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Entry version 120 (12 Aug 2020)
Sequence version 1 (01 Aug 1992)
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Protein

Structural polyprotein

Gene
N/A
Organism
Eastern equine encephalitis virus (strain va33[ten broeck]) (EEEV) (Eastern equine encephalomyelitis virus)
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

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 (PubMed:30540945). 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 (By similarity). 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). 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. 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 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.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 sitei137Charge relay systemPROSITE-ProRule annotation1
Active sitei159Charge 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>Sitei185Involved in dimerization of the capsid proteinBy similarity1
Active sitei211Charge relay systemPROSITE-ProRule annotation1
Sitei218Involved 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 processEukaryotic 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 entry into host cell

<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
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%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>OrganismiEastern equine encephalitis virus (strain va33[ten broeck]) (EEEV) (Eastern equine encephalomyelitis virus)
<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 identifieri11022 [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 lineageiVirusesRiboviriaOrthornaviraeKitrinoviricotaAlsuviricetesMartelliviralesTogaviridaeAlphavirus
<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 hostiAedes [TaxID: 7158]
Homo sapiens (Human) [TaxID: 9606]
Passeriformes [TaxID: 9126]

<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 domaini261 – 682ExtracellularSequence analysisAdd BLAST422
<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>Transmembranei683 – 703HelicalSequence analysisAdd BLAST21
Topological domaini704 – 743CytoplasmicSequence analysisAdd BLAST40
Topological domaini744 – 758ExtracellularSequence analysisAdd BLAST15
Transmembranei759 – 779HelicalSequence analysisAdd BLAST21
Topological domaini780CytoplasmicSequence analysis1
Transmembranei781 – 801HelicalSequence analysisAdd BLAST21
Topological domaini802 – 1216ExtracellularSequence analysisAdd BLAST415
Transmembranei1217 – 1237HelicalSequence analysisAdd BLAST21
Topological domaini1238 – 1240CytoplasmicSequence analysis3

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cell membrane, Host cytoplasm, Host membrane, Host nucleus, Membrane, T=4 icosahedral capsid 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_00000412461 – 260Capsid proteinBy similarityAdd BLAST260
ChainiPRO_0000234317261 – 743Precursor of protein E3/E2By similarityAdd BLAST483
ChainiPRO_0000041247261 – 323Assembly protein E3By similarityAdd BLAST63
ChainiPRO_0000041248324 – 743Spike glycoprotein E2By similarityAdd BLAST420
ChainiPRO_0000041249744 – 7996K proteinBy similarityAdd BLAST56
ChainiPRO_0000041250800 – 1240Spike glycoprotein E1By similarityAdd BLAST441

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>Glycosylationi49N-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 residuei109PhosphoserineBy similarity1
Modified residuei112PhosphothreonineBy similarity1
Glycosylationi271N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi638N-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>Lipidationi706S-palmitoyl cysteine; by hostSequence analysis1
Lipidationi716S-palmitoyl cysteine; by hostBy similarity1
Lipidationi736S-palmitoyl cysteine; by hostBy similarity1
Lipidationi737S-palmitoyl cysteine; by hostBy similarity1
Glycosylationi834N-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 bondi848 ↔ 913By similarity
Disulfide bondi861 ↔ 893By similarity
Disulfide bondi862 ↔ 895By similarity
Disulfide bondi867 ↔ 877By similarity
Glycosylationi933N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi1059 ↔ 1071By similarity
Disulfide bondi1101 ↔ 1176By similarity
Disulfide bondi1106 ↔ 1180By 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
Sitei260 – 261Cleavage; by autolysisBy similarity2
Sitei323 – 324Cleavage; by host furinBy similarity2
Sitei743 – 744Cleavage; by host signal peptidaseBy similarity2
Sitei799 – 800Cleavage; by host signal peptidaseBy similarity2

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P27284

<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).

By similarity

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

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 (By similarity). 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).

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).

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
P27284

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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>Domaini111 – 260Peptidase 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 – 35Necessary for nucleocapsid assembly and virus assemblyBy similarityAdd BLAST35
Regioni36 – 69Host transcription inhibitionBy similarityAdd BLAST34
Regioni82 – 112Binding to the viral RNA1 PublicationAdd BLAST31
Regioni97 – 111Ribosome-binding1 PublicationAdd BLAST15
Regioni261 – 272Functions as an uncleaved signal peptide for the precursor of protein E3/E2By similarityAdd BLAST12
Regioni715 – 735Transient transmembrane before p62-6K protein processingSequence analysisAdd BLAST21
Regioni883 – 900E1 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>Motifi43 – 50Supraphysiological nuclear export signalBy similarity8
Motifi66 – 70Nuclear localization signalBy similarity5

<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
2.60.98.10, 3 hits
3.30.1490.280, 1 hit

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.

