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Entry version 195 (26 Feb 2020)
Sequence version 1 (21 Jul 1986)
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Protein

Genome polyprotein

Gene
N/A
Organism
Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O) (FMDV)
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

Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Cleaves also the host translation initiation factors EIF4G1 and EIF4G3, in order to shutoff the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechanisms. Possesses a deubiquitinase activity acting on both 'Lys'-48 and 'Lys'-63-linked polyubiquitin chains. In turn, inhibits the ubiquitination and subsequent activation of key signaling molecules of type I IFN response such as host DDX58, TBK1, TRAF3 and TRAF6. Inhibits host NF-kappa-B activity by inducing a decrease in RELA mRNA levels. Cleaves a peptide bond in the C-terminus of host ISG15, resulting in the damaging of this mofidier that can no longer be attached to target proteins. Cleaves also host G3BP1 and G3BP2 in order to inhibit cytoplasmic stress granules assembly.By similarity6 Publications
Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm. After genome has been released, the channel shrinks.By similarity
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP1 and VP3. The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome.1 Publication
Capsid protein V1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome. Mediates cell entry by attachment to an integrin receptor, usually host ITGAV/ITGB6, via a conserved arginine-glycine-aspartic acid (R-G-D) motif.4 Publications
Capsid protein V3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP0 and VP3. The capsid is composed of 60 copies of each capsid protein organized in the form of twelve pentamers and encloses the viral positive strand RNA genome.1 Publication
Mediates self-processing of the polyprotein by a translational effect termed 'ribosome skipping'. Mechanistically, 2A-mediated cleavage occurs between the C-terminal glycine and the proline of the downstream protein 2B. In the case of foot-and-mouth disease virus, the 2A oligopeptide is post-translationally 'trimmed' from the C-terminus of the upstream protein 1D by 3C proteinase.1 Publication
Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.1 Publication
Associates with and induces structural rearrangements of intracellular membranes. Triggers host autophagy by interacting with host BECN1 and thereby promotes viral replication. Participates in viral replication and interacts with host DHX9. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.4 Publications
Plays important roles in virus replication, virulence and host range.2 Publications
Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.1 Publication
Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.1 Publication
Covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. Acts as a genome-linked replication primer.1 Publication
Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, binds to viral RNA and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease.1 Publication
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated.PROSITE-ProRule annotation1 Publication

Miscellaneous

contains the main antigenic determinants of the virion; therefore, changes in its sequence must be responsible for the high antigenic variability of the virus.

<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

  • Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-. EC:3.4.22.46
  • Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.PROSITE-ProRule annotation EC:3.4.22.28

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 sitei51For leader protease activity1
Active sitei148For leader protease activity1
Active sitei163For leader protease activity1
Active sitei1695For protease 3C activity; Proton donor/acceptorPROSITE-ProRule annotation1
Active sitei1733For protease 3C activityPROSITE-ProRule annotation1
Active sitei1812For protease 3C activityPROSITE-ProRule annotation1
Active sitei2200For RdRp activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi1217 – 1224ATPPROSITE-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, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel
Biological processClathrin- and caveolin-independent endocytosis of virus by host, Clathrin-mediated endocytosis of virus by host, Host-virus interaction, Ion transport, Modulation of host chromatin by virus, Translation regulation, Transport, Viral attachment to host cell, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.22.46 2315

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C03.008

Transport Classification Database

More...
TCDBi
1.A.85.1.8 the poliovirus 2b viroporin (2b viroporin) family

UniLectin database of carbohydrate-binding proteins

More...
UniLectini
P03305

<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:
Genome polyprotein
Cleaved into the following 15 chains:
Leader protease (EC:3.4.22.461 Publication)
Short name:
Lb(pro)
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Virion protein 4
Alternative name(s):
P1B
Virion protein 2
Alternative name(s):
P1C
Virion protein 3
Alternative name(s):
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Alternative name(s):
P52
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3A
Short name:
P3A
Protein 3B-1
Short name:
P3B-1
Alternative name(s):
Genome-linked protein VPg1
Protein 3B-2
Short name:
P3B-2
Alternative name(s):
Genome-linked protein VPg2
Protein 3B-3
Short name:
P3B-3
Alternative name(s):
Genome-linked protein VPg3
Protease 3C (EC:3.4.22.281 Publication)
Alternative name(s):
Picornain 3C
Short name:
P3C
Protease P20B
RNA-directed RNA polymerase 3D-POL (EC:2.7.7.48)
Short name:
P3D-POL
Alternative name(s):
P56A
<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>OrganismiFoot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O) (FMDV)
<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 identifieri73482 [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 lineageiVirusesRiboviriaPicornaviralesPicornaviridaeAphthovirus
<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]
Capra hircus (Goat) [TaxID: 9925]
Cervidae (deer) [TaxID: 9850]
Erinaceidae (hedgehogs) [TaxID: 9363]
Loxodonta africana (African elephant) [TaxID: 9785]
Ovis aries (Sheep) [TaxID: 9940]
Rattus norvegicus (Rat) [TaxID: 10116]
Sus scrofa (Pig) [TaxID: 9823]
<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
  • UP000008765 <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 domaini1 – 1480CytoplasmicSequence analysisAdd BLAST1480
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei1481 – 1501Sequence analysisAdd BLAST21
Topological domaini1502 – 2332CytoplasmicSequence analysisAdd BLAST831

