Skip Header

Contribute Send feedback
Read comments (?) or add your own

P27914 (POLG_DEN2T) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 5 chains:

  1. Envelope protein E
  2. Non-structural protein 1
    Short name=NS1
  3. Non-structural protein 2A
    Short name=NS2A
  4. Non-structural protein 2A-alpha
    Short name=NS2A-alpha
  5. Serine protease NS3
    EC=3.4.21.91
    EC=3.6.1.15
    EC=3.6.4.13
    Alternative name(s):
    Non-structural protein 3
OrganismDengue virus type 2 (strain Tonga/EKB194/1974) (DENV-2)
Taxonomic identifier11067 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaeFlavivirusDengue virus group
Virus hostErythrocebus patas (Red guenon) (Cercopithecus patas) [TaxID: 9538]
Homo sapiens (Human) [TaxID: 9606]
Diceromyia [TaxID: 53539]
Aedimorphus [TaxID: 53540]
Stegomyia [TaxID: 53541]

Protein attributes

Sequence length1683 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as an homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes By similarity.

Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome By similarity.

Non-structural protein 2A may be involved viral RNA replication and capsid assembly Potential.

Non-structural protein 2B is a required cofactor for the serine protease function of NS3 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 By similarity.

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.

NTP + H2O = NDP + phosphate.

ATP + H2O = ADP + phosphate.

Subunit structure

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. NS1 forms homodimers as well as homohexamers when secreted. NS1 may interact with NS4A. NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter, acting as a cofactor. In the absence of the NS2B, NS3 protease is unfolded and inactive By similarity.

Subcellular location

Envelope protein E: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Non-structural protein 1: Secreted. Host endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity.

Non-structural protein 2A-alpha: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein Potential.

Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Remains non-covalently associated to NS3 protease By similarity.

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins By similarity.

Sequence similarities

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 peptidase S7 domain.

Ontologies

Keywords
   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
Initiation of viral infection
Viral attachment to host cell
Viral penetration into host cytoplasm
Virus endocytosis by host
   Cellular componentHost endoplasmic reticulum
Host membrane
Membrane
Secreted
Viral envelope protein
Virion
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
Viral nucleoprotein
   Molecular functionCapsid protein
Hydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processinterspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

viral genome replication

Inferred from electronic annotation. Source: InterPro

   Cellular componenthost cell endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: InterPro

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

double-stranded RNA binding

Inferred from electronic annotation. Source: InterPro

serine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›1683›1683Genome polyprotein
PRO_0000405219
Chain1 – 495495Envelope protein E By similarity
PRO_0000037980
Chain496 – 847352Non-structural protein 1 By similarity
PRO_0000037981
Chain848 – 1065218Non-structural protein 2A By similarity
PRO_0000308290
Chain848 – 1035188Non-structural protein 2A-alpha By similarity
PRO_0000037982
Chain1066 – 1683618Serine protease NS3 By similarity
PRO_0000037983

Regions

Topological domain‹1 – 445›445Extracellular Potential
Intramembrane446 – 46621Helical; Potential
Topological domain467 – 4726Extracellular Potential
Intramembrane473 – 49321Helical; Potential
Topological domain494 – 844351Extracellular Potential
Transmembrane845 – 86521Helical; Potential
Topological domain866 – 87611Cytoplasmic Potential
Transmembrane877 – 89721Helical; Potential
Topological domain898 – 9025Lumenal Potential
Transmembrane903 – 92321Helical; Potential
Topological domain924 – 99168Cytoplasmic Potential
Transmembrane992 – 101221Helical; Potential
Topological domain1013 – 103725Lumenal Potential
Transmembrane1038 – 105821Helical; Potential
Topological domain1059 – ›1683›625Cytoplasmic Potential
Domain1066 – 1243178Peptidase S7
Domain1245 – 1401157Helicase ATP-binding
Domain1411 – 1582172Helicase C-terminal
Nucleotide binding1258 – 12658ATP Potential
Motif1349 – 13524DEAH box

Sites

Active site11161Charge relay system; for serine protease NS3 activity By similarity
Active site11401Charge relay system; for serine protease NS3 activity By similarity
Active site12001Charge relay system; for serine protease NS3 activity By similarity
Site495 – 4962Cleavage; by host signal peptidase Potential

