replication. The NS2B/NS3 protease complex processes the viral polyprotein.
CATALYTIC ACTIVITY: Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m₇G(5')pppR-RNA.
SUBUNIT: NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter (By similarity).
SUBCELLULAR LOCATION: Protein C: Virion (Potential). Membrane; Single-pass membrane protein (Potential).
SUBCELLULAR LOCATION: Small envelope protein M: Virion (Potential). Membrane; Single-pass membrane protein (Potential).
SUBCELLULAR LOCATION: Envelope protein E: Virion (Potential). Membrane; Multi-pass membrane protein (Potential).
SUBCELLULAR LOCATION: Non-structural protein 4A: Membrane; Single-pass membrane protein (Potential).
SUBCELLULAR LOCATION: Non-structural protein 4B: Membrane; Multi-pass membrane protein (Potential).
PTM: Specific enzymatic cleavages in vivo yield mature proteins (By similarity).
MISCELLANEOUS: The virion of this virus is a nucleocapsid covered by a lipoprotein envelope. The envelope contains two proteins: the protein M and glycoprotein E. The nucleocapsid is a complex of protein C and mRNA. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E (By similarity).
SIMILARITY: Contains 1 helicase ATP-binding domain.
SIMILARITY: Contains 1 helicase C-terminal domain.
SIMILARITY: Contains 1 peptidase S7 domain [view classification].
SIMILARITY: Contains 1 RdRp catalytic domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M93130; AAA99437.1; -; Genomic_RNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A34774; GNWVD3.

3D structure databases

PDB

1UZG; X-ray; 3.50 A; A/B=281-672.	[ExPASy / RCSB / EBI]
2J7U; X-ray; 1.85 A; A=2762-3390.	[ExPASy / RCSB / EBI]
2J7W; X-ray; 2.60 A; A=2762-3390.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1UZG; -.
2J7U; -.
2J7W; -.

SMR

P27915; 1650-2092, 2497-2757, 2763-3373.

ModBase

P27915.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0019031;	Cellular component: viral envelope (inferred from electronic annotation from InterPro).
GO:0019013;	Cellular component: viral nucleocapsid (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0008026;	Molecular function: ATP-dependent helicase activity (inferred from electronic annotation from InterPro).
GO:0003725;	Molecular function: double-stranded RNA binding (inferred from electronic annotation from InterPro).
GO:0004482;	Molecular function: mRNA (guanine-N7-)-methyltransferase activity (inferred from electronic annotation from EC).
GO:0003724;	Molecular function: RNA helicase activity (inferred from electronic annotation from InterPro).
GO:0003968;	Molecular function: RNA-directed RNA polymerase activity (inferred from electronic annotation from InterPro).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0005198;	Molecular function: structural molecule activity (inferred from electronic annotation from InterPro).
GO:0016070;	Biological process: RNA metabolic process (inferred from electronic annotation from InterPro).
GO:0006410;	Biological process: transcription, RNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0019079;	Biological process: viral genome replication (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR014001; DEAD-like_N.
IPR011492; DEAD_Flavivir.
IPR001650; DNA/RNA_helicase_C.
IPR002464; DNA/RNA_helicase_DEAH_CS.
IPR011999; Flav_glyE_cen_dm.
IPR013754; Flav_glyE_dim.
IPR001122; Flavi_capsidC.
IPR000069; Flavi_M.
IPR001157; Flavi_NS1.
IPR000752; Flavi_NS2A.
IPR000487; Flavi_NS2B.
IPR000404; Flavi_NS4A.
IPR001528; Flavi_NS4B.
IPR002535; Flavi_propep.
IPR000336; Flv_glyE_Ig-like.
IPR014412; Gen_Poly_FLV.
IPR014021; Helicase_SF1/SF2_ATP-bd.
IPR001850; Peptidase_S7.
IPR000208; RNA_pol_flaviviral.
IPR007094; RNA_pol_PSvir.
IPR002877; RrmJFtsJ_MeTrfase.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.98.10; Flav_glyE_dim; 1.
G3DSA:2.60.40.350; Flv_glyE_Ig-like; 1.

