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P29838 (POLG_LANVY) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 5 chains:

  1. Capsid protein C
    Alternative name(s):
    Core protein
  2. prM
  3. Peptide pr
  4. Small envelope protein M
    Alternative name(s):
    Matrix protein
  5. Envelope protein E
OrganismLangat virus (strain Yelantsev)
Taxonomic identifier31639 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › tick-borne encephalitis virus group
Virus hostIxodida (ticks) [TaxID: 6935]
Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length776 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA By similarity.

prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated By similarity.

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.

Subcellular location

Capsid protein C: Virion Potential.

Peptide pr: Secreted By similarity.

Small envelope protein M: Virion membrane; Multi-pass membrane protein By similarity. Host endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

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

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins Peptide 2K acts as a signal sequence and is removed from the N-terminus of NS4B by the host signal peptidase in the ER lumen. Signal cleavage at the 2K-4B site requires a prior NS3 protease-mediated cleavage at the 4A-2K site By similarity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›776›776Genome polyprotein
PRO_0000405133
Chain1 – 9696Capsid protein C By similarity
PRO_0000037699
Propeptide97 – 11721ER anchor for the protein C, removed in mature form by serine protease NS3 By similarity
PRO_0000405134
Chain118 – 280163prM By similarity
PRO_0000405135
Chain118 – 20588Peptide pr By similarity
PRO_0000037700
Chain206 – 28075Small envelope protein M By similarity
PRO_0000037701
Chain281 – 776496Envelope protein E By similarity
PRO_0000037702

Regions

Topological domain1 – 9898Cytoplasmic Potential
Transmembrane99 – 11719Helical; Potential
Topological domain118 – 242125Extracellular Potential
Transmembrane243 – 26018Helical; Potential
Topological domain2611Cytoplasmic Potential
Transmembrane262 – 28019Helical; Potential
Topological domain281 – 727447Extracellular Potential
Intramembrane728 – 74821Helical; Potential
Topological domain749 – 7557Extracellular Potential
Intramembrane756 – 77621Helical; Potential
Region33 – 6836Hydrophobic; homodimerization of capsid protein C By similarity

Sites

Site96 – 972Cleavage; by viral protease NS3 Potential
Site117 – 1182Cleavage; by host signal peptidase By similarity
Site205 – 2062Cleavage; by host furin Potential
Site280 – 2812Cleavage; by host signal peptidase Potential

Amino acid modifications

Glycosylation1441N-linked (GlcNAc...); by host Potential
Glycosylation4341N-linked (GlcNAc...); by host Potential
Disulfide bond283 ↔ 310 By similarity
Disulfide bond340 ↔ 396 By similarity
Disulfide bond354 ↔ 385 By similarity
Disulfide bond372 ↔ 401 By similarity
Disulfide bond466 ↔ 570 By similarity
Disulfide bond587 ↔ 618 By similarity

Experimental info

Non-terminal residue7761

Secondary structure

1 ................. 776
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29838 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 5F7557E55A33BE3B

FASTA77684,537
        10         20         30         40         50         60 
MAGKAVLKGK GGGPPRRASK VAPKKTRQLR VQMPNGLVLM RMLGVLWHAL TGTARSPVLK 

        70         80         90        100        110        120 
AFWKVVPLKQ ATLALRKIKR TVSTLMVGLH RRGSRRTTID WMTPLLITVM LGMCLTATVR 

       130        140        150        160        170        180 
RERDGSMVIR AEGRDAATQV RVENGTCVIL ATDMGSWCDD SLAYECVTID QGEEPVDVDC 

       190        200        210        220        230        240 
FCRGVEKVTL EYGRCGRREG SRSRRSVLIP SHAQRDLTGR GHQWLEGEAV KAHLTRVEGW 

       250        260        270        280        290        300 
VWKNKLFTLS LVMVAWLMVD GLLPRILIVV VALALVPAYA SRCTHLENRD FVTGVQGTTR 

       310        320        330        340        350        360 
LTLVLELGGC VTVTADGKPS LDVWLDSIYQ ESPAQTREYC LHAKLTGTKV AARCPTMGPA 

       370        380        390        400        410        420 
TLPEEHQSGT VCKRDQSDRG WGNHCGLFGK GSIVTCVKFT CEDKKKATGH VYDVNKITYT 

       430        440        450        460        470        480 
IKVEPHTGEF VAANETHSGR KSASFTVSSE KTILTLGDYG DVSLLCRVAS GVDLAQTVVL 

       490        500        510        520        530        540 
ALDKTHEHLP TAWQVHRDWF NDLALPWKHD GAEAWNEAGR LVEFGTPHAV KMDVFNLGDQ 

       550        560        570        580        590        600 
TGVLLKSLAG VPVASIEGTK YHLKSGHVTC EVGLEKLKMK GLTYTVCDKT KFTWKRAPTD 

       610        620        630        640        650        660 
SGHDTVVMEV GFSGTRPCRI PVRAVAHGVP EVNVAMLITP NPTMENNGGG FIEMQLPPGD 

       670        680        690        700        710        720 
NIIYVGDLNH QWFQKGSSIG RVLQKTRKGI ERLTVLGEHA WDFGSVGGVM TSIGRAMHTV 

       730        740        750        760        770 
LGGAFNTLLG GVGFLPKILL GVAMAWLGLN MRNPTLSMGF LLSGGLVLAM TLGVGA

« Hide

References

[1]"Sequence of the genes encoding the structural proteins of the low-virulence tick-borne flaviviruses Langat TP21 and Yelantsev."
Mandl C.W., Iacono-Connors L.C., Wallner G., Holzmann H., Kunz C., Heinz F.X.
Virology 185:891-895(1991) [PubMed: 1720591] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"NMR solution structure and backbone dynamics of domain III of the E protein of tick-borne Langat flavivirus suggests a potential site for molecular recognition."
Mukherjee M., Dutta K., White M.A., Cowburn D., Fox R.O.
Protein Sci. 15:1342-1355(2006) [PubMed: 16731969] [Abstract]
Cited for: STRUCTURE BY NMR OF 580-675.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M73835 Unassigned RNA. Translation: AAA02740.1.
PIRA41704.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z66NMR-A580-675[»]
ProteinModelPortalP29838.
SMRP29838. Positions 281-675.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000069. Env_glycoprot_M_flavivir.
IPR013755. Flav_glyE_cen_dom_subdom1.
IPR013756. Flav_glyE_cen_dom_subdom2.
IPR013754. Flav_glyE_dim.
IPR001122. Flavi_capsidC.
IPR002535. Flavi_propep.
IPR000336. Flv_glyE_Ig-like.
IPR011999. GlycoprotE_cen/dimer_Flavivir.
IPR011998. GlycoprotE_cen/dimer_vir.
IPR014756. Ig_E-set.
[Graphical view]
Gene3DG3DSA:3.30.387.10. Flav_glyE_cen_1. 1 hit.
G3DSA:3.30.67.10. Flav_glyE_cen_2. 1 hit.
G3DSA:2.60.98.10. Flav_glyE_dim. 1 hit.
G3DSA:2.60.40.350. Flv_glyE_Ig-like. 1 hit.
PfamPF01003. Flavi_capsid. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF01570. Flavi_propep. 1 hit.
[Graphical view]
SUPFAMSSF56983. Flavi_glycoprotE. 1 hit.
SSF81296. Ig_E-set. 1 hit.
ProtoNetSearch...

Entry information

Entry namePOLG_LANVY
AccessionPrimary (citable) accession number: P29838
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1996
Last modified: September 21, 2011
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents