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Entry version 160 (08 May 2019)
Sequence version 1 (21 Jul 1986)
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Protein

Structural polyprotein

Gene
N/A
Organism
Semliki forest virus (SFV)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Capsid protein: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release (By similarity). Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein (PubMed:3553612, PubMed:9642067). 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 icosahedric core particles (PubMed:516447). The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions (By similarity). In case of infection, new virions attach to target cells and after clathrin-mediated endocytosis their membrane fuses with the host endosomal membrane (PubMed:15954801). This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible (PubMed:1433506). The uncoating might be triggered by the interaction of capsid proteins with ribosomes (PubMed:1433506). Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (PubMed:1433506).By similarity5 Publications
Assembly protein E3: Provides the signal sequence for the translocation of the precursor of protein E3/E2 to the host endoplasmic reticulum. Furin-cleaved E3 remains associated with spike glycoprotein E1 and mediates pH protection of the latter during the transport via the secretory pathway. After virion release from the host cell, the assembly protein E3 is gradually released in the extracellular space.2 Publications
Spike glycoprotein E2: Plays a role in 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.1 Publication
6K protein: 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.2 Publications
Spike glycoprotein E1: 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. Fusion is optimal at levels of about 1 molecule of cholesterol per 2 molecules of phospholipids, and is specific for sterols containing a 3-beta-hydroxyl group.1 Publication

Miscellaneous

The mature virion nucleocapsid consists of 240 copies of the capsid protein. 80 spike trimers of E1 and E2 are present at the surface of mature virion. They project about 100 Angstroms from the outer surface and are located at the local and strict three fold axis of the icosahedral lattice. The glycoproteins splay out to form a protein shell or skirt covering most of the outer surface of the membrane bilayer.
Structural polyprotein: Translated from a subgenomic RNA synthesized during togavirus replication.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.1 Publication EC:3.4.21.90

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei145Charge relay systemPROSITE-ProRule annotation1
Active sitei167Charge relay systemPROSITE-ProRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei193Involved in dimerization of the capsid proteinBy similarity1
Active sitei219Charge relay systemPROSITE-ProRule annotation1 Publication1
Sitei226Involved in dimerization of the capsid proteinBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, RNA-binding, Serine protease
Biological processClathrin-mediated endocytosis of virus by host, 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 endocytosis by host, Virus entry into host cell

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S03.001

Transport Classification Database

More...
TCDBi
1.G.4.1.1 the viral pore-forming membrane fusion protein-4 (vmfp4) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Structural polyprotein
Alternative name(s):
p130
Cleaved into the following 6 chains:
Capsid protein (EC:3.4.21.901 Publication)
Alternative name(s):
Coat protein
Short name:
C
Alternative name(s):
p62
pE2
Alternative name(s):
E2 envelope glycoprotein
Alternative name(s):
E1 envelope glycoprotein
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSemliki forest virus (SFV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri11033 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageTogaviridaeAlphavirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiAedes [TaxID: 7158]
Atelerix albiventris (Middle-African hedgehog) (Four-toed hedgehog) [TaxID: 9368]
Culex tritaeniorhynchus (Mosquito) [TaxID: 7178]
Halcyon [TaxID: 170865]
Homo sapiens (Human) [TaxID: 9606]
Quelea [TaxID: 158617]
Rhipicephalus [TaxID: 34630]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000108382 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome
  • UP000125835 Componenti: Genome
  • UP000174511 Componenti: Genome
  • UP000000570 Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Capsid protein :
Spike glycoprotein E2 :
6K protein :
Spike glycoprotein E1 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini268 – 701ExtracellularSequence analysisAdd BLAST434
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei702 – 722HelicalSequence analysisAdd BLAST21
Topological domaini723 – 755CytoplasmicSequence analysisAdd BLAST33
Topological domaini756 – 770ExtracellularSequence analysisAdd BLAST15
Transmembranei771 – 791HelicalSequence analysisAdd BLAST21
Topological domaini792CytoplasmicSequence analysis1
Transmembranei793 – 813HelicalSequence analysisAdd BLAST21
Topological domaini814 – 1230ExtracellularSequence analysisAdd BLAST417
Transmembranei1231 – 1251HelicalSequence analysisAdd BLAST21
Topological domaini1252 – 1253CytoplasmicSequence analysis2

