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Structural polyprotein (PP) [Cleaved into: Precursor of VP2 (Pre-VP2); Capsid protein VP2; Structural peptide 1 (p1) (pep46); Structural peptide 2 (p2) (pep7a); Structural peptide 3 (p3) (pep7b); Structural peptide 4 (p4) (pep11); Protease VP4 (EC 3.4.21.-) (Non-structural protein VP4) (NS); Capsid protein VP3]

 POLS_IBDVO              Reviewed;        1012 AA.
P27276;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
28-MAR-2018, entry version 77.
RecName: Full=Structural polyprotein;
Short=PP;
Contains:
RecName: Full=Precursor of VP2;
Short=Pre-VP2;
Contains:
RecName: Full=Capsid protein VP2;
Contains:
RecName: Full=Structural peptide 1;
Short=p1;
AltName: Full=pep46;
Contains:
RecName: Full=Structural peptide 2;
Short=p2;
AltName: Full=pep7a;
Contains:
RecName: Full=Structural peptide 3;
Short=p3;
AltName: Full=pep7b;
Contains:
RecName: Full=Structural peptide 4;
Short=p4;
AltName: Full=pep11;
Contains:
RecName: Full=Protease VP4;
EC=3.4.21.-;
AltName: Full=Non-structural protein VP4;
Short=NS;
Contains:
RecName: Full=Capsid protein VP3;
Avian infectious bursal disease virus (strain OH) (IBDV) (Gumboro
disease virus).
Viruses; dsRNA viruses; Birnaviridae; Avibirnavirus.
NCBI_TaxID=10999;
NCBI_TaxID=9031; Gallus gallus (Chicken).
NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=1651602; DOI=10.1016/0042-6822(91)90865-9;
Kibenge F.S.B., McKenna P.K., Dybing J.K.;
"Genome cloning and analysis of the large RNA segment (segment A) of a
naturally avirulent serotype 2 infectious bursal disease virus.";
Virology 184:437-440(1991).
[2]
ACTIVE SITES OF PROTEASE VP4, AND MUTAGENESIS OF SER-490; SER-497;
SER-504; ASP-515; HIS-547; ASP-590 AND SER-653.
PubMed=11878927; DOI=10.1006/viro.2001.1260;
Rodriguez-Lecompte J.C., Kibenge F.S.B.;
"Site-directed mutagenesis of Avibirnavirus VP4 gene.";
Virology 292:241-246(2002).
-!- FUNCTION: 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).
{ECO:0000250}.
-!- FUNCTION: 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).
{ECO:0000250}.
-!- FUNCTION: 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. {ECO:0000255|PROSITE-ProRule:PRU00881}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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).
{ECO:0000250}.
-!- FUNCTION: 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).
{ECO:0000250}.
-!- FUNCTION: Structural peptide 4 is a small peptide derived from
pVP2 C-terminus. It is essential for the virus viability (By
similarity). {ECO:0000250}.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP2: Virion {ECO:0000305}.
Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein VP3: Virion {ECO:0000305}.
Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Structural peptide 1: Virion {ECO:0000305}.
Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Structural peptide 2: Virion {ECO:0000305}.
Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Structural peptide 3: Virion {ECO:0000305}.
Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Structural peptide 4: Virion {ECO:0000305}.
Host cytoplasm {ECO:0000305}.
-!- PTM: 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). {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; M66722; AAA46239.1; -; Genomic_RNA.
EMBL; U30818; AAC55351.1; -; Genomic_RNA.
PIR; A40569; GNXSOH.
ProteinModelPortal; P27276; -.
SMR; P27276; -.
PMAP-CutDB; P27276; -.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0039621; C:T=13 icosahedral viral capsid; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
Gene3D; 2.60.120.20; -; 2.
InterPro; IPR002662; Birna_VP2.
InterPro; IPR002663; Birna_VP3.
InterPro; IPR025775; Birna_VP4_Prtase_dom.
InterPro; IPR029053; Viral_coat.
Pfam; PF01766; Birna_VP2; 1.
Pfam; PF01767; Birna_VP3; 1.
Pfam; PF01768; Birna_VP4; 1.
PROSITE; PS51548; BIRNAVIRUS_VP4_PRO; 1.
1: Evidence at protein level;
Capsid protein; Host cytoplasm; Hydrolase; Metal-binding; Protease;
Serine protease; T=13 icosahedral capsid protein; Virion.
CHAIN 1 1012 Structural polyprotein.
/FTId=PRO_0000392592.
CHAIN 1 513 Precursor of VP2.
/FTId=PRO_0000392593.
CHAIN 1 442 Capsid protein VP2.
/FTId=PRO_0000036770.
PEPTIDE 443 488 Structural peptide 1. {ECO:0000250}.
/FTId=PRO_0000227841.
PEPTIDE 489 495 Structural peptide 2. {ECO:0000250}.
/FTId=PRO_0000227842.
PEPTIDE 496 502 Structural peptide 3. {ECO:0000250}.
/FTId=PRO_0000227843.
PEPTIDE 503 513 Structural peptide 4. {ECO:0000250}.
/FTId=PRO_0000227844.
CHAIN 514 755 Protease VP4.
/FTId=PRO_0000036771.
CHAIN 756 1012 Capsid protein VP3.
/FTId=PRO_0000036772.
DOMAIN 514 755 Peptidase S50. {ECO:0000255|PROSITE-
ProRule:PRU00881}.
REGION 1003 1012 Interaction with VP1 protein.
{ECO:0000250}.
ACT_SITE 653 653 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00881}.
ACT_SITE 692 692 {ECO:0000255|PROSITE-ProRule:PRU00881}.
METAL 30 30 Divalent metal cation; shared with
trimeric partners. {ECO:0000250}.
SITE 442 443 Cleavage; by protease VP4. {ECO:0000250}.
SITE 488 489 Cleavage; by protease VP4. {ECO:0000250}.
SITE 495 496 Cleavage; by protease VP4. {ECO:0000250}.
SITE 502 503 Cleavage; by protease VP4. {ECO:0000250}.
SITE 513 514 Cleavage; by protease VP4. {ECO:0000250}.
SITE 755 756 Cleavage; by protease VP4. {ECO:0000250}.
MUTAGEN 490 490 S->K: Partial loss of pVP2-VP4 cleavage
and complete loss of VP3-VP4 cleavage;
when associated with K-497 and K-504.
{ECO:0000269|PubMed:11878927}.
MUTAGEN 497 497 S->K: Partial loss of pVP2-VP4 cleavage
and complete loss of VP3-VP4 cleavage;
when associated with K-490 and K-504.
{ECO:0000269|PubMed:11878927}.
MUTAGEN 504 504 S->K: Partial loss of pVP2-VP4 cleavage
and complete loss of VP3-VP4 cleavage;
when associated with K-490 and K-497.
{ECO:0000269|PubMed:11878927}.
MUTAGEN 515 515 D->S: Partial loss of polyprotein
processing.
{ECO:0000269|PubMed:11878927}.
MUTAGEN 547 547 H->P: Almost complete loss of polyprotein
processing.
{ECO:0000269|PubMed:11878927}.
MUTAGEN 590 590 D->P: Almost complete loss of polyprotein
processing.
{ECO:0000269|PubMed:11878927}.
MUTAGEN 653 653 S->P: Almost complete loss of polyprotein
processing.
{ECO:0000269|PubMed:11878927}.
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


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