ID POLS_IBDVE Reviewed; 1012 AA. AC P29802; Q9WHR0; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 2. DT 07-APR-2021, entry version 83. DE RecName: Full=Structural polyprotein; DE Short=PP; DE Contains: DE RecName: Full=Precursor of VP2; DE Short=Pre-VP2; DE Contains: DE RecName: Full=Capsid protein VP2; DE Contains: DE RecName: Full=Structural peptide 1; DE Short=p1; DE AltName: Full=pep46; DE Contains: DE RecName: Full=Structural peptide 2; DE Short=p2; DE AltName: Full=pep7a; DE Contains: DE RecName: Full=Structural peptide 3; DE Short=p3; DE AltName: Full=pep7b; DE Contains: DE RecName: Full=Structural peptide 4; DE Short=p4; DE AltName: Full=pep11; DE Contains: DE RecName: Full=Protease VP4; DE EC=3.4.21.-; DE AltName: Full=Non-structural protein VP4; DE Short=NS; DE Contains: DE RecName: Full=Capsid protein VP3; OS Avian infectious bursal disease virus (strain E) (IBDV) (Gumboro disease OS virus). OC Viruses; Riboviria; Orthornavirae; Birnaviridae; Avibirnavirus. OX NCBI_TaxID=31560; OH NCBI_TaxID=9031; Gallus gallus (Chicken). OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=10507413; DOI=10.1016/s0166-0934(99)00083-x; RA Akin A., Wu C.C., Lin T.L.; RT "Amplification and cloning of infectious bursal disease virus genomic RNA RT segments by long and accurate PCR."; RL J. Virol. Methods 82:55-61(1999). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=1651980; DOI=10.1099/0022-1317-72-8-1835; RA Heine H.G., Haritou M., Failla P., Fahey K.J., Azad A.A.; RT "Sequence analysis and expression of the host-protective immunogen VP2 of a RT variant strain of infectious bursal disease virus which can circumvent RT vaccination with standard type I strains."; RL J. Gen. Virol. 72:1835-1843(1991). CC -!- FUNCTION: Capsid protein VP2 self assembles to form an icosahedral CC capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of CC 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also CC involved in attachment and entry into the host cell by interacting with CC host ITGA4/ITGB1 (By similarity). {ECO:0000250}. CC -!- FUNCTION: The precursor of VP2 plays an important role in capsid CC assembly. First, pre-VP2 and VP2 oligomers assemble to form a CC procapsid. Then, the pre-VP2 intermediates may be processed into VP2 CC proteins by proteolytic cleavage mediated by VP4 to obtain the mature CC virion. The final capsid is composed of pentamers and hexamers but VP2 CC has a natural tendency to assemble into all-pentameric structures. CC Therefore pre-VP2 may be required to allow formation of the hexameric CC structures (By similarity). {ECO:0000250}. CC -!- FUNCTION: Protease VP4 is a serine protease that cleaves the CC polyprotein into its final products. Pre-VP2 is first partially CC cleaved, and may be completely processed by VP4 upon capsid maturation. CC {ECO:0000255|PROSITE-ProRule:PRU00881}. CC -!- FUNCTION: Capsid protein VP3 plays a key role in virion assembly by CC providing a scaffold for the capsid made of VP2. May self-assemble to CC form a T=4-like icosahedral inner-capsid composed of at least 180 CC trimers. Plays a role in genomic RNA packaging by recruiting VP1 into CC the capsid and interacting with the dsRNA genome segments to form a CC ribonucleoprotein complex. Additionally, the interaction of the VP3 C- CC terminal tail with VP1 removes the inherent structural blockade of the CC polymerase active site. Thus, VP3 can also function as a CC transcriptional activator (By similarity). {ECO:0000250}. CC -!