POLS_IBDVO
ID POLS_IBDVO Reviewed; 1012 AA.
AC P27276;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 OH) (IBDV) (Gumboro disease
OS virus).
OC Viruses; Riboviria; Orthornavirae; Birnaviridae; Avibirnavirus.
OX NCBI_TaxID=10999;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1651602; DOI=10.1016/0042-6822(91)90865-9;
RA Kibenge F.S.B., McKenna P.K., Dybing J.K.;
RT "Genome cloning and analysis of the large RNA segment (segment A) of a
RT naturally avirulent serotype 2 infectious bursal disease virus.";
RL Virology 184:437-440(1991).
RN [2]
RP ACTIVE SITES OF PROTEASE VP4, AND MUTAGENESIS OF SER-490; SER-497; SER-504;
RP ASP-515; HIS-547; ASP-590 AND SER-653.
RX PubMed=11878927; DOI=10.1006/viro.2001.1260;
RA Rodriguez-Lecompte J.C., Kibenge F.S.B.;
RT "Site-directed mutagenesis of Avibirnavirus VP4 gene.";
RL Virology 292:241-246(2002).
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}.
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DR EMBL; M66722; AAA46239.1; -; Genomic_RNA.
DR EMBL; U30818; AAC55351.1; -; Genomic_RNA.
DR PIR; A40569; GNXSOH.
DR SMR; P27276; -.
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 1: Evidence at protein level;
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_0000392592"
FT CHAIN 1..513
FT /note="Precursor of VP2"
FT /id="PRO_0000392593"
FT CHAIN 1..442
FT /note="Capsid protein VP2"
FT /id="PRO_0000036770"
FT PEPTIDE 443..488
FT /note="Structural peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227841"
FT PEPTIDE 489..495
FT /note="Structural peptide 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227842"
FT PEPTIDE 496..502
FT /note="Structural peptide 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227843"
FT PEPTIDE 503..513
FT /note="Structural peptide 4"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227844"
FT CHAIN 514..755
FT /note="Protease VP4"
FT /id="PRO_0000036771"
FT CHAIN 756..1012
FT /note="Capsid protein VP3"
FT /id="PRO_0000036772"
FT DOMAIN 514..755
FT /note="Peptidase S50"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT REGION 972..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 653
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 442..443
FT /note="Cleavage; by protease VP4"
FT /evidence="ECO:0000250"
FT SITE 488..489
FT /note="Cleavage; by protease VP4"
FT /evidence="ECO:0000250"
FT SITE 495..496
FT /note="Cleavage; by protease VP4"
FT /evidence="ECO:0000250"
FT SITE 502..503
FT /note="Cleavage; by protease VP4"
FT /evidence="ECO:0000250"
FT SITE 513..514
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 MUTAGEN 490
FT /note="S->K: Partial loss of pVP2-VP4 cleavage and complete
FT loss of VP3-VP4 cleavage; when associated with K-497 and K-
FT 504."
FT /evidence="ECO:0000269|PubMed:11878927"
FT MUTAGEN 497
FT /note="S->K: Partial loss of pVP2-VP4 cleavage and complete
FT loss of VP3-VP4 cleavage; when associated with K-490 and K-
FT 504."
FT /evidence="ECO:0000269|PubMed:11878927"
FT MUTAGEN 504
FT /note="S->K: Partial loss of pVP2-VP4 cleavage and complete
FT loss of VP3-VP4 cleavage; when associated with K-490 and K-
FT 497."
FT /evidence="ECO:0000269|PubMed:11878927"
FT MUTAGEN 515
FT /note="D->S: Partial loss of polyprotein processing."
FT /evidence="ECO:0000269|PubMed:11878927"
FT MUTAGEN 547
FT /note="H->P: Almost complete loss of polyprotein
FT processing."
FT /evidence="ECO:0000269|PubMed:11878927"
FT MUTAGEN 590
FT /note="D->P: Almost complete loss of polyprotein
FT processing."
FT /evidence="ECO:0000269|PubMed:11878927"
FT MUTAGEN 653
FT /note="S->P: Almost complete loss of polyprotein
FT processing."
FT /evidence="ECO:0000269|PubMed:11878927"
SQ SEQUENCE 1012 AA; 109866 MW; B4A2CE492C65221A CRC64;
MTNLMDHTQQ IVPFIRSLLM PTTGPASIPD DTLEKHTLRS ETSTYNLTVG DTGSGLIVFF
PGFPGSVVGA HYTLQSSGSY QFDQMLLTAQ NLPVSYNYCR LVSRSLTVRS STLPGGVYAL
NGTINAVTFQ GSLSELTDYS YNGLMSATAN INDKIGNVLV GEGVTVLSLP TSYDLSYVRL
GDPIPAAGLD PKLMATCDSS DRPRVYTVTA ADEYQFSSQL IPSGVKTTLF TANIDALTSL
SVGGELIFSQ VTIHSIEVDV TIYFIGFDGT EVTVKAVATD FGLTTGTNNL VPFNLGGPTS
EITQPITSMK LEVVTYKRGG TAGDPISWTV SGTLAVTVHG GNYPGALRPV TLVAYERVAA
GSVVTVAGVS NFELIPNPEL AKNLVTEYGR FDPGAMNYTK LILSERDRLG IKTVWPTREY
TDFREYFMEV ADLNSPLKIA GAFGFKDIIR AIRKIAVPVV STLFPPAAPL AHANREGVDY
LLGDEAQAAS GTARGASGKA RAASGRIRQL TLAADKGYEV VANMFQVPQN PIVDGILASP
GILRGAHNLD CVSKEGATLF PVVITTLEDE LTPKALNSKM FAVIEGARED LQPPSQRGSF
IRTLSGHRVY GYAPDGVLPL ETGRDYTVVP IDDVWDDSIM LSQDPIPPIV GNSGNLAIAY
MDVFRPKVPI HVAMTGALNA SEIESVSFRS TKLATAHRLG MKLAGPGDYD INTGPNWATF
IKRFPHNPRG WDRLPYLNLP YLPPTAGRQF HLALAASEFK ETPELEDAVR AMDAAANADP
LFRSALQVFM WLEENGIVTD MANFALSDPN AHRMKNFLAN APQAGSKSQR AKYGTAGYGV
EARGPTPEEA QRAKDARISK KMETMGIYFA TPEWVALNGH RGPSPGQLKY WQNTREIPEP
NEDYPDYVHA EKSRLASEEQ ILRAATSIYG APGQAEPPQA FIDEVARVYE TNHGRVPNQE
QMKDLLLTAM EMKHRNPRRA PPKPKPKPNA PSQRPPGRLG RWIRTVSDED LE