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host endoplasmic reticulum, Host membrane, Host nucleus, Membrane, T=pseudo3 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_00000398721 – 2332Genome polyproteinAdd BLAST2332
ChainiPRO_00000398731 – 201Leader proteaseAdd BLAST201
ChainiPRO_0000374076202 – 504Capsid protein VP0Sequence analysisAdd BLAST303
ChainiPRO_0000039876202 – 286Capsid protein VP4Sequence analysisAdd BLAST85
ChainiPRO_0000039877287 – 504Capsid protein VP2Sequence analysisAdd BLAST218
ChainiPRO_0000039878505 – 724Capsid protein VP3Sequence analysisAdd BLAST220
ChainiPRO_0000039879725 – 935Capsid protein VP1Add BLAST211
ChainiPRO_0000039880936 – 953Protein 2ASequence analysisAdd BLAST18
ChainiPRO_0000310976954 – 1107Protein 2BSequence analysisAdd BLAST154
ChainiPRO_00000398811108 – 1425Protein 2CSequence analysisAdd BLAST318
ChainiPRO_00000398821426 – 1578Protein 3ASequence analysisAdd BLAST153
ChainiPRO_00000398831579 – 1601Protein 3B-1Sequence analysisAdd BLAST23
ChainiPRO_00003109771602 – 1625Protein 3B-2Sequence analysisAdd BLAST24
ChainiPRO_00003109781626 – 1649Protein 3B-3Sequence analysisAdd BLAST24
ChainiPRO_00000398841650 – 1862Protease 3CSequence analysisAdd BLAST213
ChainiPRO_00000398851863 – 2332RNA-directed RNA polymerase 3D-POLSequence analysisAdd BLAST470

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(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi202N-myristoyl glycine; 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 bondi406 ↔ 858Interchain (between VP2 and VP1 chains)
Disulfide bondi511Interchain; in VP3 dimer
<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 residuei1581O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1604O-(5'-phospho-RNA)-tyrosineBy similarity1
Modified residuei1628O-(5'-phospho-RNA)-tyrosineBy similarity1

<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

Removes six residues from its own C-terminus, generating sLb(pro).1 Publication
Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond. This process would release the L-P1-2A peptide from the translational complex.1 Publication
During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and is followed by a conformational change of the particle.By similarity
Myristoylation is required during RNA encapsidation and formation of the mature virus particle.By similarity
Uridylylated by the polymerase and are covalently linked to the 5'-end of genomic RNA. These uridylylated forms act as a nucleotide-peptide primer for the polymerase.1 Publication
Uridylylated by the polymerase and are covalently linked to the 5'-end of genomic RNA. These uridylylated forms act as a nucleotide-peptide primer for the polymerase.1 Publication
Uridylylated by the polymerase and are covalently linked to the 5'-end of genomic RNA. These uridylylated forms act as a nucleotide-peptide primer for the polymerase.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>Sitei201 – 202Cleavage; by leader proteaseSequence analysis2
Sitei286 – 287CleavageSequence analysis2
Sitei504 – 505Cleavage; by picornain 3CSequence analysis2
Sitei724 – 725Cleavage; by picornain 3CSequence analysis2
Sitei935 – 936Cleavage; by picornain 3CSequence analysis2
Sitei953 – 954Cleavage; by ribosomal skipSequence analysis2
Sitei1107 – 1108Cleavage; by picornain 3CSequence analysis2
Sitei1425 – 1426Cleavage; by picornain 3CSequence analysis2
Sitei1578 – 1579Cleavage; by picornain 3CSequence analysis2
Sitei1601 – 1602Cleavage; by picornain 3CSequence analysis2
Sitei1625 – 1626Cleavage; by picornain 3CSequence analysis2
Sitei1649 – 1650Cleavage; by picornain 3CSequence analysis2
Sitei1862 – 1863Cleavage; by picornain 3CSequence analysis2

Keywords - PTMi

Autocatalytic cleavage, Covalent protein-RNA linkage, Disulfide bond, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P03305

<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

Interacts with host ISG15 (PubMed:29463763).

