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Q5XXP3 (POLS_CHIK3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural polyprotein
Alternative name(s):
p130

Cleaved into the following 6 chains:

  1. Capsid protein
    EC=3.4.21.90
    Alternative name(s):
    Coat protein
    Short name=C
  2. p62
    Alternative name(s):
    E3/E2
  3. E3 protein
    Alternative name(s):
    Spike glycoprotein E3
  4. E2 envelope glycoprotein
    Alternative name(s):
    Spike glycoprotein E2
  5. 6K protein
  6. E1 envelope glycoprotein
    Alternative name(s):
    Spike glycoprotein E1
OrganismChikungunya virus (strain 37997) (CHIKV) [Complete proteome]
Taxonomic identifier371095 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirusSFV complex
Virus hostAedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159]
Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) [TaxID: 7160]
Aedes furcifer (Mosquito) [TaxID: 299627]
Aedes polynesiensis (Polynesian tiger mosquito) [TaxID: 188700]
Cercopithecus [TaxID: 9533]
Homo sapiens (Human) [TaxID: 9606]
Macaca (macaques) [TaxID: 9539]
Pan troglodytes (Chimpanzee) [TaxID: 9598]
Papio (baboons) [TaxID: 9554]
Presbytis [TaxID: 9573]

Protein attributes

Sequence length1248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Capsid protein possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein. Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosaedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. New virions attach to target cells, and after endocytosis their membrane fuses with the target cell membrane. This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible. The uncoating might be triggered by the interaction of capsid proteins with ribosomes. Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding By similarity.

E3 protein's function is unknown By similarity.

E2 is responsible for viral attachment to target host cell, by binding to the cell receptor. Synthesized as a p62 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The p62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. p62 is processed at the last step, presumably to avoid E1 fusion activation before its final export to cell surface. E2 C-terminus contains a transitory transmembrane that would be disrupted by palmitoylation, resulting in reorientation of the C-terminal tail from lumenal to cytoplasmic side. This step is critical since E2 C-terminus is involved in budding by interacting with capsid proteins. This release of E2 C-terminus in cytoplasm occurs lately in protein export, and precludes premature assembly of particles at the endoplasmic reticulum membrane By similarity.

6K is a constitutive membrane protein involved in virus glycoprotein processing, cell permeabilization, and the budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level. This leads to cytoplasmic calcium elevation. Because of its lipophilic properties, the 6K protein is postulated to influence the selection of lipids that interact with the transmembrane domains of the glycoproteins, which, in turn, affects the deformability of the bilayer required for the extreme curvature that occurs as budding proceeds. Present in low amount in virions, about 3% compared to viral glycoproteins By similarity.

E1 is a class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits. This E1 trimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. Efficient fusion requires the presence of cholesterol and sphingolipid in the target membrane By similarity.

Catalytic activity

Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.

Subunit structure

p62 and E1 form a heterodimer shortly after synthesis. Processing of p62 into E2 and E3 results in a heterodimer of E2 and E1. Spike at virion surface are constituted of three E2-E1 heterodimers. After target cell attachment and endocytosis, E1 change conformation to form homotrimers By similarity.

Subcellular location

Capsid protein: Virion By similarity. Host cytoplasm By similarity.

p62: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity.

E2 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity.

E1 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity.

6K protein: Host cell membrane; Multi-pass membrane protein By similarity. Virion membrane; Multi-pass membrane protein By similarity.

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking p62 signal peptide. The remaining polyprotein is then targeted to the endoplasmic reticulum, where host signal peptidase cleaves it into p62, 6K and E1 proteins. p62 is further processed to mature E3 and E2 by host furin in trans-Golgi vesicle By similarity.

E2 is palmitoylated via thioester bonds. These palmitoylations may induce disruption of the C-terminus transmembrane. This would result in the reorientation of E2 c-terminus from lumenal to cytoplasmic side. 6K protein is also palmitoylated. E1 is stearoylated By similarity.

Miscellaneous

Structural polyprotein is translated from a subgenomic RNA synthesized during togavirus replication.

Sequence similarities

Contains 1 peptidase S3 domain.

