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Q8JUX5

- POLS_CHIKS

UniProt

Q8JUX5 - POLS_CHIKS

Protein

Structural polyprotein

Gene
N/A
Organism
Chikungunya virus (strain S27-African prototype) (CHIKV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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.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.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.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.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei139 – 1391Charge relay systemPROSITE-ProRule annotation
    Active sitei145 – 1451Charge relay systemPROSITE-ProRule annotation
    Active sitei213 – 2131Charge relay systemPROSITE-ProRule annotation
    Sitei261 – 2622Cleavage; by capsid proteinBy similarity
    Sitei325 – 3262Cleavage; by host furinBy similarity
    Sitei748 – 7492Cleavage; by host signal peptidaseBy similarity
    Sitei809 – 8102Cleavage; by host signal peptidaseBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro
    2. structural molecule activity Source: InterPro

    GO - Biological processi

    1. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
    2. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Fusion 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

    Protein family/group databases

    MEROPSiS03.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Structural polyprotein
    Alternative name(s):
    p130
    Cleaved into the following 6 chains:
    Alternative name(s):
    Coat protein
    Short name:
    C
    Alternative name(s):
    E3/E2
    Alternative name(s):
    Spike glycoprotein E3
    Alternative name(s):
    Spike glycoprotein E2
    Alternative name(s):
    Spike glycoprotein E1
    OrganismiChikungunya virus (strain S27-African prototype) (CHIKV)
    Taxonomic identifieri371094 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirusSFV complex
    Virus hostiAedes 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]
    ProteomesiUP000000569: Genome

    Subcellular locationi

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

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell
    2. host cell plasma membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. T=4 icosahedral viral capsid Source: UniProtKB-KW
    5. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Capsid protein, Host cell membrane, Host cytoplasm, Host membrane, Membrane, T=4 icosahedral capsid protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261Capsid proteinBy similarityPRO_0000226219Add
    BLAST
    Chaini262 – 748487p62By similarityPRO_0000226220Add
    BLAST
    Chaini262 – 32564E3 proteinBy similarityPRO_0000226221Add
    BLAST
    Signal peptidei262 – 27514Not cleavedSequence AnalysisAdd
    BLAST
    Chaini326 – 748423E2 envelope glycoproteinBy similarityPRO_0000226222Add
    BLAST
    Chaini749 – 809616K proteinBy similarityPRO_0000226223Add
    BLAST
    Chaini810 – 1248439E1 envelope glycoproteinBy similarityPRO_0000226224Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi113 ↔ 128By similarity
    Glycosylationi273 – 2731N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi588 – 5881N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi670 – 6701N-linked (GlcNAc...); by hostSequence Analysis
    Lipidationi721 – 7211S-palmitoyl cysteine; by hostBy similarity
    Lipidationi741 – 7411S-palmitoyl cysteine; by hostBy similarity
    Lipidationi742 – 7421S-palmitoyl cysteine; by hostBy similarity
    Disulfide bondi858 ↔ 923By similarity
    Disulfide bondi871 ↔ 903By similarity
    Disulfide bondi872 ↔ 905By similarity
    Disulfide bondi877 ↔ 887By similarity
    Glycosylationi950 – 9501N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi1068 ↔ 1080By similarity
    Disulfide bondi1110 ↔ 1185By similarity
    Disulfide bondi1115 ↔ 1189By similarity
    Disulfide bondi1137 ↔ 1179By similarity
    Lipidationi1242 – 12421S-stearoyl cysteine; by hostBy similarity

    Post-translational modificationi

    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.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.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

    Interactioni

    Subunit structurei

    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.By similarity

    Structurei

    Secondary structure

    1
    1248
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi895 – 8995
    Turni904 – 9074

