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P22056 (POLS_ONNVG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural polyprotein
Alternative name(s):
p130

Cleaved into the following 6 chains:

  1. Capsid protein
    EC=3.4.21.90
    Alternative name(s):
    Coat protein
    Short name=C
  2. p62
    Alternative name(s):
    E3/E2
  3. E3 protein
    Alternative name(s):
    Spike glycoprotein E3
  4. E2 envelope glycoprotein
    Alternative name(s):
    Spike glycoprotein E2
  5. 6K protein
  6. E1 envelope glycoprotein
    Alternative name(s):
    Spike glycoprotein E1
OrganismO'nyong-nyong virus (strain Gulu) (ONNV) [Complete proteome]
Taxonomic identifier11028 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirusSFV complex
Virus hostAnopheles [TaxID: 44482]
Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length1247 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.

Subunit structure

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.

Subcellular location

Capsid protein: Virion By similarity. Host cytoplasm By similarity.

p62: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity.

E2 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity.

E1 envelope glycoprotein: Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass type I membrane protein By similarity.

6K protein: Host cell membrane; Multi-pass membrane protein By similarity. Virion membrane; Multi-pass membrane protein By similarity.

Post-translational modification

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.

Miscellaneous

Structural polyprotein is translated from a subgenomic RNA synthesized during togavirus replication.

Sequence similarities

Contains 1 peptidase S3 domain.

Ontologies

Keywords
   Biological processFusion 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
   Cellular componentCapsid protein
Host cell membrane
Host cytoplasm
Host membrane
Membrane
T=4 icosahedral capsid protein
Virion
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processfusion of virus membrane with host endosome membrane

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentT=4 icosahedral viral capsid

Inferred from electronic annotation. Source: UniProtKB-KW

host cell cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 260260Capsid protein By similarity
PRO_0000041281
Chain261 – 747487p62 By similarity
PRO_0000226239
Chain261 – 32464E3 protein By similarity
PRO_0000041282
Signal peptide261 – 27414Not cleaved Potential
Chain325 – 747423E2 envelope glycoprotein By similarity
PRO_0000041283
Chain748 – 808616K protein By similarity
PRO_0000041284
Chain809 – 1247439E1 envelope glycoprotein By similarity
PRO_0000041285

Regions

Transmembrane692 – 71221Helical; Potential
Transmembrane720 – 74021Helical; Potential
Transmembrane763 – 78321Helical; Potential
Transmembrane1224 – 124421Helical; Potential
Domain112 – 260149Peptidase S3
Region1 – 106106Intrinsically disordered, in contact with genomic RNA in nucleocapsid Potential
Region86 – 9914Ribosome-binding By similarity
Region720 – 74021Transient transmembrane before p62-6K protein processing Potential
Region892 – 90918E1 fusion peptide loop By similarity

Sites

Active site1381Charge relay system By similarity
Active site1441Charge relay system By similarity
Active site2121Charge relay system By similarity
Site260 – 2612Cleavage; by capsid protein By similarity
Site324 – 3252Cleavage; by host furin By similarity
Site747 – 7482Cleavage; by host signal peptidase By similarity
Site808 – 8092Cleavage; by host signal peptidase By similarity

Amino acid modifications

Lipidation7201S-palmitoyl cysteine; by host By similarity
Lipidation7401S-palmitoyl cysteine; by host By similarity
Lipidation7411S-palmitoyl cysteine; by host By similarity
Lipidation12411S-stearoyl cysteine; by host By similarity
Glycosylation2721N-linked (GlcNAc...); by host Potential
Glycosylation5871N-linked (GlcNAc...); by host Potential
Glycosylation6691N-linked (GlcNAc...); by host Potential
Glycosylation9491N-linked (GlcNAc...); by host Potential
Disulfide bond112 ↔ 127 By similarity
Disulfide bond857 ↔ 922 By similarity
Disulfide bond870 ↔ 902 By similarity
Disulfide bond871 ↔ 904 By similarity
Disulfide bond876 ↔ 886 By similarity
Disulfide bond1067 ↔ 1079 By similarity
Disulfide bond1109 ↔ 1184 By similarity
Disulfide bond1114 ↔ 1188 By similarity
Disulfide bond1136 ↔ 1178 By similarity

Sequences

Sequence LengthMass (Da)Tools
P22056 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: B7DCBDD17D9563CB

FASTA1,247137,970
        10         20         30         40         50         60 
MEFIPAQTYY NRRYQPRPWT QRPTIQVIRP KPRRRRPAGQ LAQLISAVSR LALRTVPQKP 

