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Entry version 162 (16 Oct 2019)
Sequence version 2 (10 Apr 2019)
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Protein

Polyprotein P1234

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

Polyprotein P1234: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2.By similarity
Polyprotein P123: The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (PubMed:8107248, PubMed:7517863). Polyprotein P123 is a short-lived polyprotein that accumulates during early stage of infection (PubMed:8107248, PubMed:7517863). As soon P123 is cleaved into mature proteins, the plus-strand RNAs synthesis begins (PubMed:8107248, PubMed:7517863).2 Publications
Polyprotein P123': The early replication complex formed by the polyprotein P123' and nsP4 synthesizes minus-strand RNAs (Probable). Polyprotein P123' is a short-lived polyprotein that accumulates during early stage of infection (Probable). As soon P123' is cleaved into mature proteins, the plus-strand RNAs synthesis begins (Probable).2 Publications
mRNA-capping enzyme nsP1: Cytoplasmic capping enzyme that catalyzes two virus-specific reactions: methyltransferase and nsP1 guanylyltransferase (PubMed:7831320). mRNA-capping is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus (Probable). The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP (Probable). nsP1 capping consists in the following reactions: GTP is first methylated into 7-methyl-GMP and then is covalently linked to nsP1 to form the m7GMp-nsP1 complex from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure (Probable). NsP1 is needed for the initiation of the minus-strand RNAs synthesis (PubMed:1824787). Probably serves as a membrane anchor for the replication complex composed of nsP1-nsP4 (By similarity). Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell (By similarity).By similarityCurated2 Publications
Protease nsP2: Multifunctional protein whose N-terminus is part of the RNA polymerase complex and displays NTPase, RNA triphosphatase and helicase activities (By similarity). NTPase and RNA triphosphatase are involved in viral RNA capping and helicase keeps a check on the dsRNA replication intermediates (By similarity). The C-terminus harbors a protease that specifically cleaves the polyproteins and releases the mature proteins (By similarity). Required for the shutoff of minus-strand RNAs synthesis (PubMed:8627744). Specifically inhibits the host IFN response by promoting the nuclear export of host STAT1 (By similarity). Also inhibits host transcription by inducing rapid proteasome-dependent degradation of POLR2A, a catalytic subunit of the RNAPII complex (PubMed:22514352, PubMed:17108023, PubMed:30232189). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (Probable).By similarity1 Publication4 Publications
Non-structural protein 3: Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis (PubMed:8057460). Displays mono-ADP-ribosylhydrolase activity (PubMed:28150709). ADP-ribosylation is a post-translantional modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication (PubMed:28150709). Binds proteins of G3BP family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs (PubMed:18684830). The nsp3-G3BP complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of G3BP family members to self-assemble and bind DNA (By similarity).By similarity3 Publications
Non-structural protein 3': Seems to be essential for minus-strand RNAs and subgenomic 26S mRNAs synthesis (Probable). Displays mono-ADP-ribosylhydrolase activity (Probable). ADP-ribosylation is a post-translational modification that controls various processes of the host cell and the virus probably needs to revert it for optimal viral replication (Probable). Binds proteins of G3BP family and sequesters them into the viral RNA replication complexes thereby inhibiting the formation of host stress granules on viral mRNAs (Probable). The nsp3'-G3BP complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes, thanks to the ability of G3BP family members to self-assemble and bind DNA (By similarity).By similarity3 Publications
RNA-directed RNA polymerase nsP4: RNA dependent RNA polymerase (PubMed:8107248, PubMed:7517863, PubMed:19036396). Replicates genomic and antigenomic RNA by recognizing replications specific signals. The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (PubMed:8107248, PubMed:7517863, PubMed:2529379). The late replication complex composed of fully processed nsP1-nsP4 is responsible for the production of genomic and subgenomic plus-strand RNAs (PubMed:8107248, PubMed:7517863). The core catalytic domain of nsP4 also possesses terminal adenylyltransferase (TATase) activity that is probably involved in maintenance and repair of the poly(A) tail, an element required for replication of the viral genome (PubMed:17005674).5 Publications

