Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Structural polyprotein

Gene
N/A
Organism
Avian infectious bursal disease virus (strain 52/70) (IBDV) (Gumboro disease 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>
-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Capsid protein VP2 self assembles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell by interacting with host ITGA4/ITGB1 (By similarity).By similarity
The precursor of VP2 plays an important role in capsid assembly. First, pre-VP2 and VP2 oligomers assemble to form a procapsid. Then, the pre-VP2 intermediates may be processed into VP2 proteins by proteolytic cleavage mediated by VP4 to obtain the mature virion. The final capsid is composed of pentamers and hexamers but VP2 has a natural tendency to assemble into all-pentameric structures. Therefore pre-VP2 may be required to allow formation of the hexameric structures (By similarity).By similarity
Protease VP4 is a serine protease that cleaves the polyprotein into its final products. Pre-VP2 is first partially cleaved, and may be completely processed by VP4 upon capsid maturation.PROSITE-ProRule annotation
Capsid protein VP3 plays a key role in virion assembly by providing a scaffold for the capsid made of VP2. May self-assemble to form a T=4-like icosahedral inner-capsid composed of at least 180 trimers. Plays a role in genomic RNA packaging by recruiting VP1 into the capsid and interacting with the dsRNA genome segments to form a ribonucleoprotein complex. Additionally, the interaction of the VP3 C-terminal tail with VP1 removes the inherent structural blockade of the polymerase active site. Thus, VP3 can also function as a transcriptional activator (By similarity).By similarity
Structural peptide 1 is a small peptide derived from pre-VP2 C-terminus. It destabilizes and perforates cell membranes, suggesting a role during entry (By similarity).By similarity
Structural peptide 2 is a small peptide derived from pVP2 C-terminus. It is not essential for the virus viability, but viral growth is affected when missing (By similarity).By similarity
Structural peptide 3 is a small peptide derived from pVP2 C-terminus. It is not essential for the virus viability, but viral growth is affected when missing (By similarity).By similarity
Structural peptide 4 is a small peptide derived from pVP2 C-terminus. It is essential for the virus viability (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi30Divalent metal cation; shared with trimeric partnersBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei652NucleophilePROSITE-ProRule annotation1
Active sitei692PROSITE-ProRule annotation1

<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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Serine protease
LigandMetal-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Structural polyprotein
Short name:
PP
Cleaved into the following 8 chains:
Precursor of VP2
Short name:
Pre-VP2
Structural peptide 1
Short name:
p1
Alternative name(s):
pep46
Structural peptide 2
Short name:
p2
Alternative name(s):
pep7a
Structural peptide 3
Short name:
p3
Alternative name(s):
pep7b
Structural peptide 4
Short name:
p4
Alternative name(s):
pep11
Alternative name(s):
Non-structural protein VP4
Short name:
NS
<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>OrganismiAvian infectious bursal disease virus (strain 52/70) (IBDV) (Gumboro disease virus)
<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 identifieri10996 [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 lineageiVirusesdsRNA virusesBirnaviridaeAvibirnavirus
<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 hostiGallus gallus (Chicken) [TaxID: 9031]
Meleagris gallopavo (Wild turkey) [TaxID: 9103]

<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

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, T=13 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003925841 – 1012Structural polyproteinAdd BLAST1012
ChainiPRO_00003925851 – 512Precursor of VP2Add BLAST512
ChainiPRO_00000367591 – 441Capsid protein VP2By similarityAdd BLAST441
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_0000227823442 – 487Structural peptide 1By similarityAdd BLAST46
PeptideiPRO_0000227824488 – 494Structural peptide 2By similarity7
PeptideiPRO_0000227825495 – 501Structural peptide 3By similarity7
PeptideiPRO_0000227826502 – 512Structural peptide 4By similarityAdd BLAST11
ChainiPRO_0000036760513 – 755Protease VP4By similarityAdd BLAST243
ChainiPRO_0000036761756 – 1012Capsid protein VP3By similarityAdd BLAST257

<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

Specific enzymatic cleavages yield mature proteins. The capsid assembly seems to be regulated by polyprotein processing. The protease VP4 cleaves itself off the polyprotein, thus releasing pre-VP2 and VP3 within the infected cell. During capsid assembly, the C-terminus of pre-VP2 is further processed by VP4, giving rise to VP2, the external capsid protein and three small peptides that all stay closely associated with the capsid (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei441 – 442Cleavage; by protease VP4By similarity2
Sitei487 – 488Cleavage; by protease VP4By similarity2
Sitei494 – 495Cleavage; by protease VP4By similarity2
Sitei501 – 502Cleavage; by protease VP4By similarity2
Sitei512 – 513Cleavage; by protease VP4By similarity2
Sitei755 – 756Cleavage; by protease VP4By similarity2

