POLS_ONNVS
ID POLS_ONNVS Reviewed; 1247 AA.
AC O90369;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Structural polyprotein;
DE AltName: Full=p130;
DE Contains:
DE RecName: Full=Capsid protein;
DE EC=3.4.21.90;
DE AltName: Full=Coat protein;
DE Short=C;
DE Contains:
DE RecName: Full=Precursor of protein E3/E2;
DE AltName: Full=p62;
DE AltName: Full=pE2;
DE Contains:
DE RecName: Full=Assembly protein E3;
DE Contains:
DE RecName: Full=Spike glycoprotein E2;
DE AltName: Full=E2 envelope glycoprotein;
DE Contains:
DE RecName: Full=6K protein;
DE Contains:
DE RecName: Full=Spike glycoprotein E1;
DE AltName: Full=E1 envelope glycoprotein;
OS O'nyong-nyong virus (strain SG650) (ONNV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=374989;
OH NCBI_TaxID=44482; Anopheles.
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9875334; DOI=10.1006/viro.1998.9437;
RA Lanciotti R.S., Ludwig M.L., Rwaguma E.B., Lutwama J.J., Kram T.M.,
RA Karabatsos N., Cropp B.C., Miller B.R.;
RT "Emergence of epidemic O'nyong-nyong fever in Uganda after a 35-year
RT absence: genetic characterization of the virus.";
RL Virology 252:258-268(1998).
CC -!- FUNCTION: [Capsid protein]: Possesses a protease activity that results
CC in its autocatalytic cleavage from the nascent structural protein.
CC Following its self-cleavage, the capsid protein transiently associates
CC with ribosomes, and within several minutes the protein binds to viral
CC RNA and rapidly assembles into icosahedric core particles. The
CC resulting nucleocapsid eventually associates with the cytoplasmic
CC domain of the spike glycoprotein E2 at the cell membrane, leading to
CC budding and formation of mature virions. In case of infection, new
CC virions attach to target cells and after clathrin-mediated endocytosis
CC their membrane fuses with the host endosomal membrane. This leads to
CC the release of the nucleocapsid into the cytoplasm, followed by an
CC uncoating event necessary for the genomic RNA to become accessible. The
CC uncoating might be triggered by the interaction of capsid proteins with
CC ribosomes. Binding of ribosomes would release the genomic RNA since the
CC same region is genomic RNA-binding and ribosome-binding.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- FUNCTION: [Assembly protein E3]: Provides the signal sequence for the
CC translocation of the precursor of protein E3/E2 to the host endoplasmic
CC reticulum. Mediates pH protection of spike glycoprotein E1 during the
CC transport via the secretory pathway. {ECO:0000250|UniProtKB:P03315}.
CC -!- FUNCTION: [Spike glycoprotein E2]: Plays a role in viral attachment to
CC target host cell, by binding to the cell receptor. Synthesized as a p62
CC precursor which is processed by furin at the cell membrane just before
CC virion budding, giving rise to E2-E1 heterodimer. The p62-E1
CC heterodimer is stable, whereas E2-E1 is unstable and dissociate at low
CC pH. p62 is processed at the last step, presumably to avoid E1 fusion
CC activation before its final export to cell surface. E2 C-terminus
CC contains a transitory transmembrane that would be disrupted by
CC palmitoylation, resulting in reorientation of the C-terminal tail from
CC lumenal to cytoplasmic side. This step is critical since E2 C-terminus
CC is involved in budding by interacting with capsid proteins. This
CC release of E2 C-terminus in cytoplasm occurs lately in protein export,
CC and precludes premature assembly of particles at the endoplasmic
CC reticulum membrane. {ECO:0000250|UniProtKB:P03315}.