Amino acid modifications

Glycosylation671N-linked (GlcNAc...); by host Potential
Glycosylation1531N-linked (GlcNAc...); by host Potential
Disulfide bond3 ↔ 30 By similarity
Disulfide bond60 ↔ 121 By similarity
Disulfide bond74 ↔ 105 By similarity
Disulfide bond92 ↔ 116 By similarity
Disulfide bond185 ↔ 285 By similarity
Disulfide bond302 ↔ 333 By similarity

Experimental info

Non-adjacent residues1065 – 10662
Non-terminal residue11
Non-terminal residue16831

Secondary structure

........................................................................ 1683
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27914 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 3B0438D96196BFC8

FASTA1,683187,440
        10         20         30         40         50         60 
MRCIGISNRD FVEGVSGGSW VDIVLEHGSC VTTMAKNKPT LDFELIKTEA KQPATLRKYC 

        70         80         90        100        110        120 
IEAKLTNTTT DSRCPTQGEP TLNEEQDKRF VCKHSMVDRG WGNGCGLFGK GGIVTCAMFT 

       130        140        150        160        170        180 
CKKNMEGKIV QPENLEYTVV ITPHSGEEHA VGNDTGKHGK EVKITPQSSI TEAELTGYGT 

       190        200        210        220        230        240 
VTMECSPRTG LDFNEMVLLQ MEDKAWLVHR QWFLDLPLPW LPGADTQGSN WIQKETLVTF 

       250        260        270        280        290        300 
KNPHAKKQDV VVLGSQEGAM HTALTGATEI QMSSGNLLFT GHLKCRLRMD KLQLKGMSYS 

       310        320        330        340        350        360 
MCTGKFKIVK EIAETQHGTI VIRVQYEGDG SPCKIPFEIM DLEKRHVLGR LITVNPIVTE 

       370        380        390        400        410        420 
KDSPVNIEAE PPFGDSYIII GVEPGQLKLD WFKKGSSIGQ MFETTMRGAK RMAILGDTAW 

       430        440        450        460        470        480 
DFGSLGGVFT SIGKALHQVF GAIYGAAFSG VSWTMKILIG VIITWIGMNS RSTSLSVSLV 

       490        500        510        520        530        540 
LVGIVTLYLG VMVQADSGCV VSWKNKELKC GSGIFVTDNV HTWTEQYKFQ PESPSKLASA 

       550        560        570        580        590        600 
IQKAHEEGIC GIRSVTRLEN LMWKQITSEL NHILSENEVK LTIMTGDIKG IMQVGKRSLR 

       610        620        630        640        650        660 
PQPTELRYSW KTWGKAKMLS TELHNQTFLI DGPETAECPN TNRAWNSLEV EDYGFGVFTT 

       670        680        690        700        710        720 
NIWLRLREKQ DVFCDSKLMS AAIKDNRAVH ADMGYWIESA LNDTWKIEKA SFIEVKSCHW 

       730        740        750        760        770        780 
PKSHTLWSNG VLESEMVIPK NFAGPVSQHN NRPGYYTQTA GPWHLGKLEM DFDFCEGTTV 

       790        800        810        820        830        840 
VVTEDCGNRG PSLRTTTASG KLITEWCCRS CTLPPLRYRG EDGCWYGMEI RPLKEKEENL 

       850        860        870        880        890        900 
VSSLVTAGHG QIDNFSLGIL GMALFLEEML RTRVGTKHAI LLVAVSFVTL ITGNMSFRDL 

       910        920        930        940        950        960 
GRVMVMVGAT MTDDIGMGVT YLALLAAFRV RPTFAAGLLL RKLTSKELMM TTIGIVLLSQ 

       970        980        990       1000       1010       1020 
SSIPETILEL TDALALGMMV LKMVRNMEKY QLAVTIMAIL CVPNAVILQN AWKVSCTILA 

      1030       1040       1050       1060       1070       1080 
VVSVSPLLLT SSQQKADWIP LALTIKGLNP TAIFLTTLSR TSKKRAGVLW DVPSPPPVGK 

      1090       1100       1110       1120       1130       1140 
AELEDGAYRI KQKGILGYSQ IGAGVYKEGT FHTMWHVTRG AVLMHKGKRI EPSWADVKKD 