        70         80         90        100        110        120 
RRTRKIKKQK QVKQEQQSTT NQKKKAPKQK QTQKKKRPGR RERMCMKIEN DCIFEVRHEG 

       130        140        150        160        170        180 
KVTGYACLVG DKVMKPAHVK GTIDNADLAK LAFKRSSKYD LECAQIPVHM KSDASKFTHE 

       190        200        210        220        230        240 
KPEGYYNWHH GAVQYSGGRF TIPTGAGKPG DSGRPIFDNK GRVVAIVLGG ANEGTRTALS 

       250        260        270        280        290        300 
VVTWNKDIVT KITPEGSVEW SLALPVMCLL ANTTFPCSQP PCAPCCYEKK PEETLRMLED 

       310        320        330        340        350        360 
NVMQPGYYQL LDSALACSQR RQKRNARENF NVYKVTRPYL AHCPDCGEGH SCHSPIALER 

       370        380        390        400        410        420 
IRSEATDGTL KIQVSLQIGI KTDDSHDWTK LRYMDSHTPV DADRSGLFVR TSAPCTITGT 

       430        440        450        460        470        480 
MGHFILARCP KGETLTVGFV DSRRISHTCM HPFRHEPPLI GREKFHSRPQ HGKELPCSTY 

       490        500        510        520        530        540 
VHTTAATAEE IEVHMPPDTP DYTLMTQQAG NVKITVDGQT VRYKCKCDGS NEGLITADKV 

       550        560        570        580        590        600 
INNCKVDQCH TAVTNHKKWQ YNSPLTPRNS EQGDRKGKIH IPFPLVNTTC RVPKARNPTV 

       610        620        630        640        650        660 
TYGKNRVTLL LHPDHPTLLS YRAMGRIPDY HEEWITNKKE ISITVPAEGL EVTWGNNDPY 

       670        680        690        700        710        720 
KYWPQLSTNG TAHGHPHEII LYYYELYPTT TIAVLAAASI VITSLVGLSL GMCICARRRC 

       730        740        750        760        770        780 
ITPYELTPGA TIPFLLGVLC CARTAKAASY YEAATYLWNE QQPLFWLQLL IPLSAAIVVC 

       790        800        810        820        830        840 
NCLKLLPCCC KTLTFLAVMS IGARTVTAYE HATVIPNTVG VPCKTLVSRP GYSPMVLEME 

       850        860        870        880        890        900 
LQSVTLEPAL SLDYITCEYK TITPSPYVKC CGTAECKAKN LPDYNCKVFT GVYPFMWGGA 

       910        920        930        940        950        960 
YCFCDAENTQ LSEAHVEKSE SCKTEFASAY RAHTASVSAK LRVFYQGNNI TVSAYANGDH 

       970        980        990       1000       1010       1020 
AVTVEDAKFV IGPLSSAWSP FDNKIVVYKG EVYNMDYPPF GAGRPGQFGD IQSRTPDSKD 

      1030       1040       1050       1060       1070       1080 
VYANTQLILQ RPAAGAIHVP YSQAPSGFKY WLKEKGASLQ HTAPFGCQIA TNPVRAVNCA 

      1090       1100       1110       1120       1130       1140 
VGNIPVSIDI PDAAFTRVTD APSITDMSCE VASCTHSSDF GGAAVIKYTA SKKGKCAVHS 

      1150       1160       1170       1180       1190       1200 
VTNAVTIREP NVDVKGTAQL QIAFSTALAS AEFKVQICST LVHCSATCHP PKDHIVNYPS 

      1210       1220       1230       1240 
PHTTLGVQDI STTAMSWVQK ITGGVGLVVA IAALILIIVL CVSFSRH 

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References

[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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20303 Genomic RNA. Translation: AAA46785.1.
PIRVHWVN2. B34680.
RefSeqNP_041255.1. NC_001512.1.

3D structure databases

ProteinModelPortalP22056.
SMRP22056. Positions 112-260, 809-1198.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1502147.

Family and domain databases

Gene3D2.60.40.350. 1 hit.
2.60.98.10. 3 hits.
InterProIPR002548. 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]
PfamPF01589. Alpha_E1_glycop. 1 hit.
PF00943. Alpha_E2_glycop. 1 hit.
PF01563. Alpha_E3_glycop. 1 hit.
PF00944. Peptidase_S3. 1 hit.
[Graphical view]
PRINTSPR00798. TOGAVIRIN.
SUPFAMSSF50494. SSF50494. 1 hit.
SSF56983. SSF56983. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS51690. ALPHAVIRUS_CP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePOLS_ONNVG
AccessionPrimary (citable) accession number: P22056
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: February 19, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries