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Protein

Structural polyprotein

Gene
N/A
Organism
Barmah forest virus (BFV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 sitei131 – 1311Charge relay systemPROSITE-ProRule annotation
Active sitei137 – 1371Charge relay systemPROSITE-ProRule annotation
Active sitei205 – 2051Charge 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.
TCDBi1.G.4.1.3. the viral pore-forming membrane fusion protein-4 (vmfp4) family.

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
OrganismiBarmah forest virus (BFV)
Taxonomic identifieri11020 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirus
Virus hostiAnopheles amictus [TaxID: 59117]
Culex annulirostris (Common banded mosquito) [TaxID: 162997]
Homo sapiens (Human) [TaxID: 9606]
Macropus [TaxID: 9312]
Proteomesi
  • UP000007609 Componenti: Genome

Subcellular locationi

Capsid protein :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini322 – 686365ExtracellularSequence analysisAdd
BLAST
Transmembranei687 – 70721HelicalSequence analysisAdd
BLAST
Topological domaini708 – 75144CytoplasmicSequence analysisAdd
BLAST
Topological domaini752 – 7565ExtracellularSequence analysis
Transmembranei757 – 77721HelicalSequence analysisAdd
BLAST
Topological domaini778 – 7792CytoplasmicSequence analysis
Transmembranei780 – 80021HelicalSequence analysisAdd
BLAST
Topological domaini801 – 1216416ExtracellularSequence analysisAdd
BLAST
Transmembranei1217 – 123721HelicalSequence analysisAdd
BLAST
Topological domaini1238 – 12392CytoplasmicSequence 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 – 253253Capsid proteinBy similarityPRO_0000238712Add
BLAST
Chaini254 – 742489p62By similarityPRO_0000238713Add
BLAST
Chaini254 – 32168E3 proteinBy similarityPRO_0000238714Add
BLAST
Signal peptidei254 – 28027Not cleavedSequence analysisAdd
BLAST
Chaini322 – 742421E2 envelope glycoproteinBy similarityPRO_0000238715Add
BLAST
Chaini743 – 800586K proteinBy similarityPRO_0000238716Add
BLAST
Chaini801 – 1239439E1 envelope glycoproteinBy similarityPRO_0000238717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi268 – 2681N-linked (GlcNAc...); by hostSequence analysis
Lipidationi715 – 7151S-palmitoyl cysteine; by hostBy similarity
Lipidationi735 – 7351S-palmitoyl cysteine; by hostBy similarity
Lipidationi736 – 7361S-palmitoyl cysteine; by hostBy similarity
Disulfide bondi849 ↔ 914By similarity
Disulfide bondi862 ↔ 894By similarity
Disulfide bondi863 ↔ 896By similarity
Disulfide bondi868 ↔ 878By similarity
Glycosylationi941 – 9411N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi1009 – 10091N-linked (GlcNAc...); by hostSequence analysis
Disulfide bondi1059 ↔ 1071By similarity
Disulfide bondi1101 ↔ 1176By similarity
Disulfide bondi1106 ↔ 1180By similarity
Disulfide bondi1128 ↔ 1170By 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
Sitei253 – 2542Cleavage; by capsid proteinBy similarity
Sitei321 – 3222Cleavage; by host furinBy similarity
Sitei742 – 7432Cleavage; by host signal peptidaseBy similarity
Sitei800 – 8012Cleavage; 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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YEWelectron microscopy5.00A/D/G/J1-253[»]
B/E/H/K804-1239[»]
C/F/I/L322-742[»]
ProteinModelPortaliP89946.
SMRiP89946. Positions 105-253, 801-1191.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini105 – 253149Peptidase S3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 peptidase S3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19288.

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.

