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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.
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.
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.
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.

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 system By similarity
Active sitei144 – 1441Charge relay system By similarity
Active sitei212 – 2121Charge relay system By similarity
Sitei260 – 2612Cleavage; by capsid protein By similarity
Sitei324 – 3252Cleavage; by host furin By similarity
Sitei747 – 7482Cleavage; by host signal peptidase By similarity
Sitei808 – 8092Cleavage; by host signal peptidase By 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei692 – 71221Helical; Reviewed prediction
Add
BLAST
Transmembranei720 – 74021Helical; Reviewed prediction
Add
BLAST
Transmembranei763 – 78321Helical; Reviewed prediction
Add
BLAST
Transmembranei1224 – 124421Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. T=4 icosahedral viral capsid Source: UniProtKB-KW
  2. host cell cytoplasm Source: UniProtKB-SubCell
  3. host cell plasma membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB-KW
  5. virion membrane Source: UniProtKB-SubCell
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 protein By similarity
PRO_0000041281Add
BLAST
Chaini261 – 747487p62 By similarity
PRO_0000226239Add
BLAST
Chaini261 – 32464E3 protein By similarity
PRO_0000041282Add
BLAST
Signal peptidei261 – 27414Not cleaved Reviewed prediction
Add
BLAST
Chaini325 – 747423E2 envelope glycoprotein By similarity
PRO_0000041283Add
BLAST
Chaini748 – 808616K protein By similarity
PRO_0000041284Add
BLAST
Chaini809 – 1247439E1 envelope glycoprotein By similarity
PRO_0000041285Add
BLAST

Amino acid modifications

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

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.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 260149Peptidase S3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 106106Intrinsically disordered, in contact with genomic RNA in nucleocapsid Reviewed prediction
Add
BLAST
Regioni86 – 9914Ribosome-binding By similarity
Add
BLAST
Regioni720 – 74021Transient transmembrane before p62-6K protein processing Reviewed prediction
Add
BLAST
Regioni892 – 90918E1 fusion peptide loop By similarity
Add
BLAST

Sequence similaritiesi

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: May 14, 2014
This is version 106 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

Similar proteinsi