- FUNCTION: Structural peptide 1 is a small peptide derived from pre-VP2 CC C-terminus. It destabilizes and perforates cell membranes, suggesting a CC role during entry (By similarity). {ECO:0000250}. CC -!- FUNCTION: Structural peptide 2 is a small peptide derived from pVP2 C- CC terminus. It is not essential for the virus viability, but viral growth CC is affected when missing (By similarity). {ECO:0000250}. CC -!- FUNCTION: Structural peptide 3 is a small peptide derived from pVP2 C- CC terminus. It is not essential for the virus viability, but viral growth CC is affected when missing (By similarity). {ECO:0000250}. CC -!- FUNCTION: Structural peptide 4 is a small peptide derived from pVP2 C- CC terminus. It is essential for the virus viability (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Capsid protein VP2 is a homotrimer. A central divalent metal CC stabilizes the VP2 trimer, possibly calcium (By similarity). Capsid CC protein VP3 is a homodimer. Capsid protein VP2 interacts with host CC ITGA4/ITGB1. Capsid protein VP3 interacts (via C-terminus) with VP1 in CC the cytoplasm. Capsid VP3 interacts with VP2 (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000305}. Host CC cytoplasm {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000305}. Host CC cytoplasm {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Structural peptide 1]: Virion {ECO:0000305}. CC Host cytoplasm {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Structural peptide 2]: Virion {ECO:0000305}. CC Host cytoplasm {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Structural peptide 3]: Virion {ECO:0000305}. CC Host cytoplasm {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Structural peptide 4]: Virion {ECO:0000305}. CC Host cytoplasm {ECO:0000305}. CC -!- PTM: Specific enzymatic cleavages yield mature proteins. The capsid CC assembly seems to be regulated by polyprotein processing. The protease CC VP4 cleaves itself off the polyprotein, thus releasing pre-VP2 and VP3 CC within the infected cell. During capsid assembly, the C-terminus of CC pre-VP2 is further processed by VP4, giving rise to VP2, the external CC capsid protein and three small peptides that all stay closely CC associated with the capsid (By similarity). {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF133904; AAD32617.1; -; Genomic_RNA. DR EMBL; D10065; BAA00954.1; -; Genomic_RNA. DR PIR; PQ0283; GNXSIE. DR SMR; P29802; -. DR MEROPS; S50.002; -. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0039621; C:T=13 icosahedral viral capsid; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR Gene3D; 1.10.150.620; -; 1. DR Gene3D; 1.10.8.880; -; 1. DR Gene3D; 2.60.120.20; -; 1. DR InterPro; IPR002662; Birna_VP2. DR InterPro; IPR002663; Birna_VP3. DR InterPro; IPR043048; Birna_VP3_dom1. DR InterPro; IPR043049; Birna_VP3_dom2. DR InterPro; IPR025775; Birna_VP4_Prtase_dom. DR InterPro; IPR029053; Viral_coat. DR Pfam; PF01766; Birna_VP2; 1. DR Pfam; PF01767; Birna_VP3; 1. DR Pfam; PF01768; Birna_VP4; 1. DR PROSITE; PS51548; BIRNAVIRUS_VP4_PRO; 1. PE 3: Inferred from homology; KW Capsid protein; Host cytoplasm; Hydrolase; Metal-binding; Protease; KW Serine protease; T=13 icosahedral capsid