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host membrane, Host nucleus, Membrane, T=4 icosahedral capsid protein, Viral envelope protein, Virion

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi219 – 220SG → RST: Loss of autocatalytic cleavage by capsid protein. 1 Publication2
Mutagenesisi267W → A or R: Complete loss of cleavage by capsid protease. 1
Mutagenesisi330R → S: Complete loss of p62 precursor processing. 1 Publication1
Mutagenesisi333R → F: Complete loss of p62 precursor processing. 1 Publication1
Mutagenesisi755A → F: Complete loss of p62 precursor-6K cleavage. 1 Publication1
Mutagenesisi815A → F: Complete loss of 6K protein-E1 envelope glycoprotein cleavage. 1 Publication1
Mutagenesisi859L → F: E1 fusion is less cholesterol and sphingolipid dependent. 1 Publication1
Mutagenesisi890D → A: Shifts the pH threshold for fusion to a more acidic range. 1 Publication1
Mutagenesisi894K → Q: No effect on E1 fusion activity. 1 Publication1
Mutagenesisi898G → A: Shifts the pH threshold for fusion to a more acidic range. 2 Publications1
Mutagenesisi898G → D: No effect on E1 fusion activity. 2 Publications1
Mutagenesisi901P → D: Retention of E1 protein in endoplasmic reticulum. 1 Publication1
Mutagenesisi903M → L: No effect on E1 fusion activity. 1 Publication1
Mutagenesisi906G → A: Shifts the pH threshold for fusion to a more acidic range. 2 Publications1
Mutagenesisi906G → D: Complete loss of E1 fusion activity. 2 Publications1
Mutagenesisi906G → P: Retention of E1 protein in endoplasmic reticulum. 2 Publications1
Mutagenesisi993V → A: E1 fusion is less cholesterol and sphingolipid dependent. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000413111 – 267Capsid proteinAdd BLAST267
ChainiPRO_0000226237268 – 755Precursor of protein E3/E2Add BLAST488
ChainiPRO_0000041312268 – 333Assembly protein E3Add BLAST66
ChainiPRO_0000041313334 – 755Spike glycoprotein E2Add BLAST422
ChainiPRO_0000041314756 – 8156K proteinAdd BLAST60
ChainiPRO_0000041315816 – 1253Spike glycoprotein E1Add BLAST438

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi119 ↔ 134
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi280N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi327N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi533N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi595N-linked (GlcNAc...) asparagine; by hostSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi718S-palmitoyl cysteine; by hostSequence analysis1
Lipidationi728S-palmitoyl cysteine; by hostBy similarity1
Lipidationi748S-palmitoyl cysteine; by hostBy similarity1
Lipidationi749S-palmitoyl cysteine; by hostBy similarity1
Disulfide bondi864 ↔ 929
Disulfide bondi877 ↔ 909
Disulfide bondi878 ↔ 911
Disulfide bondi883 ↔ 893
Glycosylationi956N-linked (GlcNAc...) asparagine; by host2 Publications1
Disulfide bondi1074 ↔ 1086
Disulfide bondi1116 ↔ 1191
Disulfide bondi1121 ↔ 1195
Disulfide bondi1143 ↔ 1185
Lipidationi1248S-stearoyl cysteine; by host1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2 (PubMed:3553612). The remaining polyprotein is then targeted to the host endoplasmic reticulum, where host signal peptidase cleaves it into pE2, 6K and E1 proteins. pE2 is further processed to mature E3 and E2 by host furin in trans-Golgi vesicle (PubMed:12584323). Protein processing process takes about 30 minutes at physiologic temperatures. The folding of the p62/6K/E1 precursor requires the formation of intrachain disulfide bonds and has been shown to involve a transient covalent interaction between the nascent and newly synthesized heterodimer and the host-cell chaperones, P4HB/PDI and PDIA3/ERp57. The folding pathway also includes non covalent interaction with human CANX/calnexin and CALR/calreticulin.5 Publications
Spike glycoprotein E2: 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.1 Publication
Envelope E1, E2 and E3 proteins are N-glycosylated.1 Publication
Spike glycoprotein E1: Stearoylated.1 Publication
6K protein: Palmitoylated via thioester bonds with about four covalently bound fatty acids per molecule.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei267 – 268Cleavage; by autolysis1 Publication2
Sitei333 – 334Cleavage; by host furin2
Sitei755 – 756Cleavage; by host signal peptidase2
Sitei815 – 816Cleavage; by host signal peptidase2