Ontologies

Keywords
   Biological processFusion of virus membrane with host endosomal membrane
Fusion of virus membrane with host membrane
Host-virus interaction
Viral attachment to host cell
Viral penetration into host cytoplasm
Virus entry into host cell
   Cellular componentCapsid protein
Host cell membrane
Host cytoplasm
Host membrane
Membrane
T=4 icosahedral capsid protein
Virion
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processfusion of virus membrane with host endosome membrane

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentT=4 icosahedral viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

host cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261Capsid protein By similarity
PRO_0000226225
Chain262 – 748487p62 By similarity
PRO_0000226226
Chain262 – 32564E3 protein By similarity
PRO_0000226227
Signal peptide262 – 27514Not cleaved Potential
Chain326 – 748423E2 envelope glycoprotein By similarity
PRO_0000226228
Chain749 – 809616K protein By similarity
PRO_0000226229
Chain810 – 1248439E1 envelope glycoprotein By similarity
PRO_0000226230

Regions

Topological domain1 – 692692Extracellular Potential
Transmembrane693 – 71321Helical; Potential
Topological domain714 – 74835Cytoplasmic Potential
Topological domain749 – 76315Extracellular Potential
Transmembrane764 – 78421Helical; Potential
Topological domain785 – 79511Cytoplasmic Potential
Transmembrane796 – 81621Helical; Potential
Topological domain817 – 1224408Extracellular Potential
Transmembrane1225 – 124521Helical; Potential
Topological domain1246 – 12483Cytoplasmic Potential
Domain113 – 261149Peptidase S3
Region1 – 107107Intrinsically disordered, in contact with genomic RNA in nucleocapsid Potential
Region88 – 10013Ribosome-binding By similarity
Region721 – 74121Transient transmembrane before p62-6K protein processing Potential
Region893 – 91018E1 fusion peptide loop By similarity

Sites

Active site1391Charge relay system By similarity
Active site1451Charge relay system By similarity
Active site2131Charge relay system By similarity
Site261 – 2622Cleavage; by capsid protein By similarity
Site325 – 3262Cleavage; by host furin By similarity
Site748 – 7492Cleavage; by host signal peptidase By similarity
Site809 – 8102Cleavage; by host signal peptidase By similarity

Amino acid modifications

Lipidation7211S-palmitoyl cysteine; by host By similarity
Lipidation7411S-palmitoyl cysteine; by host By similarity
Lipidation7421S-palmitoyl cysteine; by host By similarity
Lipidation12421S-stearoyl cysteine; by host By similarity
Glycosylation2731N-linked (GlcNAc...); by host Potential
Glycosylation5881N-linked (GlcNAc...); by host Potential
Glycosylation6701N-linked (GlcNAc...); by host Potential
Glycosylation9501N-linked (GlcNAc...); by host Potential
Disulfide bond113 ↔ 128 By similarity
Disulfide bond858 ↔ 923 By similarity
Disulfide bond871 ↔ 903 By similarity
Disulfide bond872 ↔ 905 By similarity
Disulfide bond877 ↔ 887 By similarity
Disulfide bond1068 ↔ 1080 By similarity
Disulfide bond1110 ↔ 1185 By similarity
Disulfide bond1115 ↔ 1189 By similarity
Disulfide bond1137 ↔ 1179 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5XXP3 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: A19160F7E5ED521E

FASTA1,248138,071
        10         20         30         40         50         60 
MEFIPTQTFY NRRYQPRPWA PRPTIQVIRP RPRPQRQAGQ LAQLISAVNK LTMRAVPQQK 

        70         80         90        100        110        120 
PRRNRKNKKQ RQKKQAPQND PKQKKQPPQK KPAQKKKKPG RRERMCMKIE NDCIFEVKHE 

       130        140        150        160        170        180 
GKVMGYACLV GDKVMKPAHV KGTIDNADLA KLAFKRSSKY DLECAQIPVH MKSDASKFTH 

       190        200        210        220        230        240 
EKPEGYYNWH HGAVQYSGGR FTIPTGAGKP GDSGRPIFDN KGRVVAIVLG GANEGARTAL 

       250        260        270        280        290        300 
SVVTWNKDIV TKITPEGAEE WSLALPVLCL LANTTFPCSQ PPCTPCCYEK EPESTLRMLE 

       310        320        330        340        350        360 
DNVMRPGYYQ LLKASLTCSP HRQRRSTKDN FNVYKATRPY LAHCPDCGEG HSCHSPIALE 

       370        380        390        400        410        420 
RIRNEATDGT LKIQVSLQIG IKTDDSHDWT KLRYMDSHTP ADAERAGLLV RTSAPCTITG 