1 Publication

Interacts (via R-G-D motif) with host ITGAV/ITGB6 (PubMed:28534487).

1 Publication

Forms homooligomers.

Curated

Interacts with host VIM (PubMed:23576498).

Interacts with host BECN1 (PubMed:22933281).

2 Publications

Interacts with host DCTN3 (PubMed:24352458).

1 Publication

Protein-protein interaction databases

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P03305

<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

12332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P03305

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P03305

<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>Domaini1 – 201Peptidase C28Add BLAST201
Domaini1189 – 1353SF3 helicasePROSITE-ProRule annotationAdd BLAST165
Domaini1652 – 1848Peptidase C3PROSITE-ProRule annotationAdd BLAST197
Domaini2096 – 2214RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

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>Motifi869 – 871Cell attachment site1 Publication3
Motifi1879 – 1886Nuclear localization signal1 Publication8

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

Belongs to the picornaviruses polyprotein family.Curated

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00205 rhv_like, 3 hits

Database of protein disorder

More...
DisProti
DP00573

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.120.20, 3 hits
4.10.90.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR015031 Capsid_VP4_Picornavir
IPR037080 Capsid_VP4_sf_Picornavirus
IPR004080 FMDV_VP1_coat
IPR004004 Helic/Pol/Pept_Calicivir-typ
IPR000605 Helicase_SF3_ssDNA/RNA_vir
IPR014759 Helicase_SF3_ssRNA_vir
IPR027417 P-loop_NTPase
IPR038765 Papain-like_cys_pep_sf
IPR008739 Peptidase_C28
IPR000199 Peptidase_C3A/C3B_picornavir
IPR009003 Peptidase_S1_PA
IPR001676 Picornavirus_capsid
IPR033703 Rhv-like
IPR001205 RNA-dir_pol_C
IPR007094 RNA-dir_pol_PSvirus
IPR029053 Viral_coat

Pfam protein domain database

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Pfami
View protein in Pfam
PF05408 Peptidase_C28, 1 hit
PF00548 Peptidase_C3, 1 hit
PF00680 RdRP_1, 1 hit
PF00073 Rhv, 3 hits
PF00910 RNA_helicase, 1 hit
PF08935 VP4_2, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00918 CALICVIRUSNS
PR01542 FMDVP1COAT