Keywords - PTMi

Autocatalytic cleavage, Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PRoteomics IDEntifications database

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PRIDEi
P03315

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
575
576
577

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P03315

SwissPalm database of S-palmitoylation events

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SwissPalmi
P03315

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P03315

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Capsid protein: Homodimer (By similarity). Homomultimer (Probable). Capsid protein: Interacts with host karyopherin KPNA4; this interaction allows the nuclear import of the viral capsid protein (By similarity). Capsid protein: Interacts with spike glycoprotein E2 (By similarity). Precursor of protein E3/E2: The precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (By similarity). Spike glycoprotein E1: The precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (By similarity). Spike glycoprotein E1: Processing of the precursor of protein E3/E2 into E2 and E3 results in a heterodimer of the spike glycoproteins E2 and E1 (By similarity). Spike glycoprotein E2: Processing of the precursor of protein E3/E2 into E2 and E3 results in a heterodimer of the spike glycoproteins E2 and E1 (By similarity). Spike glycoprotein E1: Spike at virion surface are constituted of three E2-E1 heterodimers (By similarity). Spike glycoprotein E2: Spike at virion surface are constituted of three E2-E1 heterodimers (By similarity). Spike glycoprotein E1: After target cell attachment and endocytosis, E1 change conformation to form homotrimers (PubMed:1433520, PubMed:14737160). 6K protein: Interacts with spike glycoprotein E1 (By similarity). Spike glycoprotein E1: Interacts with 6K protein (By similarity). 6K protein: Interacts with spike glycoprotein E2 (By similarity). Spike glycoprotein E2: Interacts with 6K protein (By similarity).By similarityCurated

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11253
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DYLelectron microscopy9.00A/B/C/D119-267[»]
1I9WX-ray3.00A816-1205[»]
1RERX-ray3.20A/B/C816-1206[»]
1VCPX-ray3.00A/B/C119-267[»]
1VCQX-ray3.10A/B119-267[»]
2ALAX-ray3.00A816-1206[»]
2V33X-ray1.55A/B1107-1197[»]

Database of protein disorder

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DisProti
DP00999

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P03315

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P03315

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini119 – 267Peptidase S3PROSITE-ProRule annotationAdd BLAST149

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 113Intrinsically disordered, in contact with genomic RNA in nucleocapsidSequence analysisAdd BLAST113
Regioni37 – 71Host transcription inhibitionBy similarityAdd BLAST35
Regioni87 – 120Binding to the viral RNABy similarityAdd BLAST34
Regioni105 – 119Ribosome-bindingBy similarityAdd BLAST15
Regioni189 – 199Dimerization of the capsid proteinBy similarityAdd BLAST11
Regioni225 – 229Dimerization of the capsid proteinBy similarity5
Regioni728 – 748Transient transmembrane before p62-6K protein processingSequence analysisAdd BLAST21
Regioni899 – 916E1 fusion peptide loopBy similarityAdd BLAST18

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi64 – 105Nuclear localization signalBy similarityAdd BLAST42
Motifi150 – 160Nuclear export signalBy similarityAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Capsid protein: The N-terminus contains a nuclear localization signal and a CRM1-mediated nuclear export signal (By similarity). The C-terminus functions as a protease during translation to cleave itself from the translating structural polyprotein (By similarity).By similarity

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

KEGG Orthology (KO)

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KOi
K19288

Database of Orthologous Groups

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OrthoDBi
740at10239

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.350, 1 hit
2.60.98.10, 3 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002548 Alpha_E1_glycop
IPR000936 Alpha_E2_glycop
IPR002533 Alpha_E3_glycop
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR014756 Ig_E-set
IPR009003 Peptidase_S1_PA
IPR000930 Peptidase_S3

Pfam protein domain database

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Pfami
View protein in Pfam
PF01589 Alpha_E1_glycop, 1 hit
PF00943 Alpha_E2_glycop, 1 hit
PF01563 Alpha_E3_glycop, 1 hit
PF00944 Peptidase_S3, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00798 TOGAVIRIN