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P25219

<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

Capsid protein VP2 is a homotrimer. A central divalent metal stabilizes the VP2 trimer, possibly calcium (By similarity). Capsid protein VP3 is a homodimer. Capsid protein VP2 interacts with host ITGA4/ITGB1. Capsid protein VP3 interacts (via C-terminus) with VP1 in the cytoplasm. Capsid VP3 interacts with VP2 (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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P25219

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

More...
SMRi
P25219

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Domaini513 – 755Peptidase S50PROSITE-ProRule annotationAdd BLAST243

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>Regioni1003 – 1012Interaction with VP1 proteinBy similarity10

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002662 Birna_VP2
IPR002663 Birna_VP3
IPR025775 Birna_VP4_Prtase_dom
IPR029053 Viral_coat

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01766 Birna_VP2, 1 hit
PF01767 Birna_VP3, 1 hit
PF01768 Birna_VP4, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51548 BIRNAVIRUS_VP4_PRO, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>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.

P25219-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTNLQDQTQQ IVPFIRSLLM PTTGPASIPD DTLEKHTLRS ETSTYNLTVG
60 70 80 90 100
DTGSGLIVFF PGFPGSIVGA HYTLQSNGNY KFDQMLLTAQ NLPASYNYCR
110 120 130 140 150
LVSRSLTVRS STLPGGVYAL NGTINAVTFQ GSLSELTDVS YNGLMSATAN
160 170 180 190 200
INDKIGNVLV GEGVTVLSLP TSYDLGYVRL GDPIPAIGLD PKMVATCDSS
210 220 230 240 250
DRPRVYTITA ADDYQFSSQY QPGGVTITLF SANIDAITSL SIGGELVFQT
260 270 280 290 300
SVQGLVLGAT IYLIGFDGTA VITRAVAADN GLTAGTDNLM PFNLVIPTNE
310 320 330 340 350
ITQPITSIKL EIVTSKSGGQ AGDQMSWSAS GSLAVTIHGG NYPGALRPVT
360 370 380 390 400
LVAYERVATG SVVTVAGVSN FELIPNPELA KNLVTEYGRF DPGAMNYTKL
410 420 430 440 450
ILSERDRLGI KTVWPTREYT DFREYFMEVA DLNSPLKIAG AFGFKDIIRA
460 470 480 490 500
IRRIAVPVVS TLFPPAAPLA HAIGEGVDYL LGDEAQAASG TARAASGKAR
510 520 530 540 550
AASGRIRQLT LAADKGYEVV ANLFQVPQNP VVDGILASPG VLRGAHNLDC
560 570 580 590 600
VLREGATLFP VVITTVEDAM TPKALNSKMF AVIEGVREDL QPPSQRGSFI
610 620 630 640 650
RTLSGHRVYG YAPDGVLPLE TGRDYTVVPI DDVWDDSIML SKDPIPPIVG
660 670 680 690 700
NSGNLAIAYM DVFRPKVPIH VAMTGAPNAC GEIEKISFRS TKLATAHRLG
710 720 730 740 750
LKLAGPGAFD VNTGPNWATF IKRFPHNPRD WDRLPYLNLP YLPPNAGRQY
760 770 780 790 800
HLAMAASEFK DTPELESAVR AMEAAANVDS LFQSALSVFM WLEENGIVTD
810 820 830 840 850
MANFTLSDPN AHRMRNFLAN APQAGSKSQR AKYGTAGYGV EARGPTPEEA
860 870 880 890 900
QRKKDTRISK KMETMGIYFA TPEWVALNGH RGPSPGQLKY WQNTREIPDP
910 920 930 940 950
NEDYLDYVHA EKSRLASDEQ ILRAATSIYG APGQAEPPQA FIDEVAKVYE
960 970 980 990 1000
INHGRGPNQE QMKDLLLTAM EMKHRNPRRA PPKPKPKPNA PTQRPPGRLG
1010
RWIRTVSDED LE
Length:1,012
Mass (Da):109,568
Last modified:May 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:i71A5D93A064DB36D
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D00869 Genomic RNA Translation: BAA00745.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JQ0941 GNXS52

<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
D00869 Genomic RNA Translation: BAA00745.1
PIRiJQ0941 GNXS52

3D structure databases

ProteinModelPortaliP25219
SMRiP25219
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP25219

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.120.20, 1 hit
InterProiView protein in InterPro
IPR002662 Birna_VP2
IPR002663 Birna_VP3
IPR025775 Birna_VP4_Prtase_dom
IPR029053 Viral_coat
PfamiView protein in Pfam
PF01766 Birna_VP2, 1 hit
PF01767 Birna_VP3, 1 hit
PF01768 Birna_VP4, 1 hit
PROSITEiView protein in PROSITE
PS51548 BIRNAVIRUS_VP4_PRO, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLS_IBDV5
<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: P25219
<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: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 7, 2018
This is version 78 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again