Miscellaneous

Viral replication produces dsRNA in the late phase of infection, resulting in a strong activation of host EIF2AK2/PKR, leading to almost complete phosphorylation of EIF2A (PubMed:16391235). This inactivates completely cellular translation initiation, resulting shutoff of host proteins synthesis (PubMed:16391235). However, phosphorylation of EIF2A is probably not the only mechanism responsible for the host translation shutoff (PubMed:29419763). The viral translation can still occur normally because it relies on a hairpin structure in the coding region of sgRNA and is EIF2A-, EIF2D-, EIF4G- EIF4A-independent (PubMed:29419763).1 Publication1 Publication
The genome codes for P123, but readthrough of a terminator codon UGA occurs between the codons for Tyr-1896 and Leu-1898 giving rise to P1234 (PubMed:2521676). P1234 is cleaved quickly by nsP2 into P123' and nsP4 (By similarity). Further processing of p123' gives nsP1, nsP2 and nsP3' which is 6 amino acids longer than nsP3 since the cleavage site is after the readthrough (By similarity). This unusual molecular mechanism ensures that few nsP4 are produced compared to other non-structural proteins (By similarity). Mutant viruses with no alternative termination site grow significantly slower than wild-type virus (PubMed:2521676). The opal termination codon is frequently mutated to a sense codon on passage in cell culture (By similarity). The presence of the opal codon may be a requirement for viral maintenance in both vertebrate and invertebrate hosts and a selective advantage may be conferred in cell culture for the sense codon (By similarity).By similarity1 Publication

<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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 8.0-8.5 for nsP4 polymerase and adenylyltransferase activities.2 Publications

Temperature dependencei

Optimum temperature is 25 degrees Celsius for nsP4 adenylyltransferase activity.1 Publication

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>Sitei39Involved in the phosphoramide link with 7-methyl-GMPBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei1021For cysteine protease nsP2 activityPROSITE-ProRule annotation1
Active sitei1098For cysteine protease nsP2 activityPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1371ADP-riboseBy similarity1
Binding sitei1379ADP-riboseBy similarity1
Binding sitei1459ADP-riboseBy similarity1
Binding sitei1460ADP-riboseBy similarity1
Binding sitei1461ADP-riboseBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1610Zinc1 Publication1
Metal bindingi1612Zinc1 Publication1
Metal bindingi1635Zinc1 Publication1
Metal bindingi1653Zinc1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi726 – 733NTPPROSITE-ProRule annotation8

<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 functionHelicase, Hydrolase, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase
Biological processEukaryotic host gene expression shutoff by virus, Eukaryotic host transcription shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host RNA polymerase II by virus, Inhibition of host STAT1 by virus, mRNA capping, mRNA processing, Viral immunoevasion, Viral RNA replication
LigandATP-binding, GTP-binding, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine, Zinc

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C09.001

<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:
Polyprotein P1234
Short name:
P1234
Alternative name(s):
Non-structural polyprotein
p270 nonstructural polyprotein
Cleaved into the following 7 chains:
Polyprotein P123'
Short name:
P123'
Polyprotein P123
Short name:
P123
mRNA-capping enzyme nsP1 (EC:2.1.1.-By similarity, EC:2.7.7.-1 Publication)
Alternative name(s):
Non-structural protein 1
Protease nsP2 (EC:3.1.3.33By similarity, EC:3.4.22.-By similarity, EC:3.6.1.15By similarity, EC:3.6.4.13By similarity)
Alternative name(s):
Non-structural protein 2
Short name:
nsP2
Non-structural protein 3' (EC:3.1.3.84Curated)
Short name:
nsP3'
Non-structural protein 3 (EC:3.1.3.84By similarity)
Short name:
nsP3
RNA-directed RNA polymerase nsP4 (EC:2.7.7.191 Publication, EC:2.7.7.48PROSITE-ProRule annotation1 Publication)
Alternative name(s):
Non-structural protein 4
Short name:
nsP4
<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 lineageiVirusesRiboviriaTogaviridaeAlphavirus
<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