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 1 hit
SSF54001 SSF54001, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51887 APHTHOVIRUS_LPRO, 1 hit
PS51874 PCV_3C_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51218 SF3_HELICASE_2, 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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Isoform Lab (identifier: P03305-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MNTTDCFIAL VQAIREIKAL FLSRTTGKME LTLYNGEKKT FYSRPNNHDN
60 70 80 90 100
CWLNAILQLF RYVEEPFFDW VYSSPENLTL EAIKQLEDLT GLELHEGGPP
110 120 130 140 150
ALVIWNIKHL LHTGIGTASR PSEVCMVDGT DMCLADFHAG IFLKGQEHAV
160 170 180 190 200
FACVTSNGWY AIDDEDFYPW TPDPSDVLVF VPYDQEPLNG EWKAKVQRKL
210 220 230 240 250
KGAGQSSPAT GSQNQSGNTG SIINNYYMQQ YQNSMDTQLG DNAISGGSNE
260 270 280 290 300
GSTDTTSTHT TNTQNNDWFS KLASSAFSGL FGALLADKKT EETTLLEDRI
310 320 330 340 350
LTTRNGHTTS TTQSSVGVTY GYATAEDFVS GPNTSGLETR VVQAERFFKT
360 370 380 390 400
HLFDWVTSDS FGRCHLLELP TDHKGVYGSL TDSYAYMRNG WDVEVTAVGN
410 420 430 440 450
QFNGGCLLVA MVPELYSIQK RELYQLTLFP HQFINPRTNM TAHITVPFVG
460 470 480 490 500
VNRYDQYKVH KPWTLVVMVV APLTVNTEGA PQIKVYANIA PTNVHVAGEF
510 520 530 540 550
PSKEGIFPVA CSDGYGGLVT TDPKTADPVY GKVFNPPRNQ LPGRFTNLLD
560 570 580 590 600
VAEACPTFLR FEGGVPYVTT KTDSDRVLAQ FDMSLAAKQM SNTFLAGLAQ
610 620 630 640 650
YYTQYSGTIN LHFMFTGPTD AKARYMVAYA PPGMEPPKTP EAAAHCIHAE
660 670 680 690 700
WDTGLNSKFT FSIPYLSAAD YAYTASGVAE TTNVQGWVCL FQITHGKADG
710 720 730 740 750
DALVVLASAG KDFELRLPVD ARAETTSAGE SADPVTTTVE NYGGETQIQR
760 770 780 790 800
RQHTDVSFIM DRFVKVTPQN QINILDLMQI PSHTLVGALL RASTYYFSDL
810 820 830 840 850
EIAVKHEGDL TWVPNGAPEK ALDNTTNPTA YHKAPLTRLA LPYTAPHRVL
860 870 880 890 900
ATVYNGECRY NRNAVPNLRG DLQVLAQKVA RTLPTSFNYG AIKATRVTEL
910 920 930 940 950
LYRMKRAETY CPRPLLAIHP TEARHKQKIV APVKQTLNFD LLKLAGDVES
960 970 980 990 1000
NPGPFFFSDV RSNFSKLVET INQMQEDMST KHGPDFNRLV SAFEELAIGV
1010 1020 1030 1040 1050
KAIRTGLDEA KPWYKLIKLL SRLSCMAAVA ARSKDPVLVA IMLADTGLEI
1060 1070 1080 1090 1100
LDSTFVVKKI SDSLSSLFHV PAPVFSFGAP VLLAGLVKVA SSFFRSTPED
1110 1120 1130 1140 1150
LERAEKQLKA RDINDIFAIL KNGEWLVKLI LAIRDWIKAW IASEEKFVTM
1160 1170 1180 1190 1200
TDLVPGILEK QRDLNDPSKY KEAKEWLDNA RQACLKSGNV HIANLCKVVA
1210 1220 1230 1240 1250
PAPSKSRPEP VVVCLRGKSG QGKSFLANVL AQAISTHFTG RIDSVWYCPP
1260 1270 1280 1290 1300
DPDHFDGYNQ QTVVVMDDLG QNPDGKDFKY FAQMVSTTGF IPPMASLEDK
1310 1320 1330 1340 1350
GKPFNSKVII ATTNLYSGFT PRTMVCPDAL NRRFHFDIDV SAKDGYKINS
1360 1370 1380 1390 1400
KLDIIKALED THANPVAMFQ YDCALLNGMA VEMKRMQQDM FKPQPPLQNV
1410 1420 1430 1440 1450
YQLVQEVIDR VELHEKVSSH PIFKQISIPS QKSVLYFLIE KGQHEAAIEF
1460 1470 1480 1490 1500
FEGMVHDSIK EELRPLIQQT SFVKRAFKRL KENFEIVALC LTLLANIVIM
1510 1520 1530 1540 1550
IRETRKRQKM VDDAVNEYIE KANITTDDKT LDEAEKSPLE TSGASTVGFR
1560 1570 1580 1590 1600
ERTLPGQKAC DDVNSEPAQP VEEQPQAEGP YAGPLERQKP LKVRAKLPQQ
1610 1620 1630 1640 1650
EGPYAGPMER QKPLKVKAKA PVVKEGPYEG PVKKPVALKV KAKNLIVTES
1660 1670 1680 1690 1700
GAPPTDLQKM VMGNTKPVEL ILDGKTVAIC CATGVFGTAY LVPRHLFAEK
1710 1720 1730 1740 1750
YDKIMVDGRA MTDSDYRVFE FEIKVKGQDM LSDAALMVLH RGNRVRDITK
1760 1770 1780 1790 1800
HFRDTARMKK GTPVVGVINN ADVGRLIFSG EALTYKDIVV CMDGDTMPGL
1810 1820 1830 1840 1850
FAYRAATKAG YCGGAVLAKD GADTFIVGTH SAGGNGVGYC SCVSRSMLLK
1860 1870 1880 1890 1900
MKAHIDPEPH HEGLIVDTRD VEERVHVMRK TKLAPTVAHG VFNPEFGPAA
1910 1920 1930 1940 1950
LSNKDPRLNE GVVLDEVIFS KHKGDTKMSE EDKALFRRCA ADYASRLHSV
1960 1970 1980 1990 2000
LGTANAPLSI YEAIKGVDGL DAMEPDTAPG LPWALQGKRR GALIDFENGT
2010 2020 2030 2040 2050
VGPEVEAALK LMEKREYKFV CQTFLKDEIR PLEKVRAGKT RIVDVLPVEH
2060 2070 2080 2090 2100
ILYTRMMIGR FCAQMHSNNG PQIGSAVGCN PDVDWQRFGT HFAQYRNVWD
2110 2120 2130 2140 2150
VDYSAFDANH CSDAMNIMFE EVFRTEFGFH PNAEWILKTL VNTEHAYENK
2160 2170 2180 2190 2200
RITVGGGMPS GCSATSIINT ILNNIYVLYA LRRHYEGVEL DTYTMISYGD
2210 2220 2230 2240 2250
DIVVASDYDL DFEALKPHFK SLGQTITPAD KSDKGFVLGH SITDVTFLKR
2260 2270 2280 2290 2300
HFHMDYGTGF YKPVMASKTL EAILSFARRG TIQEKLISVA GLAVHSGPDE
2310 2320 2330
YRRLFEPFQG LFEIPSYRSL YLRWVNAVCG DA
Length:2,332
Mass (Da):258,927
Last modified:July 21, 1986 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4A83176F43447D68
GO
Isoform Lb (identifier: P03305-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Show »
Length:2,304
Mass (Da):255,803
Checksum:i5372D197CC761349
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti780I → V in strain: Isolate O1BFS. 1
Natural varianti808G → R in strain: Isolate O1BFS. 1
Natural varianti861N → S in strain: Isolate O1BFS. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0189821 – 28Missing in isoform Lb. CuratedAdd BLAST28