CC -!- FUNCTION: [6K protein]: Constitutive membrane protein involved in virus
CC glycoprotein processing, cell permeabilization, and the budding of
CC viral particles. Disrupts the calcium homeostasis of the cell, probably
CC at the endoplasmic reticulum level. This leads to cytoplasmic calcium
CC elevation. Because of its lipophilic properties, the 6K protein is
CC postulated to influence the selection of lipids that interact with the
CC transmembrane domains of the glycoproteins, which, in turn, affects the
CC deformability of the bilayer required for the extreme curvature that
CC occurs as budding proceeds. Present in low amount in virions, about 3%
CC compared to viral glycoproteins. {ECO:0000250|UniProtKB:P03315}.
CC -!- FUNCTION: [Spike glycoprotein E1]: Class II viral fusion protein.
CC Fusion activity is inactive as long as E1 is bound to E2 in mature
CC virion. After virus attachment to target cell and endocytosis,
CC acidification of the endosome would induce dissociation of E1/E2
CC heterodimer and concomitant trimerization of the E1 subunits. This E1
CC trimer is fusion active, and promotes release of viral nucleocapsid in
CC cytoplasm after endosome and viral membrane fusion. Efficient fusion
CC requires the presence of cholesterol and sphingolipid in the target
CC membrane. Fusion is optimal at levels of about 1 molecule of
CC cholesterol per 2 molecules of phospholipids, and is specific for
CC sterols containing a 3-beta-hydroxyl group.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Autocatalytic release of the core protein from the N-terminus
CC of the togavirus structural polyprotein by hydrolysis of a -Trp-|-
CC Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03316};
CC -!- SUBUNIT: [Capsid protein]: Homomultimer (Probable). Interacts with host
CC karyopherin KPNA4; this interaction allows the nuclear import of the
CC viral capsid protein (By similarity). Interacts with spike glycoprotein
CC E2 (By similarity). Interacts with host IRAK1; the interaction leads to
CC inhibition of IRAK1-dependent signaling (By similarity).
CC {ECO:0000250|UniProtKB:P03316, ECO:0000250|UniProtKB:Q8JUX5}.
CC -!- SUBUNIT: [Precursor of protein E3/E2]: The precursor of protein E3/E2
CC and E1 form a heterodimer shortly after synthesis.
CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316}.
CC -!- SUBUNIT: [Spike glycoprotein E1]: The precursor of protein E3/E2 and E1
CC form a heterodimer shortly after synthesis. Processing of the precursor
CC of protein E3/E2 into E2 and E3 results in a heterodimer of the spike
CC glycoproteins E2 and E1. Spike at virion surface are constituted of
CC three E2-E1 heterodimers. After target cell attachment and endocytosis,
CC E1 change conformation to form homotrimers. Interacts with 6K protein.
CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316}.
CC -!- SUBUNIT: [Spike glycoprotein E2]: Processing of the precursor of
CC protein E3/E2 into E2 and E3 results in a heterodimer of the spike
CC glycoproteins E2 and E1. Spike at virion surface are constituted of
CC three E2-E1 heterodimers. Interacts with 6K protein.
CC {ECO:0000250|UniProtKB:P03315, ECO:0000250|UniProtKB:P03316}.
CC -!- SUBUNIT: [6K protein]: Interacts with spike glycoprotein E1. Interacts
CC with spike glycoprotein E2. {ECO:0000250|UniProtKB:P03315,
CC ECO:0000250|UniProtKB:P03316}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion
CC {ECO:0000250|UniProtKB:P03316}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P03316}. Host cell membrane
CC {ECO:0000250|UniProtKB:P03316}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane
CC {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8JUX5}.
CC -!- SUBCELLULAR LOCATION: [6K protein]: Host cell membrane
CC {ECO:0000250|UniProtKB:P03316}; Multi-pass membrane protein
CC {ECO:0000255}. Virion membrane {ECO:0000250|UniProtKB:P03316}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Spike glycoprotein E1]: Virion membrane
CC {ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000250|UniProtKB:P03316,
CC ECO:0000250|UniProtKB:Q8JUX5}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: Structural polyprotein: As soon as the capsid protein has been
CC autocleaved, an internal uncleaved signal peptide directs the remaining
CC polyprotein to the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield
CC mature proteins. Capsid protein is auto-cleaved during polyprotein
CC translation, unmasking a signal peptide at the N-terminus of the
CC precursor of E3/E2. The remaining polyprotein is then targeted to the
CC host endoplasmic reticulum, where host signal peptidase cleaves it into
CC pE2, 6K and E1 proteins. pE2 is further processed to mature E3 and E2
CC by host furin in trans-Golgi vesicle. {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Spike glycoprotein E2]: Palmitoylated via thioester bonds. These
CC palmitoylations may induce disruption of the C-terminus transmembrane.