Polyprotein P1234 :
Polyprotein P123' :
Polyprotein P123 :
mRNA-capping enzyme nsP1 :
Protease nsP2 :
Non-structural protein 3 :
Non-structural protein 3' :
RNA-directed RNA polymerase nsP4 :

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host cell projection, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane

<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>Mutagenesisi39H → A: Complete loss of methyl transferase activity or viral infectivity. 1 Publication1
Mutagenesisi81H → A: Complete loss of methyl transferase activity or viral infectivity. 1 Publication1
Mutagenesisi91D → A: Complete loss of methyl transferase activity or viral infectivity. 1 Publication1
Mutagenesisi94R → A: Complete loss of methyl transferase activity or viral infectivity. 1 Publication1
Mutagenesisi249Y → A: Complete loss of methyl transferase activity or viral infectivity. 1 Publication1
Mutagenesisi369I → V: No effect on methyl transferase activity or viral infectivity. 1 Publication1
Mutagenesisi420C → A: Complete loss of palmitoylation. 1 Publication1
Mutagenesisi539G → A: Partial loss of polyprotein processing between nsp1 and nsp2. 1 Publication1
Mutagenesisi539G → E or V: Complete loss of polyprotein processing between nsp1 and nsp2. 1 Publication1
Mutagenesisi703E → K: No effect on the synthesis and processing of the polyproteins; blocks the conversion of the initial, short-lived minus-strand replicase complex (RCinitial) into the mature replicase and transcriptase complexes. 1 Publication1
Mutagenesisi815V → I: No effect on the synthesis and processing of the polyproteins; blocks the conversion of the initial, short-lived minus-strand replicase complex (RCinitial) into the mature replicase and transcriptase complexes. 1 Publication1
Mutagenesisi956L → S: No effect on the synthesis and processing of the polyproteins; blocks the conversion of the initial, short-lived minus-strand replicase complex (RCinitial) into the mature replicase and transcriptase complexes. 1 Publication1
Mutagenesisi1021C → A: Complete loss of nsP2 protease activity. 1 Publication1
Mutagenesisi1040C → W: NsP2 is only found in the nucleus. 1 Publication1
Mutagenesisi1098H → A: Complete loss of nsP2 protease activity. 1 Publication1
Mutagenesisi1099W → A: Complete loss of nsP2 protease activity. 1 Publication1
Mutagenesisi1159H → Q: Complete loss of nsP2-induced degradation of host POLR2A; no effect on nsP2 localization. 1 Publication1
Mutagenesisi1183H → Q: Complete loss of nsP2-induced degradation of host POLR2A; no effect on nsP2 localization. 1 Publication1
Mutagenesisi1223P → Q: NsP2 is only found in the nucleus. 1 Publication1
Mutagenesisi1224Q → P: Complete loss of nsP2-induced degradation of host POLR2A; NsP2 is only found in the nucleus. 1 Publication1
Mutagenesisi1266P → G or L: Complete loss of nsP2-induced degradation of host POLR2A, nsP2 is only found in the nucleus,. 2 Publications1
Mutagenesisi1346G → A: Partial loss of polyprotein processing between nsp2 and nsp3. 1 Publication1
Mutagenesisi1346G → E or V: Complete loss of polyprotein processing between nsp2 and nsp3. 1 Publication1
Mutagenesisi1610C → A: Complete loss of viral replication. 1 Publication1
Mutagenesisi1612C → A: Complete loss of viral replication. 1 Publication1
Mutagenesisi1635C → A: Complete loss of viral replication. 1 Publication1
Mutagenesisi1653C → A: Complete loss of viral replication. 1 Publication1
Mutagenesisi1896Y → YR, YS or YW: Reduces RNA synthesis in early phase of infection. 1 Publication1
Mutagenesisi1904Y → A: No effect on nsP4 cleavage. 1 Publication1
Mutagenesisi1904Y → C: Destabilizes nsP4. 1 Publication1
Mutagenesisi1904Y → E: Reduces nsP4 cleavage. 1 Publication1
Mutagenesisi1904Y → F: Destabilizes nsP4. 1 Publication1
Mutagenesisi1904Y → L: Reduces nsP4 cleavage and destabilizes nsP4. 1 Publication1
Mutagenesisi1904Y → M: Reduces nsP4 cleavage. 1 Publication1
Mutagenesisi1904Y → N: Reduces nsP4 cleavage. 1 Publication1
Mutagenesisi1904Y → P: Complete loss of nsP4 cleavage. 1 Publication1
Mutagenesisi1904Y → Q: Reduces nsP4 cleavage. 1 Publication1
Mutagenesisi1904Y → R: Destabilizes nsP4. 1 Publication1
Mutagenesisi1904Y → T: Reduces nsP4 cleavage. 1 Publication1
Mutagenesisi2368 – 2369DD → AA: Complete loss of RNA-directed RNA polymerase activity. 1 Publication2

<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_00003084051 – 2513Polyprotein P1234Add BLAST2513
ChainiPRO_00002277711 – 1903Polyprotein P123'Add BLAST1903
ChainiPRO_00002277721 – 1896Polyprotein P123Add BLAST1896
ChainiPRO_00000412361 – 540mRNA-capping enzyme nsP1Add BLAST540
ChainiPRO_0000041237541 – 1347Protease nsP2Add BLAST807
ChainiPRO_00000412381348 – 1903Non-structural protein 3'Add BLAST556
ChainiPRO_00002277731348 – 1896Non-structural protein 3Add BLAST549
ChainiPRO_00000412391904 – 2513RNA-directed RNA polymerase nsP4Add BLAST610

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(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi420S-palmitoyl cysteine; by host1 Publication1

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

Polyprotein P1234: Specific enzymatic cleavages in vivo yield mature proteins (PubMed:2142454, PubMed:8107248). The processing of the polyprotein is temporally regulated (PubMed:2142454). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123' and nsP4, which associate to form the early replication complex (PubMed:2142454, PubMed:8107248) (Probable). At the same time, P1234 is also cut at the nsP1/nsP2 site early in infection but with lower efficiency (PubMed:2142454). After replication of the viral minus-strand RNAs (4 hpi), the polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very efficiently, preventing accumulation of P123' and P1234 and allowing the formation of the late replication complex (PubMed:2142454, PubMed:8107248) (Probable). NsP3'/nsP4 site is not cleaved anymore and P34 is produced rather than nsP4 (PubMed:2142454).1 Publication2 Publications
Polyprotein P123: Specific enzymatic cleavages in vivo yield mature proteins (PubMed:2142454, PubMed:2529379, PubMed:2141206, PubMed:8107248). The processing of the polyprotein is temporally regulated (PubMed:2142454). In early stages (1.7 hpi), P123 is cleaved at the nsP1/nsP2 site with low efficiency (PubMed:2142454). After replication of the viral minus-strand RNAs (4 hpi), the polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very efficiently, preventing accumulation of P123 and allowing the formation of the late replication complex (PubMed:2142454).4 Publications
Polyprotein P123': Specific enzymatic cleavages in vivo yield mature proteins (Probable). The processing of the polyprotein is temporally regulated (Probable). In early stages (1.7 hpi), P123' is cleaved at the nsP1/nsP2 site with low efficiency (Probable). After replication of the viral minus-strand RNAs (4 hpi), the polyproteins are cut at the nsP1/nsP2 and nsP2/nsP3 sites very efficiently, preventing accumulation of P123' and allowing the formation of the late replication complex (Probable).5 Publications
mRNA-capping enzyme nsP1: Palmitoylated by host palmitoyltransferases ZDHHC2 and ZDHHC19.By similarity
Non-structural protein 3: Phosphorylated by host on serines and threonines.By similarity
Non-structural protein 3': Phosphorylated by host on serines and threonines.By similarity
RNA-directed RNA polymerase nsP4: ubiquitinated; targets the protein for rapid degradation via the ubiquitin system (PubMed:1924357). Nsp4 is present in extremely low quantities due to low frequency of translation through the amber stop-codon and the degradation by the ubiquitin pathway (PubMed:1924357).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei540 – 541Cleavage; by protease nsP21 Publication2
Sitei1347 – 1348Cleavage; by protease nsP21 Publication2
Sitei1903 – 1904Cleavage; by protease nsP2By similarity2

