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P22056

- POLS_ONNVG

UniProt

P22056 - POLS_ONNVG

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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

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
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

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-KW
  2. host cell plasma membrane Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
  4. T=4 icosahedral viral capsid Source: UniProtKB-KW
  5. virion membrane Source: InterPro
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_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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        10         20         30         40         50
MEFIPAQTYY NRRYQPRPWT QRPTIQVIRP KPRRRRPAGQ LAQLISAVSR
60 70 80 90 100
LALRTVPQKP RRTRKIKKQK QVKQEQQSTT NQKKKAPKQK QTQKKKRPGR
110 120 130 140 150
RERMCMKIEN DCIFEVRHEG 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 LDSALACSQR RQKRNARENF NVYKVTRPYL AHCPDCGEGH
360 370 380 390 400
SCHSPIALER IRSEATDGTL KIQVSLQIGI KTDDSHDWTK LRYMDSHTPV
410 420 430 440 450
DADRSGLFVR TSAPCTITGT MGHFILARCP KGETLTVGFV DSRRISHTCM
460 470 480 490 500
HPFRHEPPLI GREKFHSRPQ HGKELPCSTY VHTTAATAEE IEVHMPPDTP
510 520 530 540 550
DYTLMTQQAG NVKITVDGQT VRYKCKCDGS NEGLITADKV INNCKVDQCH
560 570 580 590 600
TAVTNHKKWQ YNSPLTPRNS EQGDRKGKIH IPFPLVNTTC RVPKARNPTV
610 620 630 640 650
TYGKNRVTLL LHPDHPTLLS YRAMGRIPDY HEEWITNKKE ISITVPAEGL
660 670 680 690 700
EVTWGNNDPY KYWPQLSTNG TAHGHPHEII LYYYELYPTT TIAVLAAASI
710 720 730 740 750
VITSLVGLSL GMCICARRRC ITPYELTPGA TIPFLLGVLC CARTAKAASY
760 770 780 790 800
YEAATYLWNE QQPLFWLQLL IPLSAAIVVC NCLKLLPCCC KTLTFLAVMS
810 820 830 840 850
IGARTVTAYE HATVIPNTVG VPCKTLVSRP GYSPMVLEME LQSVTLEPAL
860 870 880 890 900
SLDYITCEYK TITPSPYVKC CGTAECKAKN LPDYNCKVFT GVYPFMWGGA
910 920 930 940 950
YCFCDAENTQ LSEAHVEKSE SCKTEFASAY RAHTASVSAK LRVFYQGNNI
960 970 980 990 1000
TVSAYANGDH AVTVEDAKFV 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
APSITDMSCE VASCTHSSDF GGAAVIKYTA SKKGKCAVHS VTNAVTIREP
1160 1170 1180 1190 1200
NVDVKGTAQL QIAFSTALAS AEFKVQICST LVHCSATCHP PKDHIVNYPS
1210 1220 1230 1240
PHTTLGVQDI STTAMSWVQK ITGGVGLVVA IAALILIIVL CVSFSRH
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 29, 2014
This is version 108 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