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Protein

Structural polyprotein

Gene
N/A
Organism
Sindbis virus (SINV)
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. 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 icosahedric core particles. 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. In case of infection, new virions attach to target cells and after clathrin-mediated endocytosis their membrane fuses with the host endosomal 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.2 Publications
Assembly protein E3: May be a disulfide isomerase that catalyzes the proper folding and disulfide bond formation in pE2/E2. E3 possesses labile disulfide bonds and is in close proximity to E2 throughout the assembly pathway.1 Publication
Spike glycoprotein E2: Plays an essential role in viral attachment to target host cell, by binding to the cell receptor. Synthesized as a pE2 precursor which is processed by furin at the cell membrane just before virion budding, giving rise to E2-E1 heterodimer. The pE2-E1 heterodimer is stable, whereas E2-E1 is unstable and dissociate at low pH. pE2 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 similarity1 Publication
Protein 6K: Acts as a viroporin that participates in virus glycoprotein processing, cell permeabilization and budding of viral particles. Disrupts the calcium homeostasis of the cell, probably at the endoplasmic reticulum level resulting in the increased levels of cytoplasmic calcium. 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.5 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.2 Publications

Miscellaneous

Structural polyprotein: Translated from a subgenomic RNA synthesized during togavirus replication.By similarity

<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

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 sitei141Charge relay systemPROSITE-ProRule annotation1 Publication1
Active sitei163Charge relay systemPROSITE-ProRule annotation1 Publication1
Active sitei215Charge relay systemPROSITE-ProRule annotation1 Publication1

<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

  • clathrin-dependent endocytosis of virus by host cell Source: UniProtKB-KW
  • fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  • membrane fusion Source: CACAO
  • virion attachment to host cell Source: CACAO

<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, 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

<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:
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>OrganismiSindbis virus (SINV)
<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 identifieri11034 [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 hostiAcrocephalus scirpaceus (Eurasian reed-warbler) [TaxID: 48156]
Aedes [TaxID: 7158]
Culex [TaxID: 53527]
Homo sapiens (Human) [TaxID: 9606]
Motacilla alba (White wagtail) (Pied wagtail) [TaxID: 45807]
Streptopelia turtur [TaxID: 177155]
<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
  • UP000006710 <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

<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 :
Precursor of protein E3/E2 :
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 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>Transmembranei696 – 716HelicalSequence analysisAdd BLAST21
Transmembranei726 – 746HelicalSequence analysisAdd BLAST21
Transmembranei777 – 797HelicalSequence analysisAdd BLAST21
Transmembranei1215 – 1235HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host membrane, 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>Mutagenesisi141H → A or P: Complete loss of autocatalytic cleavage by capsid protein. 1 Publication1
Mutagenesisi141H → R: No loss of autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication1
Mutagenesisi147D → H or Y: No loss of autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication1
Mutagenesisi163D → H: No loss of autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication1
Mutagenesisi163D → N: No loss of autocatalytic cleavage by capsid protein. Infectious virus is produced. 1 Publication1
Mutagenesisi215S → A or I: Complete loss of autocatalytic cleavage by capsid protein. 1 Publication1
Mutagenesisi215S → C: 40% reduction in autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication1
Mutagenesisi215S → T: 90% reduction in autocatalytic cleavage by capsid protein. No infectious virus is produced. 1 Publication1
Mutagenesisi264W → F: 73% loss of cleavage by capsid protease. 1 Publication1
Mutagenesisi724C → A: Loss of palmitoylation. 1 Publication1
Mutagenesisi744 – 745CC → AA: Complete loss of infectivity. 2
Mutagenesisi744C → A: Loss of palmitoylation. 1 Publication1
Mutagenesisi745C → A: Loss of palmitoylation. 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_00000413211 – 264Capsid proteinAdd BLAST264
ChainiPRO_0000226238265 – 751Precursor of protein E3/E2By similarityAdd BLAST487
ChainiPRO_0000041322265 – 328Assembly protein E3Add BLAST64
ChainiPRO_0000041323329 – 751Spike glycoprotein E2Add BLAST423
ChainiPRO_0000041324752 – 8066K proteinAdd BLAST55
ChainiPRO_0000041325807 – 1245Spike glycoprotein E1Add BLAST439

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi278N-linked (GlcNAc...) asparagine; by hostSequence analysis1
<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 bondi283 ↔ 2891 Publication
Glycosylationi524N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi646N-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>Lipidationi724S-palmitoyl cysteine; by host1 Publication1
Lipidationi744S-palmitoyl cysteine; by host1 Publication1
Lipidationi745S-palmitoyl cysteine; by host1 Publication1
Disulfide bondi855 ↔ 920By similarity
Disulfide bondi868 ↔ 900By similarity
Disulfide bondi869 ↔ 902By similarity
Disulfide bondi874 ↔ 884By similarity
Glycosylationi945N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi1051N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi1065 ↔ 1077By similarity
Disulfide bondi1107 ↔ 1182By similarity
Disulfide bondi1112 ↔ 1186By similarity
Disulfide bondi1134 ↔ 1176By similarity