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P03317

PTM databases

SwissPalm database of S-palmitoylation events

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SwissPalmi
P03317

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P03317

<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

mRNA-capping enzyme nsP1:

Interacts with non-structural protein 3 (By similarity). Non-structural protein 3:

Interacts with mRNA-capping enzyme nsP1 (By similarity). mRNA-capping enzyme nsP1:

Interacts with RNA-directed RNA polymerase nsP4 (By similarity). RNA-directed RNA polymerase nsP4:

Interacts with mRNA-capping enzyme nsP1 (By similarity). RNA-directed RNA polymerase nsP4:

Interacts with protease nsP2 (By similarity). Protease nsP2:

Interacts with RNA-directed RNA polymerase nsP4 (By similarity). mRNA-capping enzyme nsP1:

Interacts with protease nsP2 (By similarity). Protease nsP2:

Interacts with mRNA-capping enzyme nsP1 (By similarity). RNA-directed RNA polymerase nsP4 interacts with itself (By similarity). mRNA-capping enzyme nsP1 interacts with itself (By similarity). Protease nsP2:

Interacts with KPNA1/karyopherin-alpha1; this interaction probably allows the active transport of protease nsP2 into the host nucleus (By similarity). Non-structural protein 3:

Interacts with host DDX1 (By similarity). Non-structural protein 3:

Interacts with host DDX3 (By similarity). Non-structural protein 3:

Interacts (via C-terminus) with host G3BP1; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-G3BP1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (PubMed:18684830). Non-structural protein 3:

Interacts (via C-terminus) with host G3BP2; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-G3BP2 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (PubMed:18684830).

By similarity1 Publication

Protein-protein interaction databases

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P03317

<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

12513
Legend: HelixTurnBeta strandPDB Structure known for this area
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3D structure databases

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

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SMRi
P03317

Database of comparative protein structure models

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ModBasei
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Protein Data Bank in Europe - Knowledge Base

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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_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>Domaini30 – 260Alphavirus-like MTPROSITE-ProRule annotationAdd BLAST231
Domaini695 – 850(+)RNA virus helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST156
Domaini851 – 999(+)RNA virus helicase C-terminalPROSITE-ProRule annotationAdd BLAST149
Domaini1012 – 1341Peptidase C9PROSITE-ProRule annotationAdd BLAST330
Domaini1348 – 1507MacroPROSITE-ProRule annotationAdd BLAST160
Domaini2267 – 2382RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

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>Regioni245 – 264NsP1 membrane-bindingBy similarityAdd BLAST20
Regioni1013 – 1032Nucleolus localization signalBy similarityAdd BLAST20

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>Motifi1066 – 1075Nuclear export signalBy similarity10
Motifi1196 – 1200Nuclear localization signalBy similarity5
Motifi1837 – 1840FGDF; binding to host G3BP1By similarity4
Motifi1860 – 1863FGDF; binding to host G3BP1By similarity4

