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-NOV-2018, entry version 77. 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 OS disease virus). OC Viruses; dsRNA viruses; 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 RT RNA 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 RT of a variant strain of infectious bursal disease virus which can RT circumvent 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 CC consisting of 260 VP2 trimers. The capsid encapsulates the genomic CC dsRNA. VP2 is also involved in attachment and entry into the host CC cell by interacting with host ITGA4/ITGB1 (By similarity). CC {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 CC VP2 proteins by proteolytic cleavage mediated by VP4 to obtain the CC mature virion. The final capsid is composed of pentamers and CC hexamers but VP2 has a natural tendency to assemble into all- CC pentameric structures. Therefore pre-VP2 may be required to allow CC formation of the hexameric structures (By similarity). CC {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 CC maturation. {ECO:0000255|PROSITE-ProRule:PRU00881}. CC -!- FUNCTION: Capsid protein VP3 plays a key role in virion assembly CC by providing a scaffold for the capsid made of VP2. May self- CC assemble to form a T=4-like icosahedral inner-capsid composed of CC at least 180 trimers. Plays a role in genomic RNA packaging by CC recruiting VP1 into the capsid and interacting with the dsRNA CC genome segments to form a ribonucleoprotein complex. Additionally, CC the interaction of the VP3 C-terminal tail with VP1 removes the CC inherent structural blockade of the polymerase active site. Thus, CC VP3 can also function as a transcriptional activator (By CC similarity). {ECO:0000250}. CC -!- FUNCTION: Structural peptide 1 is a small peptide derived from CC pre-VP2 C-terminus. It destabilizes and perforates cell membranes, CC suggesting a role during entry (By similarity). {ECO:0000250}. CC -!- FUNCTION: Structural peptide 2 is a small peptide derived from CC pVP2 C-terminus. It is not essential for the virus viability, but CC viral growth is affected when missing (By similarity). CC {ECO:0000250}. CC -!- FUNCTION: Structural peptide 3 is a small peptide derived from CC pVP2 C-terminus. It is not essential for the virus viability, but CC viral growth is affected when missing (By similarity). CC {ECO:0000250}. CC -!- FUNCTION: Structural peptide 4 is a small peptide derived from CC pVP2 C-terminus. It is essential for the virus viability (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Capsid protein VP2 is a homotrimer. A central divalent CC metal stabilizes the VP2 trimer, possibly calcium (By similarity). CC Capsid protein VP3 is a homodimer. Capsid protein VP2 interacts CC with host ITGA4/ITGB1. Capsid protein VP3 interacts (via C- CC terminus) with VP1 in the cytoplasm. Capsid VP3 interacts with VP2 CC (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Capsid protein VP2: Virion {ECO:0000305}. CC Host cytoplasm {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Capsid protein VP3: Virion {ECO:0000305}. CC Host 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 CC capsid assembly seems to be regulated by polyprotein processing. CC The protease VP4 cleaves itself off the polyprotein, thus CC releasing pre-VP2 and VP3 within the infected cell. During capsid CC assembly, the C-terminus of pre-VP2 is further processed by VP4, CC giving rise to VP2, the external capsid protein and three small CC peptides that all stay closely associated with the capsid (By CC 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 ProteinModelPortal; P29802; -. DR SMR; P29802; -. 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; 2.60.120.20; -; 1. DR InterPro; IPR002662; Birna_VP2. DR InterPro; IPR002663; Birna_VP3. 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 Structural polyprotein. FT /FTId=PRO_0000392590. FT CHAIN 1 512 Precursor of VP2. FT /FTId=PRO_0000392591. FT CHAIN 1 441 Capsid protein VP2. FT /FTId=PRO_0000036768. FT PEPTIDE 442 487 Structural peptide 1. {ECO:0000250}. FT /FTId=PRO_0000227835. FT PEPTIDE 488 494 Structural peptide 2. {ECO:0000250}. FT /FTId=PRO_0000227836. FT PEPTIDE 495 501 Structural peptide 3. {ECO:0000250}. FT /FTId=PRO_0000227837. FT PEPTIDE 502 512 Structural peptide 4. {ECO:0000250}. FT /FTId=PRO_0000227838. FT CHAIN 513 755 Protease VP4. {ECO:0000250}. FT /FTId=PRO_0000227839. FT CHAIN 756 1012 Capsid protein VP3. {ECO:0000250}. FT /FTId=PRO_0000227840. FT DOMAIN 513 755 Peptidase S50. {ECO:0000255|PROSITE- FT ProRule:PRU00881}. FT REGION 1003 1012 Interaction with VP1 protein. FT {ECO:0000250}. FT ACT_SITE 652 652 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU00881}. FT ACT_SITE 692 692 {ECO:0000255|PROSITE-ProRule:PRU00881}. FT METAL 30 30 Divalent metal cation; shared with FT trimeric partners. {ECO:0000250}. FT SITE 441 442 Cleavage; by protease VP4. {ECO:0000250}. FT SITE 487 488 Cleavage; by protease VP4. {ECO:0000250}. FT SITE 494 495 Cleavage; by protease VP4. {ECO:0000250}. FT SITE 501 502 Cleavage; by protease VP4. {ECO:0000250}. FT SITE 512 513 Cleavage; by protease VP4. {ECO:0000250}. FT SITE 755 756 Cleavage; by protease VP4. {ECO:0000250}. FT CONFLICT 5 5 Q -> S (in Ref. 2; BAA00954). FT {ECO:0000305}. FT CONFLICT 262 262 C -> Y (in Ref. 2; BAA00954). FT {ECO:0000305}. FT CONFLICT 469 469 V -> L (in Ref. 2; BAA00954). FT {ECO:0000305}. FT CONFLICT 481 481 R -> L (in Ref. 2; BAA00954). FT {ECO:0000305}. FT CONFLICT 495 496 AS -> KL (in Ref. 2; BAA00954). FT {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 //