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RSWNMR-A893-910[»]
    ProteinModelPortaliQ8JUX5.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini262 – 692431ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini714 – 74835CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini749 – 76315ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini785 – 79511CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini817 – 1224408ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1246 – 12483CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei693 – 71321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei764 – 78421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei796 – 81621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1225 – 124521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini113 – 261149Peptidase S3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 107107Intrinsically disordered, in contact with genomic RNA in nucleocapsidSequence AnalysisAdd
    BLAST
    Regioni91 – 10010Ribosome-bindingBy similarity
    Regioni721 – 74121Transient transmembrane before p62-6K protein processingSequence AnalysisAdd
    BLAST
    Regioni893 – 91018E1 fusion peptide loopBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi60 – 9839Lys-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 peptidase S3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di2.60.40.350. 1 hit.
    2.60.98.10. 3 hits.
    InterProiIPR002548. 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]
    PfamiPF01589. Alpha_E1_glycop. 1 hit.
    PF00943. Alpha_E2_glycop. 1 hit.
    PF01563. Alpha_E3_glycop. 1 hit.
    PF00944. Peptidase_S3. 1 hit.
    [Graphical view]
    PRINTSiPR00798. TOGAVIRIN.
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF56983. SSF56983. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS51690. ALPHAVIRUS_CP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8JUX5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEFIPTQTFY NRRYQPRPWT PRPTIQVIRP RPRPQRQAGQ LAQLISAVNK     50
    LTMRAVPQQK PRRNRKNKKQ KQKQQAPQNN TNQKKQPPKK KPAQKKKKPG 100
    RRERMCMKIE NDCIFEVKHE GKVTGYACLV GDKVMKPAHV KGTIDNADLA 150
    KLAFKRSSKY DLECAQIPVH MKSDASKFTH EKPEGYYNWH HGAVQYSGGR 200
    FTIPTGAGKP GDSGRPIFDN KGRVVAIVLG GANEGARTAL SVVTWNKDIV 250
    TKITPEGAEE WSLAIPVMCL LANTTFPCSQ PPCIPCCYEK EPEETLRMLE 300
    DNVMRPGYYQ LLQASLTCSP HRQRRSTKDN FNVYKATRPY LAHCPDCGEG 350
    HSCHSPVALE RIRNEATDGT LKIQVSLQIG IGTDDSHDWT KLRYMDNHIP 400
    ADAGRAGLFV RTSAPCTITG TMGHFILARC PKGETLTVGF TDSRKISHSC 450
    THPFHHDPPV IGREKFHSRP QHGKELPCST YVQSNAATAE EIEVHMPPDT 500
    PDRTLLSQQS GNVKITVNGR TVRYKCNCGG SNEGLITTDK VINNCKVDQC 550
    HAAVTNHKKW QYNSPLVPRN AELGDRKGKI HIPFPLANVT CMVPKARNPT 600
    VTYGKNQVIM LLYPDHPTLL SYRSMGEEPN YQEEWVTHKK EVVLTVPTEG 650
    LEVTWGNNEP YKYWPQLSAN GTAHGHPHEI ILYYYELYPT MTVVVVSVAS 700
    FILLSMVGMA VGMCMCARRR CITPYELTPG ATVPFLLSLI CCIRTAKAAT 750
    YQEAAVYLWN EQQPLFWLQA LIPLAALIVL CNCLRLLPCC CKTLAFLAVM 800
    SIGAHTVSAY EHVTVIPNTV GVPYKTLVNR PGYSPMVLEM ELLSVTLEPT 850
    LSLDYITCEY KTVIPSPYVK CCGTAECKDK NLPDYSCKVF TGVYPFMWGG 900
    AYCFCDAENT QLSEAHVEKS ESCKTEFASA YRAHTASASA KLRVLYQGNN 950
    ITVTAYANGD HAVTVKDAKF IVGPMSSAWT PFDNKIVVYK GDVYNMDYPP 1000
    FGAGRPGQFG DIQSRTPESK DVYANTQLVL QRPAAGTVHV PYSQAPSGFK 1050
    YWLKERGASL QHTAPFGCQI ATNPVRAMNC AVGNMPISID IPDAAFTRVV 1100
    DAPSLTDMSC EVPACTHSSD FGGVAIIKYA VSKKGKCAVH SMTNAVTIRE 1150
    AEIEVEGNSQ LQISFSTALA SAEFRVQVCS TQVHCAAECH PPKDHIVNYP 1200
    ASHTTLGVQD ISATAMSWVQ KITGGVGLVV AVAALILIVV LCVSFSRH 1248
    Length:1,248
    Mass (Da):138,114
    Last modified:July 27, 2011 - v3
    Checksum:i1A2CEB5671529482
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti63 – 631R → K in AAN05102. (PubMed:12466484)Curated
    Sequence conflicti519 – 5202GR → SQ in AAN05102. (PubMed:12466484)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF369024 Genomic RNA. Translation: AAN05102.2.
    AF339485 Genomic RNA. Translation: AAO33341.1.
    AF490259 Genomic RNA. Translation: AAM10747.2.
    RefSeqiNP_690589.2. NC_004162.2.

    Genome annotation databases

    GeneIDi956308.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF369024 Genomic RNA. Translation: AAN05102.2 .
    AF339485 Genomic RNA. Translation: AAO33341.1 .
    AF490259 Genomic RNA. Translation: AAM10747.2 .
    RefSeqi NP_690589.2. NC_004162.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RSW NMR - A 893-910 [» ]
    ProteinModelPortali Q8JUX5.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S03.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 956308.

    Family and domain databases

    Gene3Di 2.60.40.350. 1 hit.
    2.60.98.10. 3 hits.
    InterProi IPR002548. 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 ]
    Pfami PF01589. Alpha_E1_glycop. 1 hit.
    PF00943. Alpha_E2_glycop. 1 hit.
    PF01563. Alpha_E3_glycop. 1 hit.
    PF00944. Peptidase_S3. 1 hit.
    [Graphical view ]
    PRINTSi PR00798. TOGAVIRIN.
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF56983. SSF56983. 1 hit.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS51690. ALPHAVIRUS_CP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of chikungunya virus and evidence for an internal polyadenylation site."
      Khan A.H., Morita K., Parquet Md Mdel C., Hasebe F., Mathenge E.G., Igarashi A.
      J. Gen. Virol. 83:3075-3084(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Nucleotide sequence analyses of the 26S mRNAs of viruses of the genus Alphavirus."
      Kinney R.M., Pfeffer M.
      Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. Logue C.H., Atkins G.J.
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Ross.
    4. Logue C.H., Chamberlain J.F., Atkins G.J.
      Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 91-97; 576 AND 592.

    Entry informationi

    Entry nameiPOLS_CHIKS
    AccessioniPrimary (citable) accession number: Q8JUX5
    Secondary accession number(s): Q80S29, Q8QR21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 83 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3