P89946-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFIPTQTFY GRRWRPAPVQ RYIPQPQPPA PPRRRRGPSQ LQQLVAALGA
60 70 80 90 100
LALQPKQKQK RAQKKPKKTP PPKPKKTQKP KKPTQKKKSK PGKRMRNCMK
110 120 130 140 150
IENDCIFPVM LDGKVNGYAC LVGDKVMKPA HVKGTIDNPE LAKLTFKKSS
160 170 180 190 200
KYDLECAQVP VCMKSDASKF THEKPEGHYN WHHGAVQFSN GRFTIPTGSG
210 220 230 240 250
KPGDSGRPIF DNTGKVVAIV LGGANEGART ALSVVTWNKD MVTRITPEES
260 270 280 290 300
VEWSAAALNI TALCVLQNLS FPCDAPPCAP CCYEKDPAGT LRLLSDHYYH
310 320 330 340 350
PKYYELLDST MHCPQGRRPK RSVAHFEAYK ATRPYIGWCA DCGLAGSCPS
360 370 380 390 400
PVSIEHVWSD ADDGVLKIQV SMQIGIAKSN TINHAKIRYM GANGVQEAER
410 420 430 440 450
STLSVSTTAP CDILATMGHF ILARCRPGSQ VEVSLSTDPK LLCRTPFSHK
460 470 480 490 500
PRFIGNEKSP APTGHKTRIP CKTYSHQTDL TREEITMHVP PDVPIQGLVS
510 520 530 540 550
NTGKSYSLDP KTKTIKYKCT CGETVKEGTA TNKITLFNCD TAPKCITYAV
560 570 580 590 600
DNTVWQYNSQ YVPRSEVTEV KGKIHVPFPL TDSTCAVSVA PEPQVTYRLG
610 620 630 640 650
EVEFHFHPMY PTLFSIRSLG KDPSHSQEWI DTPMSKTIQV GAEGVEYVWG
660 670 680 690 700
NNNPVRLWAQ KSSSSSAHGN PISIVSHYYD LYPYWTITVL ASLGLLIVIS
710 720 730 740 750
SGFSCFLCSV ARTKCLTPYQ LAPGAQLPTF IALLCCAKSA RADTLDDFSY
760 770 780 790 800
LWTNNQAMFW LQLASPVAAF LCLSYCCRNL ACCMKIFLGI SGLCVIATQA
810 820 830 840 850
YEHSTTMPNQ VGIPFKALIE RPGYAGLPLS LVVIKSELVP SLVQDYITCN
860 870 880 890 900
YKTVVPSPYI KCCGGAECSH KNEADYKCSV FTGVYPFMWG GAYCFCDTEN
910 920 930 940 950
SQMSEVYVTR GESCEADHAI AYQVHTASLK AQVMISIGEL NQTVDVFVNG
960 970 980 990 1000
DSPARIQQSK FILGPISSAW SPFDHKVIVY RDEVYNEDYA PYGSGQAGRF
1010 1020 1030 1040 1050
GDIQSRTVNS TDVYANTNLK LKRPASGNVH VPYTQTPSGF SYWKKEKGVP
1060 1070 1080 1090 1100
LNRNAPFGCI IKVNPVRAEN CVYGNIPISM DIADAHFTRI DESPSVSLKA
1110 1120 1130 1140 1150
CEVQSCTYSS DFGGVASISY TSNKVGKCAI HSHSNSATMK DSVQDVQESG
1160 1170 1180 1190 1200
ALSLFFATSS VEPNFVVQVC NARITCHGKC EPPKDHIVPY AAKHNDAEFP
1210 1220 1230
SISTTAWQWL AHTTSGPLTI LVVAIIVVVV VSIVVCARH
Length:1,239
Mass (Da):136,297
Last modified:May 30, 2006 - v2
Checksum:iE82B5BDA41BEACD5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti826 – 8261G → A.
Natural varianti1020 – 10201K → R.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73745 Genomic RNA. Translation: AAB40702.1.
AF339488 Genomic RNA. Translation: AAO33347.1.
PIRiC37264.
D21774.
RefSeqiNP_054024.1. NC_001786.1.

Genome annotation databases

GeneIDi1489701.
KEGGivg:1489701.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73745 Genomic RNA. Translation: AAB40702.1.
AF339488 Genomic RNA. Translation: AAO33347.1.
PIRiC37264.
D21774.
RefSeqiNP_054024.1. NC_001786.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YEWelectron microscopy5.00A/D/G/J1-253[»]
B/E/H/K804-1239[»]
C/F/I/L322-742[»]
ProteinModelPortaliP89946.
SMRiP89946. Positions 105-253, 801-1191.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS03.001.
TCDBi1.G.4.1.3. the viral pore-forming membrane fusion protein-4 (vmfp4) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1489701.
KEGGivg:1489701.

Phylogenomic databases

KOiK19288.

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...

Entry informationi

Entry nameiPOLS_BFV
AccessioniPrimary (citable) accession number: P89946
Secondary accession number(s): Q80S23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 30, 2006
Last modified: December 9, 2015
This is version 101 of the entry and version 2 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

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.