<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

Protease nsP2: The N-terminus exhibits NTPase and RNA triphosphatase activities and is proposed to have helicase activity, whereas the C-terminus possesses protease activity (By similarity). Contains a nuclear localization signal and a nuclear export signal, these two motifs are probably involved in the shuttling between the cytoplasm and the nucleus of nsP2 (By similarity). The C-terminus is required for promoting the export of host STAT1 (By similarity).By similarity
Non-structural protein 3: In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (PubMed:28150709). The central part has a zinc-binding function (PubMed:23010928). The C-terminus contains two FGDF motifs necessary and sufficient for formation of the nsP3/G3BP1 complex (By similarity).By similarity2 Publications
Non-structural protein 3': In the N-terminus, the macro domain displays a mono-ADP-ribosylhydrolase activity (Probable). The central part has a zinc-binding function (Probable). The C-terminus contains two FGDF motifs necessary and sufficient for formation of the nsP3'/G3BP1 complex (By similarity).By similarity2 Publications

Phylogenomic databases

Database of Orthologous Groups

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OrthoDBi
37at10239

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR027351 (+)RNA_virus_helicase_core_dom
IPR002588 Alphavirus-like_MT_dom
IPR002620 Alphavirus_nsp2pro
IPR002589 Macro_dom
IPR027417 P-loop_NTPase
IPR007094 RNA-dir_pol_PSvirus
IPR029063 SAM-dependent_MTases
IPR001788 Tymovirus_RNA-dep_RNA_pol

Pfam protein domain database

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Pfami
View protein in Pfam
PF01661 Macro, 1 hit
PF01707 Peptidase_C9, 1 hit
PF00978 RdRP_2, 1 hit
PF01443 Viral_helicase1, 1 hit
PF01660 Vmethyltransf, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00506 A1pp, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 1 hit
SSF53335 SSF53335, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51743 ALPHAVIRUS_MT, 1 hit
PS51154 MACRO, 1 hit
PS51520 NSP2PRO, 1 hit
PS51657 PSRV_HELICASE, 1 hit
PS50507 RDRP_SSRNA_POS, 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>. 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_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.