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50494 SSF50494, 1 hit
SSF56983 SSF56983, 1 hit
SSF81296 SSF81296, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51690 ALPHAVIRUS_CP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by ribosomal frameshifting. AlignAdd to basket
Isoform Structural polyprotein (identifier: P03315-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MNYIPTQTFY GRRWRPRPAA RPWPLQATPV APVVPDFQAQ QMQQLISAVN
60 70 80 90 100
ALTMRQNAIA PARPPKPKKK KTTKPKPKTQ PKKINGKTQQ QKKKDKQADK
110 120 130 140 150
KKKKPGKRER MCMKIENDCI FEVKHEGKVT GYACLVGDKV MKPAHVKGVI
160 170 180 190 200
DNADLAKLAF KKSSKYDLEC AQIPVHMRSD ASKYTHEKPE GHYNWHHGAV
210 220 230 240 250
QYSGGRFTIP TGAGKPGDSG RPIFDNKGRV VAIVLGGANE GSRTALSVVT
260 270 280 290 300
WNKDMVTRVT PEGSEEWSAP LITAMCVLAN ATFPCFQPPC VPCCYENNAE
310 320 330 340 350
ATLRMLEDNV DRPGYYDLLQ AALTCRNGTR HRRSVSQHFN VYKATRPYIA
360 370 380 390 400
YCADCGAGHS CHSPVAIEAV RSEATDGMLK IQFSAQIGID KSDNHDYTKI
410 420 430 440 450
RYADGHAIEN AVRSSLKVAT SGDCFVHGTM GHFILAKCPP GEFLQVSIQD
460 470 480 490 500
TRNAVRACRI QYHHDPQPVG REKFTIRPHY GKEIPCTTYQ QTTAETVEEI
510 520 530 540 550
DMHMPPDTPD RTLLSQQSGN VKITVGGKKV KYNCTCGTGN VGTTNSDMTI
560 570 580 590 600
NTCLIEQCHV SVTDHKKWQF NSPFVPRADE PARKGKVHIP FPLDNITCRV
610 620 630 640 650
PMAREPTVIH GKREVTLHLH PDHPTLFSYR TLGEDPQYHE EWVTAAVERT
660 670 680 690 700
IPVPVDGMEY HWGNNDPVRL WSQLTTEGKP HGWPHQIVQY YYGLYPAATV
710 720 730 740 750
SAVVGMSLLA LISIFASCYM LVAARSKCLT PYALTPGAAV PWTLGILCCA
760 770 780 790 800
PRAHAASVAE TMAYLWDQNQ ALFWLEFAAP VACILIITYC LRNVLCCCKS
810 820 830 840 850
LSFLVLLSLG ATARAYEHST VMPNVVGFPY KAHIERPGYS PLTLQMQVVE
860 870 880 890 900
TSLEPTLNLE YITCEYKTVV PSPYVKCCGA SECSTKEKPD YQCKVYTGVY
910 920 930 940 950
PFMWGGAYCF CDSENTQLSE AYVDRSDVCR HDHASAYKAH TASLKAKVRV
960 970 980 990 1000
MYGNVNQTVD VYVNGDHAVT IGGTQFIFGP LSSAWTPFDN KIVVYKDEVF
1010 1020 1030 1040 1050
NQDFPPYGSG QPGRFGDIQS RTVESNDLYA NTALKLARPS PGMVHVPYTQ
1060 1070 1080 1090 1100
TPSGFKYWLK EKGTALNTKA PFGCQIKTNP VRAMNCAVGN IPVSMNLPDS
1110 1120 1130 1140 1150
AFTRIVEAPT IIDLTCTVAT CTHSSDFGGV LTLTYKTNKN GDCSVHSHSN
1160 1170 1180 1190 1200
VATLQEATAK VKTAGKVTLH FSTASASPSF VVSLCSARAT CSASCEPPKD
1210 1220 1230 1240 1250
HIVPYAASHS NVVFPDMSGT ALSWVQKISG GLGAFAIGAI LVLVVVTCIG

