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Protein

Structural polyprotein

Gene
N/A
Organism
O'nyong-nyong virus (strain Igbo Ora) (ONNV) (Igbo Ora virus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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, 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 sitei138 – 1381Charge relay systemPROSITE-ProRule annotation
Active sitei144 – 1441Charge relay systemPROSITE-ProRule annotation
Active sitei212 – 2121Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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
OrganismiO'nyong-nyong virus (strain Igbo Ora) (ONNV) (Igbo Ora virus)
Taxonomic identifieri79899 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirusSFV complex
Virus hostiAnopheles [TaxID: 44482]
Homo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008382 Componenti: Genome

Subcellular locationi

Capsid protein :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini325 – 691367ExtracellularSequence analysisAdd
BLAST
Transmembranei692 – 71221HelicalSequence analysisAdd
BLAST
Topological domaini713 – 74735CytoplasmicSequence analysisAdd
BLAST
Topological domaini748 – 76215ExtracellularSequence analysisAdd
BLAST
Transmembranei763 – 78321HelicalSequence analysisAdd
BLAST
Topological domaini784 – 7874CytoplasmicSequence analysis
Transmembranei788 – 80821HelicalSequence analysisAdd
BLAST
Topological domaini809 – 1223415ExtracellularSequence analysisAdd
BLAST
Transmembranei1224 – 124421HelicalSequence analysisAdd
BLAST
Topological domaini1245 – 12473CytoplasmicSequence analysis

GO - Cellular componenti

Complete GO annotation...

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_0000238760Add
BLAST
Chaini261 – 747487p62By similarityPRO_0000238761Add
BLAST
Chaini261 – 32464E3 proteinBy similarityPRO_0000238762Add
BLAST
Signal peptidei261 – 27616Not cleavedSequence analysisAdd
BLAST
Chaini325 – 747423E2 envelope glycoproteinBy similarityPRO_0000238763Add
BLAST
Chaini748 – 808616K proteinBy similarityPRO_0000238764Add
BLAST
Chaini809 – 1247439E1 envelope glycoproteinBy similarityPRO_0000238765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi272 – 2721N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi587 – 5871N-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

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 and 6K are palmitoylated via thioester bonds.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

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

ProteinModelPortaliO90371.
SMRiO90371. Positions 112-260, 809-1198.
ModBaseiSearch...
MobiDBiSearch...

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.
IPR009003. Peptidase_S1_PA.
IPR000930. Peptidase_S3.
[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.

O90371-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFIPAQTYY NRRYQPRPWT QRPTIQVIRP KPRRRRPAGQ LAQLISAVSR
60 70 80 90 100
LALRTVPQKP RRTRKIKKQK QVKQEQQSTR NQKKKAPKQK QTQKKKRPGR
110 120 130 140 150
RERMCMKIEN DCIFEVKHEG KVTGYACLVG DKVMKPAHVK GTIDNADLAK
160 170 180 190 200
LAFKRSSKYD LECAQIPVHM KSDASKFTHE KPEGYYNWHH GAVQYSGGRF
210 220 230 240 250
TIPTGAGKPG DSGRPIFDNK GRVVAIVLGG ANEGTRTALS VVTWNKDIVT
260 270 280 290 300
KITPEGSVEW SLALPVMCLL ANTTFPCSQP PCAPCCYEKK PEETLRMLED
310 320 330 340 350
NVMQPGYYQL LDSALACSQH RQRRNARENF NVYKVTRPYL AHCPDCGEGH
360 370 380 390 400
SCHSPIALER IRSEATDGTL KIQVSLQIGI KTADSHDWTK LRYMDSHTPV
410 420 430 440 450
DADRSGLFVR TSAPCTITGT MGHFILARCP KGETLTVGFV DSRRISHTCM
460 470 480 490 500
HPFHHEPPLI GREKFHSRPQ HGKELPCSTY VHTTAATTEE IEVHMPPDTP
510 520 530 540 550
DYTLMTQQAG NVKITVDGQT VRYKCKCDGS NEGLITTDKV INNCKVDQCH
560 570 580 590 600
TAVTNHKKWQ YNSPLTPRNS EQGDRKGKIH IPFPLVNTTC RVPKARNPTV
610 620 630 640 650
TYGKNRVTLL LYPDHPTLLS YRAMGRIPDY HEEWITSKKE ISITVPAEGL
660 670 680 690 700
EVTWGNNDPY KYWPQLSTNG TAHGHPHEII LYYYELYPTT TIAVLAAASI
710 720 730 740 750
VVASLVGLSL GMCICARRRC ITPYELTPGA TIPFLLGILC CVKTAKAASY
760 770 780 790 800
YEAATYLWNE QQPLFWLQLL IPLSAAIVVC NCLKLLPCCC KTLTFLAVMS
810 820 830 840 850
IGARTVSAYE HATVIPNTVG VPYKTLVSRP GYSPMVLEME LQSVTLEPTL
860 870 880 890 900
FLDYITCEYK TITPSPYVKC CGTAECKAKN LPDYNCKVFT GVYPFMWGGA
910 920 930 940 950
YCFCDAENTQ LSEAHVEKSE SCKTEFASAY RAHTASVSAK LRVFYQGNNI
960 970 980 990 1000
TVSAYANGDH AVTVKDAKFV IGPLSSAWSP FDNKIVVYKG EVYNMDYPPF
1010 1020 1030 1040 1050
GAGRPGQFGD IQSRTPDSKD VYANTQLILQ RPAAGAIHVP YSQAPSGFKY
1060 1070 1080 1090 1100
WLKEKGASLQ HTAPFGCQIA TNPVRAVNCA VGNIPVSIDI PDAAFTRVTD
1110 1120 1130 1140 1150
APSVTDMSCE VASCTHSSDF GGAAVIKYTA SKKGKCAVHS LTNAVTIREP
1160 1170 1180 1190 1200
NVDVEGTAQL QIAFSTALAS AEFKVQICST QVHCSATCHP PKDHIVNYPS
1210 1220 1230 1240
PHTTLGVQDI STTAMSWVQK ITGGVGLVVA IAALILIIVL CVSFSRH
Length:1,247
Mass (Da):138,123
Last modified:November 1, 1998 - v1
Checksum:iCD92707A7AD9B6D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079457 Genomic RNA. Translation: AAC97207.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079457 Genomic RNA. Translation: AAC97207.1.

3D structure databases

ProteinModelPortaliO90371.
SMRiO90371. Positions 112-260, 809-1198.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS03.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
IPR009003. Peptidase_S1_PA.
IPR000930. Peptidase_S3.
[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]
ProtoNetiSearch...

Publicationsi

  1. "Emergence of epidemic O'nyong-nyong fever in Uganda after a 35-year absence: genetic characterization of the virus."
    Lanciotti R.S., Ludwig M.L., Rwaguma E.B., Lutwama J.J., Kram T.M., Karabatsos N., Cropp B.C., Miller B.R.
    Virology 252:258-268(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiPOLS_ONNVI
AccessioniPrimary (citable) accession number: O90371
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 1, 1998
Last modified: October 14, 2015
This is version 95 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.