P03317-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEKPVVNVDV DPQSPFVVQL QKSFPQFEVV AQQVTPNDHA NARAFSHLAS
60 70 80 90 100
KLIELEVPTT ATILDIGSAP ARRMFSEHQY HCVCPMRSPE DPDRMMKYAS
110 120 130 140 150
KLAEKACKIT NKNLHEKIKD LRTVLDTPDA ETPSLCFHND VTCNMRAEYS
160 170 180 190 200
VMQDVYINAP GTIYHQAMKG VRTLYWIGFD TTQFMFSAMA GSYPAYNTNW
210 220 230 240 250
ADEKVLEARN IGLCSTKLSE GRTGKLSIMR KKELKPGSRV YFSVGSTLYP
260 270 280 290 300
EHRASLQSWH LPSVFHLNGK QSYTCRCDTV VSCEGYVVKK ITISPGITGE
310 320 330 340 350
TVGYAVTHNS EGFLLCKVTD TVKGERVSFP VCTYIPATIC DQMTGIMATD
360 370 380 390 400
ISPDDAQKLL VGLNQRIVIN GRTNRNTNTM QNYLLPIIAQ GFSKWAKERK
410 420 430 440 450
DDLDNEKMLG TRERKLTYGC LWAFRTKKVH SFYRPPGTQT CVKVPASFSA
460 470 480 490 500
FPMSSVWTTS LPMSLRQKLK LALQPKKEEK LLQVSEELVM EAKAAFEDAQ
510 520 530 540 550
EEARAEKLRE ALPPLVADKG IEAAAEVVCE VEGLQADIGA ALVETPRGHV
560 570 580 590 600
RIIPQANDRM IGQYIVVSPN SVLKNAKLAP AHPLADQVKI ITHSGRSGRY
610 620 630 640 650
AVEPYDAKVL MPAGGAVPWP EFLALSESAT LVYNEREFVN RKLYHIAMHG
660 670 680 690 700
PAKNTEEEQY KVTKAELAET EYVFDVDKKR CVKKEEASGL VLSGELTNPP
710 720 730 740 750
YHELALEGLK TRPAVPYKVE TIGVIGTPGS GKSAIIKSTV TARDLVTSGK
760 770 780 790 800
KENCREIEAD VLRLRGMQIT SKTVDSVMLN GCHKAVEVLY VDEAFACHAG
810 820 830 840 850
ALLALIAIVR PRKKVVLCGD PMQCGFFNMM QLKVHFNHPE KDICTKTFYK
860 870 880 890 900
YISRRCTQPV TAIVSTLHYD GKMKTTNPCK KNIEIDITGA TKPKPGDIIL
910 920 930 940 950
TCFRGWVKQL QIDYPGHEVM TAAASQGLTR KGVYAVRQKV NENPLYAITS
960 970 980 990 1000
EHVNVLLTRT EDRLVWKTLQ GDPWIKQPTN IPKGNFQATI EDWEAEHKGI
1010 1020 1030 1040 1050
IAAINSPTPR ANPFSCKTNV CWAKALEPIL ATAGIVLTGC QWSELFPQFA
1060 1070 1080 1090 1100
DDKPHSAIYA LDVICIKFFG MDLTSGLFSK QSIPLTYHPA DSARPVAHWD
1110 1120 1130 1140 1150
NSPGTRKYGY DHAIAAELSR RFPVFQLAGK GTQLDLQTGR TRVISAQHNL
1160 1170 1180 1190 1200
VPVNRNLPHA LVPEYKEKQP GPVKKFLNQF KHHSVLVVSE EKIEAPRKRI
1210 1220 1230 1240 1250
EWIAPIGIAG ADKNYNLAFG FPPQARYDLV FINIGTKYRN HHFQQCEDHA
1260 1270 1280 1290 1300
ATLKTLSRSA LNCLNPGGTL VVKSYGYADR NSEDVVTALA RKFVRVSAAR
1310 1320 1330 1340 1350
PDCVSSNTEM YLIFRQLDNS RTRQFTPHHL NCVISSVYEG TRDGVGAAPS
1360 1370 1380 1390 1400
YRTKRENIAD CQEEAVVNAA NPLGRPGEGV CRAIYKRWPT SFTDSATETG
1410 1420 1430 1440 1450
TARMTVCLGK KVIHAVGPDF RKHPEAEALK LLQNAYHAVA DLVNEHNIKS
1460 1470 1480 1490 1500
VAIPLLSTGI YAAGKDRLEV SLNCLTTALD RTDADVTIYC LDKKWKERID
1510 1520 1530 1540 1550
AALQLKESVT ELKDEDMEID DELVWIHPDS CLKGRKGFST TKGKLYSYFE
1560 1570 1580 1590 1600
GTKFHQAAKD MAEIKVLFPN DQESNEQLCA YILGETMEAI REKCPVDHNP
1610 1620 1630 1640 1650
SSSPPKTLPC LCMYAMTPER VHRLRSNNVK EVTVCSSTPL PKHKIKNVQK
1660 1670 1680 1690 1700
VQCTKVVLFN PHTPAFVPAR KYIEVPEQPT APPAQAEEAP EVVATPSPST
1710 1720 1730 1740 1750
ADNTSLDVTD ISLDMDDSSE GSLFSSFSGS DNSITSMDSW SSGPSSLEIV
1760 1770 1780 1790 1800
DRRQVVVADV HAVQEPAPIP PPRLKKMARL AAARKEPTPP ASNSSESLHL
1810 1820 1830 1840 1850
SFGGVSMSLG SIFDGETARQ AAVQPLATGP TDVPMSFGSF SDGEIDELSR
1860 1870 1880 1890 1900
RVTESEPVLF GSFEPGEVNS IISSRSAVSF PLRKQRRRRR SRRTEYXLTG
1910 1920 1930 1940 1950
VGGYIFSTDT GPGHLQKKSV LQNQLTEPTL ERNVLERIHA PVLDTSKEEQ
1960 1970 1980 1990 2000
LKLRYQMMPT EANKSRYQSR KVENQKAITT ERLLSGLRLY NSATDQPECY
2010 2020 2030 2040 2050
KITYPKPLYS SSVPANYSDP QFAVAVCNNY LHENYPTVAS YQITDEYDAY
2060 2070 2080 2090 2100
LDMVDGTVAC LDTATFCPAK LRSYPKKHEY RAPNIRSAVP SAMQNTLQNV
2110 2120 2130 2140 2150
LIAATKRNCN VTQMRELPTL DSATFNVECF RKYACNDEYW EEFARKPIRI
2160 2170 2180 2190 2200
TTEFVTAYVA RLKGPKAAAL FAKTYNLVPL QEVPMDRFVM DMKRDVKVTP
2210 2220 2230 2240 2250
GTKHTEERPK VQVIQAAEPL ATAYLCGIHR ELVRRLTAVL LPNIHTLFDM
2260 2270 2280 2290 2300
SAEDFDAIIA EHFKQGDPVL ETDIASFDKS QDDAMALTGL MILEDLGVDQ
2310 2320 2330 2340 2350
PLLDLIECAF GEISSTHLPT GTRFKFGAMM KSGMFLTLFV NTVLNVVIAS
2360 2370 2380 2390 2400
RVLEERLKTS RCAAFIGDDN IIHGVVSDKE MAERCATWLN MEVKIIDAVI
2410 2420 2430 2440 2450
GERPPYFCGG FILQDSVTST ACRVADPLKR LFKLGKPLPA DDEQDEDRRR
2460 2470 2480 2490 2500
ALLDETKAWF RVGITGTLAV AVTTRYEVDN ITPVLLALRT FAQSKRAFQA
2510
IRGEIKHLYG GPK
Length:2,513
Mass (Da):279,661
Last modified:April 10, 2019 - v2
<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:i8561459691FD395C
GO

