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UniProtKB - P36329 (POLS_EEVV3)

Entry version 127 (25 May 2022)
Sequence version 1 (01 Jun 1994)
Previous versions | rss
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Protein

Structural polyprotein

Gene
N/A
Organism
Venezuelan equine encephalitis virus (strain 3880) (VEEV)
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>-Protein inferred from homologyi <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

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 (By similarity).

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 (By similarity).

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:16427678).

This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible (By similarity).

The uncoating might be triggered by the interaction of capsid proteins with ribosomes (By similarity).

Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity).

Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression (By similarity).

Inhibits host transcription (By similarity).

Forms a tetrameric complex with XPO1/CRM1 and the nuclear import receptor importin (By similarity).

This complex blocks the central channel of host nuclear pores thereby inhibiting the receptor-mediated nuclear transport and thus the host mRNA and rRNA transcription (By similarity).

The inhibition of transcription is linked to a cytopathic effect on the host cell (By similarity).

By similarity1 Publication

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.

By similarity

Plays a role in viral attachment to target host cell, by binding to the cell receptor LDLRAD3. 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

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

Class II viral fusion protein. Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to cell receptor LDLRAD3 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.

By similarity

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%5Fsection">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.By similarity EC:3.4.21.90

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei152Charge relay systemPROSITE-ProRule annotation1
Active sitei174Charge 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>Sitei200Involved in dimerization of the capsid proteinBy similarity1
Active sitei226Charge relay systemPROSITE-ProRule annotation1
Sitei233Involved 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Eukaryotic host gene expression shutoff by virus, Eukaryotic host transcription shutoff by virus, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host gene expression shutoff by virus, 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%5Fand%5Ftaxonomy%5Fsection">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:3.4.21.90By similarity)
Alternative name(s):
Coat protein
Short name:
C
Precursor of protein E3/E2
Alternative name(s):
p62
pE2
Assembly protein E3
Spike glycoprotein E2
Alternative name(s):
E2 envelope glycoprotein
6K protein
Spike glycoprotein E1
Alternative name(s):
E1 envelope glycoprotein
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiVenezuelan equine encephalitis virus (strain 3880) (VEEV)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri36382 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiViruses › Riboviria › Orthornavirae › Kitrinoviricota › Alsuviricetes › Martellivirales › Togaviridae › Alphavirus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 hostiBos taurus (Bovine) [TaxID: 9913]
Didelphis marsupialis (Southern opossum) [TaxID: 9268]
Equus asinus (Donkey) (Equus africanus asinus) [TaxID: 9793]
Equus caballus (Horse) [TaxID: 9796]
Homo sapiens (Human) [TaxID: 9606]
Melanoconion [TaxID: 53535]
Philander opossum (Gray four-eyed opossum) [TaxID: 9272]
Proechimys [TaxID: 10162]
Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000008299 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 domaini276 – 701ExtracellularSequence analysisAdd BLAST426
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 – 757CytoplasmicSequence analysisAdd BLAST35
Topological domaini758 – 772ExtracellularSequence analysisAdd BLAST15
Transmembranei773 – 793HelicalSequence analysisAdd BLAST21
Topological domaini794CytoplasmicSequence analysis1
Transmembranei795 – 815HelicalSequence analysisAdd BLAST21
Topological domaini816 – 1225ExtracellularSequence analysisAdd BLAST410
Transmembranei1226 – 1246HelicalSequence analysisAdd BLAST21
Topological domaini1247 – 1255CytoplasmicSequence analysis9

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 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000412511 – 275Capsid proteinAdd BLAST275
ChainiPRO_0000234318276 – 757Precursor of protein E3/E2Add BLAST482
ChainiPRO_0000041252276 – 334Assembly protein E3Add BLAST59
ChainiPRO_0000041253335 – 757Spike glycoprotein E2Add BLAST423
ChainiPRO_0000041254758 – 8136K proteinAdd BLAST56
ChainiPRO_0000041255814 – 1255Spike glycoprotein E1Add BLAST442

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi47N-linked (GlcNAc...) asparagine; by hostSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei93PhosphothreonineBy similarity1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei124PhosphoserineBy similarity1
Modified residuei127PhosphothreonineBy similarity1
Glycosylationi286N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi652N-linked (GlcNAc...) asparagine; by hostSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Lipidationi730S-palmitoyl cysteine; by hostBy similarity1
Lipidationi750S-palmitoyl cysteine; by hostBy similarity1
Lipidationi751S-palmitoyl cysteine; by hostBy similarity1
<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 bondi862 ↔ 927By similarity
Disulfide bondi875 ↔ 907By similarity
Disulfide bondi876 ↔ 909By similarity
Disulfide bondi881 ↔ 891By similarity
Glycosylationi947N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi1072 ↔ 1084By similarity
Disulfide bondi1114 ↔ 1189By similarity
Disulfide bondi1119 ↔ 1193By similarity
Disulfide bondi1141 ↔ 1183By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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. 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.By similarity
Phosphorylated on serine and threonine residues.By similarity
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.By similarity
N-glycosylated.By similarity
N-glycosylated.By similarity
N-glycosylated.By similarity
Palmitoylated via thioester bonds.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei275 – 276Cleavage; by autolysisBy similarity2
Sitei334 – 335Cleavage; by host furinBy similarity2
Sitei757 – 758Cleavage; by host signal peptidaseBy similarity2
Sitei813 – 814Cleavage; by host signal peptidaseBy similarity2