<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 (By similarity). Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2 (PubMed:2335827). The remaining polyprotein is then targeted to the host endoplasmic reticulum, where host signal peptidase cleaves it into pE2, 6K and E1 proteins (By similarity). pE2 is further processed to mature E3 and E2 by host furin in trans-Golgi vesicle (By similarity).By similarity1 Publication
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.2 Publications
Spike glycoprotein E1: N-glycosylated.By similarity
Spike glycoprotein E2: N-glycosylated.By similarity
Assembly protein E3: N-glycosylated.By similarity
6K protein: Palmitoylated via thioester bonds.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei264 – 265Cleavage; by autolysisBy similarity2
Sitei328 – 329Cleavage; by host furinBy similarity2
Sitei751 – 752Cleavage; by host signal peptidaseBy similarity2
Sitei806 – 807Cleavage; by host signal peptidaseBy similarity2

Keywords - PTMi

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

PTM databases

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P03316

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P03316

<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

Precursor of protein E3/E2: The precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (PubMed:8623521). Spike glycoprotein E1: The precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (PubMed:8623521). 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 (PubMed:8623521). 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 (PubMed:8623521). Spike glycoprotein E1: Spike at virion surface are constituted of three E2-E1 heterodimers (PubMed:8623521). Spike glycoprotein E2: Spike at virion surface are constituted of three E2-E1 heterodimers (PubMed:8623521). Spike glycoprotein E1: After target cell attachment and endocytosis, E1 change conformation to form homotrimers (By similarity). 6K protein: Interacts with spike glycoprotein E1 (PubMed:8892914). 6K protein: Interacts with spike glycoprotein E2 (PubMed:8892914). Spike glycoprotein E1: Interacts with 6K protein (PubMed:8892914). Spike glycoprotein E2: Interacts with 6K protein (PubMed:8892914).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-29032N

<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

11245
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P03316

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

More...
SMRi
P03316

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P03316

<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>Domaini114 – 264Peptidase S3PROSITE-ProRule annotationAdd BLAST151

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>Regioni93 – 101Ribosome-bindingBy similarity9
Regioni265 – 279Functions as an uncleaved signal peptide for the precursor of protein E3/E2By similarityAdd BLAST15
Regioni890 – 907E1 fusion peptide loopBy similarityAdd BLAST18

<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

Structural polyprotein: As soon as the capsid protein has been autocleaved, an internal uncleaved signal peptide directs the remaining polyprotein to the endoplasmic reticulum.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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
VOG0900007W

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.350, 1 hit
2.60.98.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...
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

More...
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

More...
PRINTSi
PR00798 TOGAVIRIN

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50494 SSF50494, 1 hit
SSF56983 SSF56983, 1 hit
SSF81296 SSF81296, 1 hit