CC This would result in the reorientation of E2 C-terminus from lumenal to
CC cytoplasmic side. {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Spike glycoprotein E1]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Spike glycoprotein E2]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [Assembly protein E3]: N-glycosylated.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- PTM: [6K protein]: Palmitoylated via thioester bonds.
CC {ECO:0000250|UniProtKB:P03315}.
CC -!- MISCELLANEOUS: Structural polyprotein: Translated from a subgenomic RNA
CC synthesized during togavirus replication.
CC {ECO:0000250|UniProtKB:Q86925}.
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DR EMBL; AF079456; AAC97205.1; -; Genomic_RNA.
DR BMRB; O90369; -.
DR SMR; O90369; -.
DR MEROPS; S03.001; -.
DR Proteomes; UP000007787; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.40.2400; -; 1.
DR Gene3D; 2.60.40.3200; -; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 2.60.40.4310; -; 1.
DR Gene3D; 2.60.98.10; -; 3.
DR InterPro; IPR002548; Alpha_E1_glycop.
DR InterPro; IPR000936; Alpha_E2_glycop.
DR InterPro; IPR002533; Alpha_E3_glycop.
DR InterPro; IPR042304; Alphavir_E2_A.
DR InterPro; IPR042305; Alphavir_E2_B.
DR InterPro; IPR042306; Alphavir_E2_C.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000930; Peptidase_S3.
DR Pfam; PF01589; Alpha_E1_glycop; 1.
DR Pfam; PF00943; Alpha_E2_glycop; 1.
DR Pfam; PF01563; Alpha_E3_glycop; 1.
DR Pfam; PF00944; Peptidase_S3; 1.
DR PRINTS; PR00798; TOGAVIRIN.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56983; SSF56983; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51690; ALPHAVIRUS_CP; 1.
PE 3: Inferred from homology;
KW Capsid protein; Cleavage on pair of basic residues; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host cytoplasm; Host membrane; Host-virus interaction;
KW Hydrolase; Lipoprotein; Membrane; Palmitate; Protease; Serine protease;
KW T=4 icosahedral capsid protein; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral penetration into host cytoplasm;
KW Virion; Virus entry into host cell.
FT CHAIN 1..260
FT /note="Capsid protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000238754"
FT CHAIN 261..747
FT /note="Precursor of protein E3/E2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000238755"
FT CHAIN 261..324
FT /note="Assembly protein E3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000238756"
FT CHAIN 325..747
FT /note="Spike glycoprotein E2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000238757"
FT CHAIN 748..808
FT /note="6K protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000238758"
FT CHAIN 809..1247
FT /note="Spike glycoprotein E1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000238759"
FT TOPO_DOM 325..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..747
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TOPO_DOM 748..762
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 763..783
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 784..787
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 788..808