Keywords - PTMi

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

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Part of a tetrameric complex composed of host CRM1, host importin alpha/beta dimer and the viral capsid; this complex blocks the receptor-mediated transport through the nuclear pore (By similarity).

Interacts with host phosphatase PPP1CA; this interaction dephosphorylates the capsid protein, which increases its ability to bind to the viral genome (By similarity).

Interacts with host karyopherin KPNA4; this interaction allows the nuclear import of the viral capsid protein (By similarity).

Interacts with spike glycoprotein E2 (By similarity).

Interacts with host IRAK1; the interaction leads to inhibition of IRAK1-dependent signaling (By similarity).

By similarity

The precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (By similarity).

By similarity

The precursor of protein E3/E2 and E1 form a heterodimer shortly after synthesis (By similarity). Processing of the precursor of protein E3/E2 into E2 and E3 results in a heterodimer of the spike glycoproteins E2 and E1. Spike at virion surface are constituted of three E2-E1 heterodimers (By similarity). After target cell attachment and endocytosis, E1 change conformation to form homotrimers (By similarity).

Interacts with 6K protein (By similarity).

Interacts with host LDLRAD3; this interaction mediates viral entry to the host cell (By similarity).

By similarity

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 at virion surface are constituted of three E2-E1 heterodimers (By similarity).

Interacts with 6K protein (By similarity).

Interacts with host LDLRAD3; this interaction mediates viral entry to the host cell (By similarity).

By similarity

Interacts with spike glycoprotein E1 (By similarity).

Interacts with spike glycoprotein E2 (By similarity).

By similarity

<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

3D structure databases

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

More...SMRi		P36329

Database of comparative protein structure models

More...ModBasei		Search...

<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%5Fand%5Fdomains%5Fsection">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>Domaini126 – 275Peptidase S3PROSITE-ProRule annotationAdd BLAST150

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 – 33Necessary for nucleocapsid assembly and virus assemblyBy similarityAdd BLAST33
Regioni33 – 68Host transcription inhibitionBy similarityAdd BLAST36
Regioni44 – 119DisorderedSequence analysisAdd BLAST76
Regioni91 – 127Binding to the viral RNABy similarityAdd BLAST37
Regioni112 – 126Ribosome-bindingBy similarityAdd BLAST15
Regioni276 – 287Functions as an uncleaved signal peptide for the precursor of protein E3/E2By similarityAdd BLAST12
Regioni730 – 750Transient transmembrane before p62-6K protein processingSequence analysisAdd BLAST21
Regioni897 – 914E1 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>Motifi41 – 48Supraphysiological nuclear export signalBy similarity8
Motifi64 – 68Nuclear localization signalBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi57 – 76Basic and acidic residuesSequence analysisAdd BLAST20

<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
The very N-terminus plays a role in the particle assembly process (By similarity). The N-terminus also contains a nuclear localization signal and a supraphysiological nuclear export signal (supraNES), which is an unusually strong NES that mediates host CRM1 binding in the absence of RanGTP and thus can bind CRM1, not only in the nucleus, but also in the cytoplasm (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