PROSITE; a protein domain and family database

More...
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: P03316-1) [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
MNRGFFNMLG RRPFPAPTAM WRPRRRRQAA PMPARNGLAS QIQQLTTAVS
60 70 80 90 100
ALVIGQATRP QPPRPRPPPR QKKQAPKQPP KPKKPKTQEK KKKQPAKPKP
110 120 130 140 150
GKRQRMALKL EADRLFDVKN EDGDVIGHAL AMEGKVMKPL HVKGTIDHPV
160 170 180 190 200
LSKLKFTKSS AYDMEFAQLP VNMRSEAFTY TSEHPEGFYN WHHGAVQYSG
210 220 230 240 250
GRFTIPRGVG GRGDSGRPIM DNSGRVVAIV LGGADEGTRT ALSVVTWNSK
260 270 280 290 300
GKTIKTTPEG TEEWSAAPLV TAMCLLGNVS FPCDRPPTCY TREPSRALDI
310 320 330 340 350
LEENVNHEAY DTLLNAILRC GSSGRSKRSV IDDFTLTSPY LGTCSYCHHT
360 370 380 390 400
VPCFSPVKIE QVWDEADDNT IRIQTSAQFG YDQSGAASAN KYRYMSLKQD
410 420 430 440 450
HTVKEGTMDD IKISTSGPCR RLSYKGYFLL AKCPPGDSVT VSIVSSNSAT
460 470 480 490 500
SCTLARKIKP KFVGREKYDL PPVHGKKIPC TVYDRLKETT AGYITMHRPR
510 520 530 540 550
PHAYTSYLEE SSGKVYAKPP SGKNITYECK CGDYKTGTVS TRTEITGCTA
560 570 580 590 600
IKQCVAYKSD QTKWVFNSPD LIRHDDHTAQ GKLHLPFKLI PSTCMVPVAH
610 620 630 640 650
APNVIHGFKH ISLQLDTDHL TLLTTRRLGA NPEPTTEWIV GKTVRNFTVD
660 670 680 690 700
RDGLEYIWGN HEPVRVYAQE SAPGDPHGWP HEIVQHYYHR HPVYTILAVA
710 720 730 740 750
SATVAMMIGV TVAVLCACKA RRECLTPYAL APNAVIPTSL ALLCCVRSAN
760 770 780 790 800
AETFTETMSY LWSNSQPFFW VQLCIPLAAF IVLMRCCSCC LPFLVVAGAY
810 820 830 840 850
LAKVDAYEHA TTVPNVPQIP YKALVERAGY APLNLEITVM SSEVLPSTNQ
860 870 880 890 900
EYITCKFTTV VPSPKIKCCG SLECQPAAHA DYTCKVFGGV YPFMWGGAQC
910 920 930 940 950
FCDSENSQMS EAYVELSADC ASDHAQAIKV HTAAMKVGLR IVYGNTTSFL
960 970 980 990 1000
DVYVNGVTPG TSKDLKVIAG PISASFTPFD HKVVIHRGLV YNYDFPEYGA
1010 1020 1030 1040 1050
MKPGAFGDIQ ATSLTSKDLI ASTDIRLLKP SAKNVHVPYT QASSGFEMWK
1060 1070 1080 1090 1100
NNSGRPLQET APFGCKIAVN PLRAVDCSYG NIPISIDIPN AAFIRTSDAP
1110 1120 1130 1140 1150
LVSTVKCEVS ECTYSADFGG MATLQYVSDR EGQCPVHSHS STATLQESTV
1160 1170 1180 1190 1200
HVLEKGAVTV HFSTASPQAN FIVSLCGKKT TCNAECKPPA DHIVSTPHKN
1210 1220 1230 1240
DQEFQAAISK TSWSWLFALF GGASSLLIIG LMIFACSMML TSTRR
Note: Produced by conventional translation.
Length:1,245
Mass (Da):136,766
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:iB77C18131703F1E6
GO
Isoform Frameshifted structural polyprotein (identifier: P0DOK0-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0DOK0.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by ribosomal frameshifting.
Length:821
Mass (Da):91,215
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 varianti329 – 331SVI → RVT in strain: AR339. 3
Natural varianti333D → G in strain: HRLP. 1
Natural varianti351V → E in strain: AR339 and HRLP. 1
Natural varianti398K → E in strain: AR339. 1
Natural varianti442S → R Causes attenuation of the virus. 1
Natural varianti447N → KNGSF in strain: ov-100. 1
Natural varianti500R → G in strain: AR339. 1
Natural varianti719K → L in strain: TE12. 1
Natural varianti919D → V in strain: HRLP. 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
V01403 Genomic RNA Translation: CAA24684.1
J02363 Genomic RNA Translation: AAA96976.1
M13818 Genomic RNA Translation: AAA47485.1
AB372876 Genomic RNA Translation: BAH70330.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A03916 VHWVB
A25894 VHWVSB
B03916 VHWVB2

NCBI Reference Sequences

More...
RefSeqi
NP_062890.1, NC_001547.1 [P03316-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1502155

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
vg:1502155

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
V01403 Genomic RNA Translation: CAA24684.1
J02363 Genomic RNA Translation: AAA96976.1
M13818 Genomic RNA Translation: AAA47485.1
AB372876 Genomic RNA Translation: BAH70330.1
PIRiA03916 VHWVB
A25894 VHWVSB
B03916 VHWVB2
RefSeqiNP_062890.1, NC_001547.1 [P03316-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
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
1KXAX-ray3.10A106-264[»]
1KXBX-ray2.90A106-264[»]
1KXCX-ray3.10A106-264[»]
1KXDX-ray3.00A106-264[»]
1KXEX-ray3.20A106-264[»]
1KXFX-ray2.38A106-264[»]
1LD4electron microscopy11.40A/B/C/D1-264[»]
M/N/O/P807-1245[»]
1SVPX-ray2.00A/B106-266[»]
1Z8Yelectron microscopy9.00A/C/E/G807-1096[»]
B/D/F/H1101-1189[»]
I/K/M/O1215-1245[»]
J/L/N/P691-726[»]
Q/R/S/T114-264[»]
2SNVX-ray2.80A114-264[»]
2SNWX-ray2.70A/B107-264[»]
3J0Felectron microscopy-A/B/C/D1-264[»]
E/F/G/H807-1245[»]
I/J/K/L329-751[»]
3MUUX-ray3.29A/B/C/D/E/F329-672[»]
A/B/C/D/E/F807-1192[»]
3MUWelectron microscopy-A/D/E/F807-1190[»]
U/X/Y/Z329-672[»]
ProteinModelPortaliP03316
SMRiP03316
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29032N

Protein family/group databases

MEROPSiS03.001

PTM databases

SwissPalmiP03316

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1502155
KEGGivg:1502155

Phylogenomic databases

KOiK19288
OrthoDBiVOG0900007W

Miscellaneous databases

EvolutionaryTraceiP03316
PMAP-CutDBiP03316

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_SINDV
<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: P03316
Secondary accession number(s): C4T9C2
, P11259, Q88870, Q88871, Q88872, Q88873, Q88874
<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: December 5, 2018
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
  2. SIMILARITY comments
    Index of protein domains and families
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