LRR
Note: Produced by conventional translation.
Length:1,253
Mass (Da):138,017
Last modified:July 21, 1986 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2A73228D08B82AC5
GO
Isoform Frameshifted structural polyprotein (identifier: P0DJZ6-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0DJZ6.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshifting in Protein 6K ORF.
Length:830
Mass (Da):92,349
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti62A → T in strain: A7. 1
Natural varianti63R → G in strain: L10. 1
Natural varianti85N → K in strain: A7, L10 and MTV. 1
Natural varianti279A → T in strain: A7. 1
Natural varianti291V → A in strain: A7. 1
Natural varianti370V → I in strain: A7, L10 and MTV. 1
Natural varianti437K → T in strain: A7, L10 and MTV. 1
Natural varianti545N → S in strain: A7. 1
Natural varianti548M → K in strain: A7 and MTV. 1
Natural varianti614E → K in strain: MTV. 1
Natural varianti700V → A in strain: A7. 1
Natural varianti704V → A in strain: A7. 1
Natural varianti722V → A in strain: A7 and MTV. 1
Natural varianti880A → S in strain: A7. 1
Natural varianti930R → K in strain: A7. 1
Natural varianti1043M → T in strain: A7 and MTV. 1
Natural varianti1112I → T in strain: A7 and MTV. 1
Natural varianti1134T → K in strain: A7. 1
Natural varianti1138N → D in strain: A7, L10 and MTV. 1
Natural varianti1165G → R in strain: MTV. 1
Natural varianti1188R → K in strain: A7 and MTV. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
Z48163 Genomic RNA Translation: CAD90834.1
EU350586 Genomic RNA Translation: ACB12688.1
AY112987 Genomic RNA Translation: AAM64227.1
X04129 Genomic RNA Translation: CAA27742.1

Protein sequence database of the Protein Information Resource

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PIRi
A93861 VHWV
S42462

NCBI Reference Sequences

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RefSeqi
NP_463458.1, NC_003215.1 [P03315-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
922351

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
vg:922351

Keywords - Coding sequence diversityi

Ribosomal frameshifting

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48163 Genomic RNA Translation: CAD90834.1
EU350586 Genomic RNA Translation: ACB12688.1
AY112987 Genomic RNA Translation: AAM64227.1
X04129 Genomic RNA Translation: CAA27742.1
PIRiA93861 VHWV
S42462
RefSeqiNP_463458.1, NC_003215.1 [P03315-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DYLelectron microscopy9.00A/B/C/D119-267[»]
1I9WX-ray3.00A816-1205[»]
1RERX-ray3.20A/B/C816-1206[»]
1VCPX-ray3.00A/B/C119-267[»]
1VCQX-ray3.10A/B119-267[»]
2ALAX-ray3.00A816-1206[»]
2V33X-ray1.55A/B1107-1197[»]
DisProtiDP00999
SMRiP03315
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS03.001
TCDBi1.G.4.1.1 the viral pore-forming membrane fusion protein-4 (vmfp4) family

PTM databases

GlyConnecti575
576
577
iPTMnetiP03315
SwissPalmiP03315
UniCarbKBiP03315

Proteomic databases

PRIDEiP03315

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi922351
KEGGivg:922351

Phylogenomic databases

KOiK19288
OrthoDBi740at10239

Miscellaneous databases

EvolutionaryTraceiP03315

Family and domain databases

Gene3Di2.60.40.350, 1 hit
2.60.98.10, 3 hits
InterProiView protein in InterPro
IPR002548 Alpha_E1_glycop
IPR000936 Alpha_E2_glycop
IPR002533 Alpha_E3_glycop
IPR000336 Flavivir/Alphavir_Ig-like_sf
IPR036253 Glycoprot_cen/dimer_sf
IPR038055 Glycoprot_E_dimer_dom
IPR014756 Ig_E-set
IPR009003 Peptidase_S1_PA
IPR000930 Peptidase_S3
PfamiView protein in Pfam
PF01589 Alpha_E1_glycop, 1 hit
PF00943 Alpha_E2_glycop, 1 hit
PF01563 Alpha_E3_glycop, 1 hit
PF00944 Peptidase_S3, 1 hit
PRINTSiPR00798 TOGAVIRIN
SUPFAMiSSF50494 SSF50494, 1 hit
SSF56983 SSF56983, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS51690 ALPHAVIRUS_CP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLS_SFV
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P03315
Secondary accession number(s): B3TP01, Q809B6, Q8JMP5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 8, 2019
This is version 160 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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