protein; Virion. FT CHAIN 1..1012 FT /note="Structural polyprotein" FT /id="PRO_0000392590" FT CHAIN 1..512 FT /note="Precursor of VP2" FT /id="PRO_0000392591" FT CHAIN 1..441 FT /note="Capsid protein VP2" FT /id="PRO_0000036768" FT PEPTIDE 442..487 FT /note="Structural peptide 1" FT /evidence="ECO:0000250" FT /id="PRO_0000227835" FT PEPTIDE 488..494 FT /note="Structural peptide 2" FT /evidence="ECO:0000250" FT /id="PRO_0000227836" FT PEPTIDE 495..501 FT /note="Structural peptide 3" FT /evidence="ECO:0000250" FT /id="PRO_0000227837" FT PEPTIDE 502..512 FT /note="Structural peptide 4" FT /evidence="ECO:0000250" FT /id="PRO_0000227838" FT CHAIN 513..755 FT /note="Protease VP4" FT /evidence="ECO:0000250" FT /id="PRO_0000227839" FT CHAIN 756..1012 FT /note="Capsid protein VP3" FT /evidence="ECO:0000250" FT /id="PRO_0000227840" FT DOMAIN 513..755 FT /note="Peptidase S50" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00881" FT REGION 1003..1012 FT /note="Interaction with VP1 protein" FT /evidence="ECO:0000250" FT ACT_SITE 652 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00881" FT ACT_SITE 692 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00881" FT METAL 30 FT /note="Divalent metal cation; shared with trimeric FT partners" FT /evidence="ECO:0000250" FT SITE 441..442 FT /note="Cleavage; by protease VP4" FT /evidence="ECO:0000250" FT SITE 487..488 FT /note="Cleavage; by protease VP4" FT /evidence="ECO:0000250" FT SITE 494..495 FT /note="Cleavage; by protease VP4" FT /evidence="ECO:0000250" FT SITE 501..502 FT /note="Cleavage; by protease VP4" FT /evidence="ECO:0000250" FT SITE 512..513 FT /note="Cleavage; by protease VP4" FT /evidence="ECO:0000250" FT SITE 755..756 FT /note="Cleavage; by protease VP4" FT /evidence="ECO:0000250" FT CONFLICT 5 FT /note="Q -> S (in Ref. 2; BAA00954)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="C -> Y (in Ref. 2; BAA00954)" FT /evidence="ECO:0000305" FT CONFLICT 469 FT /note="V -> L (in Ref. 2; BAA00954)" FT /evidence="ECO:0000305" FT CONFLICT 481 FT /note="R -> L (in Ref. 2; BAA00954)" FT /evidence="ECO:0000305" FT CONFLICT 495..496 FT /note="AS -> KL (in Ref. 2; BAA00954)" FT /evidence="ECO:0000305" SQ SEQUENCE 1012 AA; 110035 MW; 9651DE7FCCAFDE20 CRC64; MTNLQDQTQQ IVPFIRSLLM PTTGPASIPD DTLEKHTLRS ETSTYNLTVG DTGSGLIVFF PGFPGSIVGA HYTLQSNGNY KFDQMLLTAQ NLPASYNYCR LVSRSLTVRS STLPGGVYAL NGTINAVTFQ GSLSELTDVS YNGLMSATAN INDKIGNVLV GEGVTVLSLP TSYDLGYVRL GDPIPAIGLD PKMVATCDSS DRPRVYTITA ADNYQFSSQY QTGGVTITLF SANIDAITSL SVGGELVFKT SVQSLVLGAT ICLIGFDGTA VITRAVAANN GLTAGIDNLM PFNLVIPTNE ITQPITSIKL EIVTSKSDGQ AGEQMSWSAS GSLAVTIHGG NYPGALRPVT LVAYERVATG SVVTVAGVSN FELIPNPELA KNLVTEYGRF DPGAMNYTKL ILSERDRLGI KTVWPTREYT DFREYFMEVA DLNSPLKIAG AFGFKDIIRA IRRIAVPVVS TLFPPAAPVA HAIGEGVDYL RGDEAQAASG TARAASGKAR AASGRIRQLT LAADKGYEVV ANLFQVPQNP VVDGILASPG ILRGAHNLDC VLREGATLFP VVITTVEDAM TPKALNNKMF AVIEGVREDL QPPSQRGSFI RTLSGHRVYG YAPDGVLPLE TGRDYTVVPI DDVWDDSIML SKDPIPPIVG NSGNLAIAYM DVFRPKVPIH VAMTGALNAC GEIEKISFRS TKLATAHRLG LKLAGPGAFD VNTGPNWATF IKRFPHNPRD WDRLPYLNLP YLPPNAGRQY HLAMAASEFK ETPELESAVR AMEAAANVDP LFQSALSVFM WLEENGIVTD MANFALSDPN AHRMRNFLAN ALQAGSKSQR AKYGTAGYGV EARGPTLEGA QREKDTRISK KMETMGIYFA TQEWVAFNRH RRPSPGQLKY WQNTREIPDP NEYYLDYVHA EKSRLASEEQ ILRAATSIYG APVQAEPLQA FIDEVAKVYE INHGRGPNQE QMKDLLLTAM EMKHRNPRRA PPKPKPKPNA PTQRPPGRLG RWIRTVSDED LE //