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
J02363 Genomic RNA Translation: AAA96974.1
J02363 Genomic RNA Translation: AAA96975.1 Sequence problems.

Protein sequence database of the Protein Information Resource

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PIRi
A03917 MNWVS

NCBI Reference Sequences

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RefSeqi
NP_062888.1, NC_001547.1
NP_062889.1, NC_001547.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
1502153
1502154

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
vg:1502153
vg:1502154

Keywords - Coding sequence diversityi

RNA suppression of termination

<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
J02363 Genomic RNA Translation: AAA96974.1
J02363 Genomic RNA Translation: AAA96975.1 Sequence problems.
PIRiA03917 MNWVS
RefSeqiNP_062888.1, NC_001547.1
NP_062889.1, NC_001547.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GUAX-ray2.85A/B/C1011-1675[»]
SMRiP03317
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

ELMiP03317

Protein family/group databases

MEROPSiC09.001

PTM databases

SwissPalmiP03317

Proteomic databases

PRIDEiP03317

Genome annotation databases

GeneIDi1502153
1502154
KEGGivg:1502153
vg:1502154

Phylogenomic databases

OrthoDBi37at10239

Miscellaneous databases

PMAP-CutDBiP03317

Family and domain databases

InterProiView protein in InterPro
IPR027351 (+)RNA_virus_helicase_core_dom
IPR002588 Alphavirus-like_MT_dom
IPR002620 Alphavirus_nsp2pro
IPR002589 Macro_dom
IPR027417 P-loop_NTPase
IPR007094 RNA-dir_pol_PSvirus
IPR029063 SAM-dependent_MTases
IPR001788 Tymovirus_RNA-dep_RNA_pol
PfamiView protein in Pfam
PF01661 Macro, 1 hit
PF01707 Peptidase_C9, 1 hit
PF00978 RdRP_2, 1 hit
PF01443 Viral_helicase1, 1 hit
PF01660 Vmethyltransf, 1 hit
SMARTiView protein in SMART
SM00506 A1pp, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51743 ALPHAVIRUS_MT, 1 hit
PS51154 MACRO, 1 hit
PS51520 NSP2PRO, 1 hit
PS51657 PSRV_HELICASE, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiPOLN_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: P03317
Secondary accession number(s): Q87644
<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: April 10, 2019
Last modified: October 16, 2019
This is version 162 of the entry and version 2 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, Reference proteome

Documents

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