P27284-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFPYPTLNYP PMAPINPMAY RDPNPPRQVA PFRPPLAAQI EDLRRSIANL
60 70 80 90 100
TLKQRAPNPP AGPPAKRKKP APKPKPAQAK KKRPPPPAKK QKRKPKPGKR
110 120 130 140 150
QRMCMKLESD KTFPIMLNGQ VNGYACVVGG RVFKPLHVEG RIDNEQLAAI
160 170 180 190 200
KLKKASIYDL EYGDVPQCMK SDTLQYTSDK PPGFYNWHHG AVQYENNRFT
210 220 230 240 250
VPRGVGGKGD SGRPILDNKG RVVAIVLGGV NEGSRTALSV VTWNQKGVTV
260 270 280 290 300
KDTPEGSEPW SLATVMCVLA NITFPCDQPP CMPCCYEKNP HETLTMLEQN
310 320 330 340 350
YDSRAYDQLL DAAVKCNARR TRRDLDTHFT QYKLARPYIA DCPNCGHSRC
360 370 380 390 400
DSPIAIEEVR GDAHAGVIRI QTSAMFGLKT DGVDLAYMSF MNGKTQKSIK
410 420 430 440 450
IDNLHVRTSA PCSLVSHHGY YILAQCPPGD TVTVGFHDGP NRHTCTVAHK
460 470 480 490 500
VEFRPVGREK YRHPPEHGVE LPCNRYTHKR ADQGHYVEMH QPGLVADHSL
510 520 530 540 550
LSIHSAKVKI TVPSGAQVKY YCKCPDVREG ITSSDHTTTC TDVKQCRAYL
560 570 580 590 600
IGNKKWVYNS GRLPRGEGDT FKGKLHVPFV PVKAKCIATL APEPLVEHKH
610 620 630 640 650
RTLILHLHPD HPTLLTTRSL GSDANPTRQW IERPTTVNFT VTGEGLEYTW
660 670 680 690 700
GNHPPKRVWA QESGEGNPHG WPHEVVVYYY NRYPLTTIIG LCTCVAIIMV
710 720 730 740 750
SCVHPCGSFA GLRNLCITPY KLAPNAQVPI LLALLCCIKP TRADDTLQVL
760 770 780 790 800
NYLWNNNQNF FWMQTLIPLA ALIVCMRIVR CLFCCGPAFL LVCGAWAAAY
810 820 830 840 850
EHTAVMPNKV GIPYKALVER PGYAPVHLQI QLVNTSIIPS TNLEYITCKY
860 870 880 890 900
KTKVPSPVVK CCGATQCTSK PHPDYQCQVF TGVYPFMWGG AYCFCDTENT
910 920 930 940 950
QMSEAYVERS EECSIDHAKA YKVHTGTVQA MVNITYGSVS WRSADVYVNG
960 970 980 990 1000
ETPAKIGDAK LIIGPLSSAW SPFDNKVVVY GHEVYNYDFP EYGTGKAGSF
1010 1020 1030 1040 1050
GDLQSRTSTS NDLYANTNLK LQRPQAGIVH TPFTQAPSGF ERWKRDKGAP
1060 1070 1080 1090 1100
LNDVAPFGCS IALEPLRAEN CAVGSIPISI DIPDAAFTRI SETPTVSDLE
1110 1120 1130 1140 1150
CKITECTYAS DFGGIATLPT NPVKQETVQF ILHQVLQLLK RMTSPLLRAG
1160 1170 1180 1190 1200
SFTFHFSTAN IHPAFKLQVC TSGVTCKGDC KPPKDHIVDY PAQHTESFTS
1210 1220 1230 1240
AISATAWSWL KVLVGGTSAF IVLGLIATAV VALVLFFHRH
Length:1,240
Mass (Da):137,291
Last modified:August 1, 1992 - 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:iAEBEB1599D083045
GO

Sequence databases

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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
M69094 Genomic RNA Translation: AAA42980.1

Protein sequence database of the Protein Information Resource

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PIRi
A39992, VHWVEV

<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
M69094 Genomic RNA Translation: AAA42980.1
PIRiA39992, VHWVEV

3D structure databases

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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
6MX4electron microscopy4.40C/F/I/L1-260[»]
6MX7electron microscopy4.80C/F/I/L1-260[»]
SMRiP27284
ModBaseiSearch...
PDBe-KBiSearch...

Proteomic databases

PRIDEiP27284

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
2.60.98.10, 3 hits
3.30.1490.280, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_EEEV3
<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: P27284
<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: August 1, 1992
Last sequence update: August 1, 1992
Last modified: August 12, 2020
This is version 120 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

Documents

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