POLS_IBDVA
ID POLS_IBDVA Reviewed; 1012 AA.
AC P08364;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 95.
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 Australian 002-73) (IBDV)
OS (Gumboro disease virus).
OC Viruses; Riboviria; Orthornavirae; Birnaviridae; Avibirnavirus.
OX NCBI_TaxID=10997;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3014441; DOI=10.1093/nar/14.12.5001;
RA Hudson P.J., McKern N.M., Power B.E., Azad A.A.;
RT "Genomic structure of the large RNA segment of infectious bursal disease
RT virus.";
RL Nucleic Acids Res. 14:5001-5012(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 703-1012.
RX PubMed=3011501; DOI=10.1016/0014-5793(86)80587-7;
RA Hudson P.J., McKern N.M., Fahey K.J., Azad A.A.;
RT "Predicted sequence of the host-protective immunogen of infectious bursal
RT disease virus.";
RL FEBS Lett. 201:143-146(1986).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA27629.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X03993; CAA27629.1; ALT_INIT; Genomic_RNA.
DR PIR; A24382; GNXSAU.
DR BMRB; P08364; -.
DR SMR; P08364; -.
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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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_0000392586"
FT CHAIN 1..512
FT /note="Precursor of VP2"
FT /id="PRO_0000392587"
FT CHAIN 1..441
FT /note="Capsid protein VP2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036762"
FT PEPTIDE 442..487
FT /note="Structural peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227827"
FT PEPTIDE 488..494
FT /note="Structural peptide 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227828"
FT PEPTIDE 495..501
FT /note="Structural peptide 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227829"
FT PEPTIDE 502..512
FT /note="Structural peptide 4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227830"
FT CHAIN 513..755
FT /note="Protease VP4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036763"
FT CHAIN 756..1012
FT /note="Capsid protein VP3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036764"
FT DOMAIN 513..755
FT /note="Peptidase S50"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT REGION 970..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 BINDING 30
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between trimeric 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"
SQ SEQUENCE 1012 AA; 109503 MW; D9320A90459DE8F6 CRC64;
MTNLSDQTQQ IVPFIRSLLM PTTGPASIPD DTLEKHTLRS ETSTYNLTVG DTGSGLIVFF
PGFPGSIVGA HYTMQSNGNY KFDQMLLTAQ NLPASYNYCR LVSRSLTVRS STLPGGVYAL
NGTINAVTFQ GSLSELTDVS YNGLMSATAN INDKIGNVLV GEGVTVLSLP TSYDLGYVRL
GDPIPAIGLD PKMVATCDSS DRPRVYTITA ADDYQFSSQY QPGGVTITLF SANIDAITNL
SVGGELVFQT SVQGLVLNAT IYLVGFDGTT VTTRAVAAGN GLTAGTDNLM PFNLVIPTSE
ITQPVTSIKL EIVTSKSGGQ AGDQMSWLAS GNLAVTIHGG NYPGALRPVT LVAYERVATG
SVVTVAGVSN FELIPNPELA KNLVTEYGRF DPGAMNYTKL ILSERDRLGI KTVWPTREYT
DFREYFMEVA DLNSPLKIAG AFGFKDIIRA IRRIAVPVVS TLFPPAAPLA HAIGEGVDYL
LGDEAGAASG TARAASGKAR AASGRIRQLT LAADKGYEVV ANLFQVPQNP VVDGILASPG
VLRGAHNLDC VLREGATLFP VVITTVEDAM TPKALNSKMF AVIEGVREDL QPPSQRGSFI
RTLSGHRVYG YAPDGVLPLE TGRDYTVVPI DDVWDDSIML SKDPIPPIVG NSGNLAIAYM
DVFRPKVPIH VAMTGALNAY GEVEKVSFRS TKLATAHRLG LKLAGPGAFD INTGPNWATF
IKRFPHNPRD WDRLPYLNLP YLPPSAGRQY HLAMAASEFK ETPELESAVR AMEAAADVDP
LFQSALSVFM WLEENGIVTD MANFALSDPN AHRMRNFLAN APQAGSKSQR AKYGTAGYGV
EARGPTPEEA QREKDTRISK KMEAMGIYFA TPEWVALNGH RGPSPGQLKY WQNTREIPDP
NEDYLDYVHA EKSRLASEEQ ILRAATSIYG APGQAEPPQA FIDEVAKVYE INHGRGPNQE
QMKDLLLTAM EMKHRNPRRA PPKPKPKPNA PSQRPPGRLG RWIRTVSDED LE