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
X00871 Genomic RNA Translation: CAA25416.1
J02185 Genomic RNA Translation: AAA42635.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:CAA25416

Keywords - Coding sequence diversityi

Alternative initiation

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure complexed with oligosaccharide receptor

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00871 Genomic RNA Translation: CAA25416.1
J02185 Genomic RNA Translation: AAA42635.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QMYX-ray1.90A/B/C29-195[»]
1QOLX-ray3.00A/B/C/D/E/F/G/H29-201[»]
1QQPX-ray1.901725-937[»]
2287-504[»]
3505-724[»]
4202-286[»]
2JQFNMR-R/S29-201[»]
2JQGNMR-R29-195[»]
4QBBX-ray1.60A/B/C29-195[»]
6FFAX-ray1.50A29-195[»]
SMRiP03305
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

ELMiP03305

Protein family/group databases

MEROPSiC03.008
TCDBi1.A.85.1.8 the poliovirus 2b viroporin (2b viroporin) family
UniLectiniP03305

Proteomic databases

PRIDEiP03305

Genome annotation databases

KEGGiag:CAA25416

Enzyme and pathway databases

BRENDAi3.4.22.46 2315

Miscellaneous databases

EvolutionaryTraceiP03305

Family and domain databases

CDDicd00205 rhv_like, 3 hits
DisProtiDP00573
Gene3Di2.60.120.20, 3 hits
4.10.90.10, 1 hit
InterProiView protein in InterPro
IPR015031 Capsid_VP4_Picornavir
IPR037080 Capsid_VP4_sf_Picornavirus
IPR004080 FMDV_VP1_coat
IPR004004 Helic/Pol/Pept_Calicivir-typ
IPR000605 Helicase_SF3_ssDNA/RNA_vir
IPR014759 Helicase_SF3_ssRNA_vir
IPR027417 P-loop_NTPase
IPR038765 Papain-like_cys_pep_sf
IPR008739 Peptidase_C28
IPR000199 Peptidase_C3A/C3B_picornavir
IPR009003 Peptidase_S1_PA
IPR001676 Picornavirus_capsid
IPR033703 Rhv-like
IPR001205 RNA-dir_pol_C
IPR007094 RNA-dir_pol_PSvirus
IPR029053 Viral_coat
PfamiView protein in Pfam
PF05408 Peptidase_C28, 1 hit
PF00548 Peptidase_C3, 1 hit
PF00680 RdRP_1, 1 hit
PF00073 Rhv, 3 hits
PF00910 RNA_helicase, 1 hit
PF08935 VP4_2, 1 hit
PRINTSiPR00918 CALICVIRUSNS
PR01542 FMDVP1COAT
SUPFAMiSSF50494 SSF50494, 1 hit
SSF52540 SSF52540, 1 hit
SSF54001 SSF54001, 1 hit
PROSITEiView protein in PROSITE
PS51887 APHTHOVIRUS_LPRO, 1 hit
PS51874 PCV_3C_PRO, 1 hit
PS50507 RDRP_SSRNA_POS, 1 hit
PS51218 SF3_HELICASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiPOLG_FMDVO
<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: P03305
<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: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 26, 2020
This is version 195 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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