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 809..1223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1224..1244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1245..1247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 112..260
FT /note="Peptidase S3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT REGION 52..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..99
FT /note="Ribosome-binding"
FT /evidence="ECO:0000250"
FT REGION 261..273
FT /note="Functions as an uncleaved signal peptide for the
FT precursor of protein E3/E2"
FT /evidence="ECO:0000250|UniProtKB:P03315"
FT REGION 720..740
FT /note="Transient transmembrane before p62-6K protein
FT processing"
FT /evidence="ECO:0000255"
FT REGION 892..909
FT /note="E1 fusion peptide loop"
FT /evidence="ECO:0000250|UniProtKB:Q8JUX5"
FT COMPBIAS 83..101
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01027"
FT SITE 260..261
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P03315"
FT SITE 324..325
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250"
FT SITE 747..748
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 808..809
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT LIPID 720
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 740
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT LIPID 741
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 857..922
FT /evidence="ECO:0000250"
FT DISULFID 870..902
FT /evidence="ECO:0000250"
FT DISULFID 871..904
FT /evidence="ECO:0000250"
FT DISULFID 876..886
FT /evidence="ECO:0000250"
FT DISULFID 1067..1079
FT /evidence="ECO:0000250"
FT DISULFID 1109..1184
FT /evidence="ECO:0000250"
FT DISULFID 1114..1188
FT /evidence="ECO:0000250"
FT DISULFID 1136..1178
FT /evidence="ECO:0000250"
SQ SEQUENCE 1247 AA; 138104 MW; E649DCF9EDCBE62F CRC64;
MEFIPAQTYY NRRYQPRPWT QRPTIQVIRP KPRRSRPAGQ LAQLISAVSR LALRTVPQKP
RRTRKTKKQK QVKQEQQSTR NQKKKAPKQK QTQKKKRPGR RERMCMKIEN DCIFEVKHEG
KITGYACLVG DKVMKPAHVK GTIDNADLAK LAFKRSSKYD LECAQIPVHM KSDASKFTHE
KPEGYYNWHH GAVQYSGGRF TIPTGAGKPG DSGRPIFDNK GRVVAIVLGG ANEGTRTALS
VVTWNKDIVT KITPEGSVEW SLALPVMCLL ANTTFPCSQP PCAPCCYEKK PEETLRMLED
NVMQPGYYQL LDSALACSQH RQRRNARENF NVYKVTRPYL AHCPDCGEGH SCHSPIALER
IRSEATDGTL KIQVSLQIGI KTDDSHDWTK LRYMDSHTPV DADRSGLFVR TSAPCTITGT
MGHFILARCP KGETLTVGFV DSRRISHTCM HPFHHEPPLI GREKFHSRPQ HGKELPCSTY
VHTTAATTEE IEVHMPPDTP DYTLMTQQAG NVKITVDGQT VRYKCKCDGS NEGLITTDKV
INNCKVDQCH TAVTNHKKWQ YNSPLTPRNS EQGDRKGKIH IPFPLVNTTC RVPKARNPTI
TYGKNRVTLL LYPDHPTLLS YRSMGRIPDY HEEWITSKKE ISITVPAEGL EVTWGNNDPY
KYWPQLSTNG TAHGHPHEII LYYYELYPTT TIAVLAAASI VVASLVSLSL GMCICARRRC
ITPYELTPGA TIPFLLGVLC CVKTAKAASY YEAATYLWNE QQPLFWLQLL IPLSAAIVAC
NCLKLLPCCC KTLTFLAVMS IGARTVSAYE HATVIPNTVG VPYKTLVSRP GYSPMVLEME
LQSVTLEPTL FLDYITCEYK TITPSPYVKC CGTAECKAKN LPDYNCKVFT GVYPFMWGGA
YCFCDAENTQ LSEAHVEKSE SCKTEFASAY RAHTASVSAK LRVFYQGNNI TVSAYANGDH
AVTVKDAKFV IGPLSSAWSP FDNKIVVYKG EVYNMDYPPF GAGRPGQFGD IQSRTPDSKD
VYANTQLILQ RPAAGAIHVP YSQAPSGFKY WLKEKGASLQ HTAPFGCQIA TNPVRAVNCA
VGNIPVSIDI PDAAFTRVTD APSVTDMSCE VASCTHSSDF GGAAVVKYTA SKKGKCAVHS
LTNAVTIREP NVDVEGTAQL QIAFSTALAS AEFKVQICST QVHCSATCHP PKDHIVNYPS
PHTTLGVQDI STTAMSWVQK ITGGVGLVVA IAALILIIVL CVSFSRH