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.10.10, 2 hits
2.60.40.2400, 1 hit
2.60.40.3200, 1 hit
2.60.40.350, 1 hit
2.60.40.4310, 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
IPR042304, Alphavir_E2_A
IPR042305, Alphavir_E2_B
IPR042306, Alphavir_E2_C
IPR000336, Flavivir/Alphavir_Ig-like_sf
IPR036253, Glycoprot_cen/dimer_sf
IPR038055, Glycoprot_E_dimer_dom
IPR014756, Ig_E-set
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P36329-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFPFQPMYPM QPMPYRNPFA APRRPWFPRT DPFLAMQVQE LTRSMANLTF 
        60         70         80         90        100
KQRREAPPEG PPAKKPKREA PQKQKGGGQG KKKKNQGKKK AKTGPPNPKA 
       110        120        130        140        150
QNGNKKKTNK KPGKRQRMVM KLESDKTFPI MLEGKINGYA CVVGGKLFRP 
       160        170        180        190        200
MHVEGKIDND VLAALKTKKA SKYDLEYADV PQNMRADTFK YTHEKPQGYY 
       210        220        230        240        250
SWHHGAVQYE NGRFTVPKGV GAKGDSGRPI LDNQGRVVAI VLGGVNEGSR 
       260        270        280        290        300
TALSVVMWNE KGVTVKYTPE NCEQWSLVTT MCLLANVTFP CAQPPICYDR 
       310        320        330        340        350
KPAETLAMLS VNVDNPGYDE LLEAAVKCPG RKRRSTEELF KEYKLTRPYM 
       360        370        380        390        400
ARCIRCAVGS CHSPIAIEAV KSDGHDGYVR LQTSSQYGLD SSGNLKGRTM 
       410        420        430        440        450
RYDMHGTIEE IPLHQVSLHT SRPCHIVDGH GYFLLARCPA GDSITMEFKK 
       460        470        480        490        500
DAVTHSCSVP YEVKFNPVGR ELYTHPPEHG AEQACQVYAH DAQNRGAYVE 
       510        520        530        540        550
MHLPGSEVDS SLVSLSGSSV TVTPPAGTSA LVECECGGTK ISETINTAKQ 
       560        570        580        590        600
FSQCTKKEQC RAYRLQNDKW VYNSDKLPKA AGATLKGKLH VPFLLADGKC 
       610        620        630        640        650
TVPLAPEPMI TFGFRSVSLK LHPKNPTYLT TRQLADEPHY THELISEPVV 
       660        670        680        690        700
RNFSVTEKGW EFVWGNHPPK RFWAQETAPG NPHGLPHEVI THYYHRYPMS 
       710        720        730        740        750
TILGLSICAA IVTVSIAAST WLLCKSRVSC LTPYRLTPNA RMPLCLAVLC 
       760        770        780        790        800
CARTARAETT WESLDHLWNN NQQMFWIQLL IPLAALIVVT RLLRCVCCVV 
       810        820        830        840        850
PFLVVAGAAG AGAYEHATTM PSQAGIPYNT IVNRAGYAPL PISITPTKIK 
       860        870        880        890        900
LIPTVNLEYV TCHYKTGMDS PAIKCCGSQE CTPTYRPDEQ CKVFTGVYPF 
       910        920        930        940        950
MWGGAYCFCD TENTQVSKAY VMKSDDCLAD HAEAYKAHTA SVQAFLNITV 
       960        970        980        990       1000
GEHSIVTTVY VNGETPVNFN GVKLTAGPLS TAWTPFDRKI VQYAGEIYNY 
      1010       1020       1030       1040       1050
DFPEYGAGQP GAFGDIQSRT VSSSDLYANT NLVLQRPKAG AIHVPYTQAP 
      1060       1070       1080       1090       1100
SGFEQWKKDK APSLKFTAPF GCEIYTNPIR AENCAVGSIP LAFDIPDALF 
      1110       1120       1130       1140       1150
TRVSETPTLS AAECTLNECV YSSDFGGIAT VKYSASKSGK CAVHVPSGTA 
      1160       1170       1180       1190       1200
TLKEAAIELA EQGSATIHFS TANIHPEFRL QICTSYVTCK GDCHPPKDHI 
      1210       1220       1230       1240       1250
VTHPQYHAQT FTAAVSKTAW TWLTSLLGGS AVIIIIGLVL ATIVAMYVLT 

NQKHN
Length:1,255
Mass (Da):138,298
Last modified:June 1, 1994 - 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:i7D730E17CAECA310
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L00930 Genomic RNA Translation: AAC19325.1

Protein sequence database of the Protein Information Resource

More...PIRi		D44213

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00930 Genomic RNA Translation: AAC19325.1
PIRiD44213

3D structure databases

SMRiP36329
ModBaseiSearch...

Protein family/group databases

MEROPSiS03.001

Family and domain databases

Gene3Di2.40.10.10, 2 hits
2.60.40.2400, 1 hit
2.60.40.3200, 1 hit
2.60.40.350, 1 hit
2.60.40.4310, 1 hit
2.60.98.10, 3 hits
InterProiView protein in InterPro
IPR002548, Alpha_E1_glycop
IPR000936, Alpha_E2_glycop
IPR002533, Alpha_E3_glycop
IPR042304, Alphavir_E2_A
IPR042305, Alphavir_E2_B
IPR042306, Alphavir_E2_C
IPR000336, Flavivir/Alphavir_Ig-like_sf
IPR036253, Glycoprot_cen/dimer_sf
IPR038055, Glycoprot_E_dimer_dom
IPR014756, Ig_E-set
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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_EEVV3
<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: P36329
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 25, 2022
This is version 127 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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