       430        440        450        460        470        480 
TMGHFILARC PKGETLTVGF TDSRKISHTC THPFHHEPPV IGRERFHSRP QHGKELPCST 

       490        500        510        520        530        540 
YVQSTAATAE EIEVHMPPDT PDRTLMTQQS GNVKITVNGQ TVRYKCNCGG SNEGLTTTDK 

       550        560        570        580        590        600 
VINNCKIDQC HAAVTNHKNW QYNSPLVPRN AELGDRKGKI HIPFPLANVT CRVPKARNPT 

       610        620        630        640        650        660 
VTYGKNQVTM LLYPDHPTLL SYRNMGQEPN YHEEWVTHKK EVTLTVPTEG LEVTWGNNEP 

       670        680        690        700        710        720 
YKYWPQMSTN GTAHGHPHEI ILYYYELYPT MTVVIVSVAS FVLLSMVGTA VGMCVCARRR 

       730        740        750        760        770        780 
CITPYELTPG ATVPFLLSLL CCVRTTKAAT YYEAAAYLWN EQQPLFWLQA LIPLAALIVL 

       790        800        810        820        830        840 
CNCLKLLPCC CKTLAFLAVM SIGAHTVSAY EHVTVIPNTV GVPYKTLVNR PGYSPMVLEM 

       850        860        870        880        890        900 
ELQSVTLEPT LSLDYITCEY KTVIPSPYVK CCGTAECKDK SLPDYSCKVF TGVYPFMWGG 

       910        920        930        940        950        960 
AYCFCDAENT QLSEAHVEKS ESCKTEFASA YRAHTASASA KLRVLYQGNN ITVAAYANGD 

       970        980        990       1000       1010       1020 
HAVTVKDAKF VVGPMSSAWT PFDNKIVVYK GDVYNMDYPP FGAGRPGQFG DIQSRTPESK 

      1030       1040       1050       1060       1070       1080 
DVYANTQLVL QRPAAGTVHV PYSQAPSGFK YWLKERGASL QHTAPFGCQI ATNPVRAVNC 

      1090       1100       1110       1120       1130       1140 
AVGNIPISID IPDAAFTRVV DAPSVTDMSC EVPACTHSSD FGGVAIIKYT ASKKGKCAVH 

      1150       1160       1170       1180       1190       1200 
SMTNAVTIRE ADVEVEGNSQ LQISFSTALA SAEFRVQVCS TQVHCAAACH PPKDHIVNYP 

      1210       1220       1230       1240 
ASHTTLGVQD ISTTAMSWVQ KITGGVGLIV AVAALILIVV LCVSFSRH 

« Hide

References

[1]"Differential infectivities of O'Nyong-Nyong and Chikungunya virus isolates in Anopheles gambiae and Aedes aegypti mosquitoes."
Vanlandingham D.L., Hong C., Klingler K., Tsetsarkin K., McElroy K.L., Powers A.M., Lehane M.J., Higgs S.
Am. J. Trop. Med. Hyg. 72:616-621(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY726732 Genomic RNA. Translation: AAU43881.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J2Welectron microscopy5.00E/F/G/H1203-1248[»]
I/J/K/L113-261[»]
M/N/O/P332-666[»]
Q/R/S/T668-748[»]
ProteinModelPortalQ5XXP3.
SMRQ5XXP3. Positions 113-261, 810-1199.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.350. 1 hit.
2.60.98.10. 3 hits.
InterProIPR002548. Alpha_E1_glycop.
IPR000936. Alpha_E2_glycop.
IPR002533. Alpha_E3_glycop.
IPR000336. Flavivir/Alphavir_Ig-like.
IPR011998. Glycoprot_cen/dimer.
IPR013754. GlyE_dim.
IPR014756. Ig_E-set.
IPR000930. Peptidase_S3.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF01589. Alpha_E1_glycop. 1 hit.
PF00943. Alpha_E2_glycop. 1 hit.
PF01563. Alpha_E3_glycop. 1 hit.
PF00944. Peptidase_S3. 1 hit.
[Graphical view]
PRINTSPR00798. TOGAVIRIN.
SUPFAMSSF50494. SSF50494. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS51690. ALPHAVIRUS_CP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLS_CHIK3
AccessionPrimary (citable) accession number: Q5XXP3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 23, 2004
Last modified: February 19, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references