Pfam

PF01003; Flavi_capsid; 1.
PF07652; Flavi_DEAD; 1.
PF02832; Flavi_glycop_C; 1.
PF00869; Flavi_glycoprot; 1.
PF01004; Flavi_M; 1.
PF00948; Flavi_NS1; 1.
PF01005; Flavi_NS2A; 1.
PF01002; Flavi_NS2B; 1.
PF01350; Flavi_NS4A; 1.
PF01349; Flavi_NS4B; 1.
PF00972; Flavi_NS5; 1.
PF01570; Flavi_propep; 1.
PF01728; FtsJ; 1.
PF00271; Helicase_C; 1.
PF00949; Peptidase_S7; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF003817; Gen_Poly_FLV; 1.

ProDom

PD001496; Flavi_NS1; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00487; DEXDc; 1.
SM00490; HELICc; 1.
SMART graphical view of domain structure.

PROSITE

PS00690; DEAH_ATP_HELICASE; FALSE_NEG.
PS51192; HELICASE_ATP_BIND_1; 1.
PS51194; HELICASE_CTER; 1.
PS50507; RDRP_SSRNA_POS; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; ATP-binding; Capsid protein; Cleavage on pair of basic residues; Complete proteome; Core protein; Direct protein sequencing; Envelope protein; Glycoprotein; Helicase; Hydrolase; Membrane; Nucleotide-binding; Nucleotidyltransferase; RNA replication; RNA-directed RNA polymerase; Transferase; Transmembrane; Virion.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 100`	`100`	`Protein C (By similarity).`	`PRO_0000037989`
`PROPEP`	`101 114`	`14`	`ER anchor for the protein C, removed in mature form by serine protease NS3 (By similarity).`	`PRO_0000037990`
`CHAIN`	`115 280`	`166`	`prM (By similarity).`	`PRO_0000308293`
`CHAIN`	`115 205`	`91`	`Peptide pr (By similarity).`	`PRO_0000308294`
`CHAIN`	`206 280`	`75`	`Small envelope protein M (By similarity).`	`PRO_0000037991`
`CHAIN`	`281 773`	`493`	`Envelope protein E (By similarity).`	`PRO_0000037992`
`CHAIN`	`774 1125`	`352`	`Non-structural protein 1 (By similarity).`	`PRO_0000037993`
`CHAIN`	`1126 1343`	`218`	`Non-structural protein 2A (By similarity).`	`PRO_0000037994`
`CHAIN`	`1126 1313`	`188`	`Non-structural protein 2A-alpha (By similarity).`	`PRO_0000308295`
`CHAIN`	`1344 1473`	`130`	`Serine protease subunit NS2B (By similarity).`	`PRO_0000037995`
`CHAIN`	`1474 2092`	`619`	`Serine protease subunit NS3 (By similarity).`	`PRO_0000037996`
`CHAIN`	`2093 2219`	`127`	`Non-structural protein 4A (By similarity).`	`PRO_0000037997`
`PEPTIDE`	`2220 2242`	`23`	`Peptide 2k (By similarity).`	`PRO_0000308296`
`CHAIN`	`2243 2490`	`248`	`Non-structural protein 4B (By similarity).`	`PRO_0000037998`
`CHAIN`	`2491 3390`	`900`	`RNA-directed RNA polymerase NS5 (By similarity).`	`PRO_0000037999`
`TOPO_DOM`	`1 101`	`101`	`Cytoplasmic (Potential).`
`TRANSMEM`	`102 122`	`21`	`Potential.`
`TOPO_DOM`	`123 238`	`116`	`Extracellular (Potential).`
`TRANSMEM`	`239 259`	`21`	`Potential.`
`TOPO_DOM`	`260 265`	`6`	`Cytoplasmic (Potential).`
`TRANSMEM`	`266 286`	`21`	`Potential.`
`TOPO_DOM`	`287 723`	`437`	`Extracellular (Potential).`
`TRANSMEM`	`724 744`	`21`	`Potential.`
`TOPO_DOM`	`745 750`	`6`	`Cytoplasmic (Potential).`
`TRANSMEM`	`751 771`	`21`	`Potential.`
`TOPO_DOM`	`772 1154`	`383`	`Extracellular (Potential).`
`TRANSMEM`	`1155 1175`	`21`	`Potential.`
`TOPO_DOM`	`1176 1445`	`270`	`Cytoplasmic (Potential).`
`TRANSMEM`	`1446 1466`	`21`	`Potential.`
`TOPO_DOM`	`1467 2191`	`725`	`Lumenal (Potential).`
