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P22056

- POLS_ONNVG

UniProt

P22056 - POLS_ONNVG

Protein

Structural polyprotein

Gene
N/A
Organism
O'nyong-nyong virus (strain Gulu) (ONNV)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      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 E3/E2 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. P62-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. P62 E3/E2 precursor 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 sitei138 – 1381Charge relay systemPROSITE-ProRule annotation
    Active sitei144 – 1441Charge relay systemPROSITE-ProRule annotation
    Active sitei212 – 2121Charge relay systemPROSITE-ProRule annotation
    Sitei260 – 2612Cleavage; by capsid proteinBy similarity
    Sitei324 – 3252Cleavage; by host furinBy similarity
    Sitei747 – 7482Cleavage; by host signal peptidaseBy similarity
    Sitei808 – 8092Cleavage; 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

    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
    OrganismiO'nyong-nyong virus (strain Gulu) (ONNV)
    Taxonomic identifieri11028 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirusSFV complex
    Virus hostiAnopheles [TaxID: 44482]
    Homo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000008868: 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 – 260260Capsid proteinBy similarityPRO_0000041281Add
    BLAST
    Chaini261 – 747487p62By similarityPRO_0000226239Add
    BLAST
    Chaini261 – 32464E3 proteinBy similarityPRO_0000041282Add
    BLAST
    Signal peptidei261 – 27414Not cleavedSequence AnalysisAdd
    BLAST
    Chaini325 – 747423E2 envelope glycoproteinBy similarityPRO_0000041283Add
    BLAST
    Chaini748 – 808616K proteinBy similarityPRO_0000041284Add
    BLAST
    Chaini809 – 1247439E1 envelope glycoproteinBy similarityPRO_0000041285Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi112 ↔ 127By similarity
    Glycosylationi272 – 2721N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi587 – 5871N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi669 – 6691N-linked (GlcNAc...); by hostSequence Analysis
    Lipidationi720 – 7201S-palmitoyl cysteine; by hostBy similarity
    Lipidationi740 – 7401S-palmitoyl cysteine; by hostBy similarity
    Lipidationi741 – 7411S-palmitoyl cysteine; by hostBy similarity
    Disulfide bondi857 ↔ 922By similarity
    Disulfide bondi870 ↔ 902By similarity
    Disulfide bondi871 ↔ 904By similarity
    Disulfide bondi876 ↔ 886By similarity
    Glycosylationi949 – 9491N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi1067 ↔ 1079By similarity
    Disulfide bondi1109 ↔ 1184By similarity
    Disulfide bondi1114 ↔ 1188By similarity
    Disulfide bondi1136 ↔ 1178By similarity
    Lipidationi1241 – 12411S-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

    3D structure databases

    ProteinModelPortaliP22056.
    SMRiP22056. Positions 112-260, 809-1198.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei692 – 71221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei720 – 74021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei763 – 78321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1224 – 124421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini112 – 260149Peptidase S3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 106106Intrinsically disordered, in contact with genomic RNA in nucleocapsidSequence AnalysisAdd
    BLAST
    Regioni86 – 9914Ribosome-bindingBy similarityAdd
    BLAST
    Regioni720 – 74021Transient transmembrane before p62-6K protein processingSequence AnalysisAdd
    BLAST
    Regioni892 – 90918E1 fusion peptide loopBy similarityAdd
    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.

    P22056-1 [UniParc]FASTAAdd to Basket

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    MEFIPAQTYY NRRYQPRPWT QRPTIQVIRP KPRRRRPAGQ LAQLISAVSR     50
    LALRTVPQKP RRTRKIKKQK QVKQEQQSTT NQKKKAPKQK QTQKKKRPGR 100
    RERMCMKIEN DCIFEVRHEG KVTGYACLVG DKVMKPAHVK GTIDNADLAK 150
    LAFKRSSKYD LECAQIPVHM KSDASKFTHE KPEGYYNWHH GAVQYSGGRF 200
    TIPTGAGKPG DSGRPIFDNK GRVVAIVLGG ANEGTRTALS VVTWNKDIVT 250
    KITPEGSVEW SLALPVMCLL ANTTFPCSQP PCAPCCYEKK PEETLRMLED 300
    NVMQPGYYQL LDSALACSQR RQKRNARENF NVYKVTRPYL AHCPDCGEGH 350
    SCHSPIALER IRSEATDGTL KIQVSLQIGI KTDDSHDWTK LRYMDSHTPV 400
    DADRSGLFVR TSAPCTITGT MGHFILARCP KGETLTVGFV DSRRISHTCM 450
    HPFRHEPPLI GREKFHSRPQ HGKELPCSTY VHTTAATAEE IEVHMPPDTP 500
    DYTLMTQQAG NVKITVDGQT VRYKCKCDGS NEGLITADKV INNCKVDQCH 550
    TAVTNHKKWQ YNSPLTPRNS EQGDRKGKIH IPFPLVNTTC RVPKARNPTV 600
    TYGKNRVTLL LHPDHPTLLS YRAMGRIPDY HEEWITNKKE ISITVPAEGL 650
    EVTWGNNDPY KYWPQLSTNG TAHGHPHEII LYYYELYPTT TIAVLAAASI 700
    VITSLVGLSL GMCICARRRC ITPYELTPGA TIPFLLGVLC CARTAKAASY 750
    YEAATYLWNE QQPLFWLQLL IPLSAAIVVC NCLKLLPCCC KTLTFLAVMS 800
    IGARTVTAYE HATVIPNTVG VPCKTLVSRP GYSPMVLEME LQSVTLEPAL 850
    SLDYITCEYK TITPSPYVKC CGTAECKAKN LPDYNCKVFT GVYPFMWGGA 900
    YCFCDAENTQ LSEAHVEKSE SCKTEFASAY RAHTASVSAK LRVFYQGNNI 950
    TVSAYANGDH AVTVEDAKFV IGPLSSAWSP FDNKIVVYKG EVYNMDYPPF 1000
    GAGRPGQFGD IQSRTPDSKD VYANTQLILQ RPAAGAIHVP YSQAPSGFKY 1050
    WLKEKGASLQ HTAPFGCQIA TNPVRAVNCA VGNIPVSIDI PDAAFTRVTD 1100
    APSITDMSCE VASCTHSSDF GGAAVIKYTA SKKGKCAVHS VTNAVTIREP 1150
    NVDVKGTAQL QIAFSTALAS AEFKVQICST LVHCSATCHP PKDHIVNYPS 1200
    PHTTLGVQDI STTAMSWVQK ITGGVGLVVA IAALILIIVL CVSFSRH 1247
    Length:1,247
    Mass (Da):137,970
    Last modified:August 1, 1991 - v1
    Checksum:iB7DCBDD17D9563CB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20303 Genomic RNA. Translation: AAA46785.1.
    PIRiB34680. VHWVN2.
    RefSeqiNP_041255.1. NC_001512.1.

    Genome annotation databases

    GeneIDi1502147.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20303 Genomic RNA. Translation: AAA46785.1 .
    PIRi B34680. VHWVN2.
    RefSeqi NP_041255.1. NC_001512.1.

    3D structure databases

    ProteinModelPortali P22056.
    SMRi P22056. Positions 112-260, 809-1198.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1502147.

    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 sequence of the genomic RNA of O'nyong-nyong virus and its use in the construction of alphavirus phylogenetic trees."
      Levinson R.S., Strauss J.H., Strauss E.G.
      Virology 175:110-123(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiPOLS_ONNVG
    AccessioniPrimary (citable) accession number: P22056
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 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

    Complete proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3