      1150       1160       1170       1180       1190       1200 
LISYGGGWKL EGEWKEGEEV QVLALEPGKN PRAVQTKPGL FRTNTGTIGA VSLDFSPGTS 

      1210       1220       1230       1240       1250       1260 
GSPIVDKKGK VVGLYGNGVV TRSGAYVSAI AQTEKSIEDN PEIEDDIFRK RRLTIMDLHP 

      1270       1280       1290       1300       1310       1320 
GAGKTKRYLP AIVREAIKRG LRTLILAPTR VVAAEMEEAL RGLPIRYQTP AIRAEHTGRE 

      1330       1340       1350       1360       1370       1380 
IVDLMCHATF TMRLLSPIRV PNYNLIIMDE AHFTDPASIA ARGYISTRVE MGEAAGIFMT 

      1390       1400       1410       1420       1430       1440 
ATPPGSRDPF PQSNAPIMDE EREIPERSWN SGHEWVTDFK GKTVWFVPSI KTGNDIAACL 

      1450       1460       1470       1480       1490       1500 
RKNGKRVIQL SRKTFDSEYV KTRTNDWDFV VTTDISEMGA NFKAERVIDP RRCMKPVILT 

      1510       1520       1530       1540       1550       1560 
DGEERVILAG PMPVTHSSAA QRRGRIGRNP RNENDQYIYM GEPLENDEDC AHWKEAKMLL 

      1570       1580       1590       1600       1610       1620 
DNINTPEGII PSIFEPEREK VDAIDGEYRL RGEARKTFVD LMRRGDLPVW LAYKVAAEGI 

      1630       1640       1650       1660       1670       1680 
NYADRRWCFD GTRNNQILEE NVEVEIWTKE GERKKLKPRW LDARIYSDPL ALKEFKEFAA 


GRK 

« Hide

References

[1]"Nucleotide sequence of the envelope glycoprotein gene of a dengue-2 virus isolated during an epidemic of benign dengue fever in Tonga in 1974."
Chen W., Maguire T.
Nucleic Acids Res. 18:5889-5889(1990) [PubMed: 2216784] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-495.
[2]Qu X., Chen W., Maguire T.
Submitted (MAR-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 496-1683.
[3]"Conformational changes of the flavivirus E glycoprotein."
Zhang Y., Zhang W., Ogata S., Clements D., Strauss J.H., Baker T.S., Kuhn R.J., Rossmann M.G.
Structure 12:1607-1618(2004) [PubMed: 15341726] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (12.5 ANGSTROMS) OF 1-395, X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 1-395.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54319 Genomic RNA. Translation: CAA38217.1.
X57469 Genomic RNA. Translation: CAA40705.1.
X57468 Genomic RNA. Translation: CAA40704.1.
PIRPQ0507.
S11482.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TG8X-ray2.61A1-395[»]
1TGEelectron microscopy12.50A/B/C1-395[»]
ProteinModelPortalP27914.
SMRP27914. Positions 1-394, 1085-1683.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR014001. DEAD-like_helicase.
IPR011492. DEAD_Flavivir.
IPR013756. Flav_glyE_cen_dom_subdom2.
IPR013754. Flav_glyE_dim.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000336. Flv_glyE_Ig-like.
IPR011999. GlycoprotE_cen/dimer_Flavivir.
IPR011998. GlycoprotE_cen/dimer_vir.
IPR001650. Helicase_C.
IPR014756. Ig_E-set.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR001850. Peptidase_S7.
[Graphical view]
Gene3DG3DSA:3.30.67.10. Flav_glyE_cen_2. 1 hit.
G3DSA:2.60.98.10. Flav_glyE_dim. 3 hits.
G3DSA:2.60.40.350. Flv_glyE_Ig-like. 1 hit.
PfamPF07652. Flavi_DEAD. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF56983. Flavi_glycoprotE. 1 hit.
SSF81296. Ig_E-set. 1 hit.
SSF50494. Pept_Ser_Cys. 1 hit.
PROSITEPS00690. DEAH_ATP_HELICASE. False negative.
PS51528. FLAVIVIRUS_NS3PRO. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLG_DEN2T
AccessionPrimary (citable) accession number: P27914
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 16, 2011
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families