`TRANSMEM`	`2192 2212`	`21`	`Potential.`
`TOPO_DOM`	`2213 2219`	`7`	`Cytoplasmic (Potential).`
`TRANSMEM`	`2220 2239`	`20`	`Potential.`
`TOPO_DOM`	`2240 2346`	`107`	`Lumenal (Potential).`
`TRANSMEM`	`2347 2367`	`21`	`Potential.`
`TOPO_DOM`	`2368 2412`	`45`	`Cytoplasmic (Potential).`
`TRANSMEM`	`2413 2433`	`21`	`Potential.`
`TOPO_DOM`	`2434 2458`	`25`	`Lumenal (Potential).`
`TRANSMEM`	`2459 2479`	`21`	`Potential.`
`TOPO_DOM`	`2480 3390`	`911`	`Cytoplasmic (Potential).`
`DOMAIN`	`1654 1810`	`157`	`Helicase ATP-binding.`
`DOMAIN`	`1820 1987`	`168`	`Helicase C-terminal.`
`DOMAIN`	`3018 3168`	`151`	`RdRp catalytic.`
`NP_BIND`	`1667 1674`	`8`	`ATP (Potential).`
`MOTIF`	`1758 1761`	`4`	`DEAH box (By similarity).`
`ACT_SITE`	`1524 1524`		`Charge relay system; for serine protease NS3 activity (By similarity).`
`ACT_SITE`	`1548 1548`		`Charge relay system; for serine protease NS3 activity (By similarity).`
`ACT_SITE`	`1608 1608`		`Charge relay system; for serine protease NS3 activity (By similarity).`
`SITE`	`100 101`	`2`	`Cleavage; by serine protease NS3 (By similarity).`
`SITE`	`114 115`	`2`	`Cleavage; by host signal peptidase (By similarity).`
`SITE`	`205 206`	`2`	`Cleavage; by host furin (By similarity).`
`SITE`	`280 281`	`2`	`Cleavage; by host signal peptidase (By similarity).`
`SITE`	`773 774`	`2`	`Cleavage; by host signal peptidase (By similarity).`
`SITE`	`1125 1126`	`2`	`Cleavage; by host (By similarity).`
`SITE`	`1313 1314`	`2`	`Cleavage; by serine protease NS3 (By similarity).`
`SITE`	`1343 1344`	`2`	`Cleavage; by serine protease NS3 (By similarity).`
`SITE`	`1473 1474`	`2`	`Cleavage; by serine protease NS3 (By similarity).`
`SITE`	`2092 2093`	`2`	`Cleavage; by serine protease NS3 (By similarity).`
`SITE`	`2219 2220`	`2`	`Cleavage; by host signal peptidase (By similarity).`
`SITE`	`2242 2243`	`2`	`Cleavage; by serine protease NS3 (By similarity).`
`SITE`	`2490 2491`	`2`	`Cleavage; by serine protease NS3 (By similarity).`
`CARBOHYD`	`183 183`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`347 347`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`433 433`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`903 903`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`980 980`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`1132 1132`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`1661 1661`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`2300 2300`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`2304 2304`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`2456 2456`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`283 310`		`By similarity.`
`DISULFID`	`340 401`		`By similarity.`
`DISULFID`	`354 385`		`By similarity.`
`DISULFID`	`372 396`		`By similarity.`
`DISULFID`	`463 563`		`By similarity.`
`DISULFID`	`580 611`		`By similarity.`
`TURN`	`282 285`	`4`
`STRAND`	`287 293`	`7`
`STRAND`	`301 305`	`5`
`STRAND`	`310 315`	`6`
`STRAND`	`318 327`	`10`
`STRAND`	`334 337`	`4`
`STRAND`	`343 351`	`9`
`HELIX`	`363 366`	`4`
`STRAND`	`368 379`	`12`
`TURN`	`381 384`	`4`
`STRAND`	`389 404`	`16`
`STRAND`	`406 409`	`4`
`STRAND`	`415 423`	`9`
`STRAND`	`434 436`	`3`
`STRAND`	`438 443`	`6`
`STRAND`	`448 453`