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Database: UniProt
Entry: POLS_IPNVJ
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Original site: POLS_IPNVJ 
ID   POLS_IPNVJ              Reviewed;         972 AA.
AC   P05844; Q82720;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   02-DEC-2020, entry version 98.
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   Contains:
DE     RecName: Full=Structural peptide 2;
DE              Short=p2;
DE   Contains:
DE     RecName: Full=Structural peptide 3;
DE              Short=p3;
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   Infectious pancreatic necrosis virus (strain Jasper) (IPNV).
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae; Aquabirnavirus.
OX   NCBI_TaxID=11003;
OH   NCBI_TaxID=8022; Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OH   NCBI_TaxID=8028; Salmo.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3737418; DOI=10.1093/nar/14.14.5934;
RA   Duncan R., Dobos P.;
RT   "The nucleotide sequence of infectious pancreatic necrosis virus (IPNV)
RT   dsRNA segment A reveals one large ORF encoding a precursor polyprotein.";
RL   Nucleic Acids Res. 14:5934-5934(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 433-972, AND SEQUENCE REVISION TO 566
RP   AND 708.
RX   PubMed=3316706; DOI=10.1128/jvi.61.12.3655-3664.1987;
RA   Duncan R., Nagy E., Krell P.J., Dobos P.;
RT   "Synthesis of the infectious pancreatic necrosis virus polyprotein,
RT   detection of a virus-encoded protease, and fine structure mapping of genome
RT   segment A coding regions.";
RL   J. Virol. 61:3655-3664(1987).
RN   [3]
RP   SUBUNIT, AND STRUCTURE BY ELECTRON MICROSCOPY (3.4 ANGSTROMS) OF SUBVIRAL
RP   PARTICLES.
RX   PubMed=20007275; DOI=10.1128/jvi.01536-09;
RA   Coulibaly F., Chevalier C., Delmas B., Rey F.A.;
RT   "Crystal structure of an aquabirnavirus particle: insights into antigenic
RT   diversity and virulence determinism.";
RL   J. Virol. 84:1792-1799(2010).
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.
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 composed of VP2. May self-assemble
CC       to 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 the C-
CC       terminus of pre-VP2. It destabilizes and perforates cell membranes,
CC       suggesting a role during viral entry (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Structural peptide 2 is a small peptide derived from the C-
CC       terminus of pre-VP2. It is not essential for virus viability, but viral
CC       growth is affected when this protein is absent (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: Structural peptide 3 is a small peptide derived from pre-VP2
CC       C-terminus. It is not essential for virus viability, but viral growth
CC       is affected when this protein is absent (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Capsid protein VP2 is a homotrimer. A central divalent metal
CC       (possibly cobalt) stabilizes the VP2 trimer. Capsid protein VP3 is a
CC       homodimer. Capsid protein VP3 interacts (via C-terminus) with VP1 in
CC       the cytoplasm. Capsid protein 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   -!- PTM: Specific enzymatic cleavages yield mature proteins. 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.
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DR   EMBL; M18049; AAA89179.1; -; Genomic_RNA.
DR   PIR; A23599; GNXSIV.
DR   PIR; T09624; T09624.
DR   RefSeq; NP_047196.1; NC_001915.1.
DR   PDB; 3ZED; X-ray; 2.20 A; D/E/F=735-972.
DR   PDBsum; 3ZED; -.
DR   SMR; P05844; -.
DR   PRIDE; P05844; -.
DR   GeneID; 956513; -.
DR   KEGG; vg:956513; -.
DR   Proteomes; UP000007248; Genome.
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   DisProt; DP02497; -.
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   3D-structure; Capsid protein; Host cytoplasm; Hydrolase; Metal-binding;
KW   Protease; Reference proteome; Serine protease;
KW   T=13 icosahedral capsid protein; Virion.
FT   CHAIN           1..972
FT                   /note="Structural polyprotein"
FT                   /id="PRO_0000391632"
FT   CHAIN           1..508
FT                   /note="Precursor of VP2"
FT                   /id="PRO_0000391633"
FT   CHAIN           1..442
FT                   /note="Capsid protein VP2"
FT                   /id="PRO_0000036780"
FT   PEPTIDE         443..486
FT                   /note="Structural peptide 1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000227859"
FT   PEPTIDE         487..495
FT                   /note="Structural peptide 2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000227860"
FT   PEPTIDE         496..508
FT                   /note="Structural peptide 3"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000227861"
FT   CHAIN           509..734
FT                   /note="Protease VP4"
FT                   /id="PRO_0000036781"
FT   CHAIN           735..972
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000036782"
FT   DOMAIN          509..734
FT                   /note="Peptidase S50"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT   ACT_SITE        633
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT   ACT_SITE        674
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT   METAL           26
FT                   /note="Divalent metal cation; shared with trimeric
FT                   partners"
FT   SITE            442..443
FT                   /note="Cleavage; by protease VP4"
FT                   /evidence="ECO:0000250"
FT   SITE            486..487
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            508..509
FT                   /note="Cleavage; by protease VP4"
FT                   /evidence="ECO:0000250"
FT   SITE            734..735
FT                   /note="Cleavage; by protease VP4"
FT                   /evidence="ECO:0000250"
FT   HELIX           968..970
FT                   /evidence="ECO:0000244|PDB:3ZED"
SQ   SEQUENCE   972 AA;  106666 MW;  5CABCD0414EE122B CRC64;
     MSTSKATATY LRSIMLPENG PASIPDDITE RHILKQETSS YNLEVSESGS GLLVCFPGAP
     GSRVGAHYRW NLNQTALEFD QWLETSQDLK KAFNYGRLIS RKYDIQSSTL PAGLYALNGT
     LNAATFEGSL SEVESLTYNS LMSLTTNPQD KVNNQLVTKG ITVLNLPTGF DKPYVRLEDE
     TPQGPQSMNG ARMRCTAAIA PRRYEIDLPS ERLPTVAATG TPTTIYEGNA DIVNSTAVTG
     DITFQLEAEP VNETRFDFIL QFLGLDNDVP VVTVTSSTLV TADNYRGASA KFTQSIPTEM
     ITKPITRVKL AYQLNQQTAI ANAATLGAKG PASVSFSSGN GNVPGVLRPI TLVAYEKMTP
     QSILTVAGVS NYELIPNPDL LKNMVTKYGK YDPEGLNYAK MILSHREELD IRTVWRTEEY
     KERTRAFKEI TDFTSDLPTS KAWGWRDLVR GIRKVAAPVL STLFPMAAPL IGAADQFIGD
     LTKTNSAGGR YLSHAAGGRY HDVMDSWASG SEAGSYSKHL KTRLESNNYE EVELPKPTKG
     VIFPVVHTVE SAPGEAFGSL VVVIPEAYPE LLDPNQQVLS YFKNDTGCVW GIGEDIPFEG
     DDMCYTALPL KEIKRNGNIV VEKIFAGPAM GPSSQLALSL LVNDIDEGIP RMVFTGEIAD
     DEETVIPICG VDIKAIAAHE HGLPLIGCQP GVDEMVANTS LASHLIQGGA LPVQKAQGAC
     RRIKYLGQLM RTTASGMDAE LQGLLQATMA RAKEVKDAEV FKLLKLMSWT RKNDLTDHMY
     EWSKEDPDAI KFGRLVSTPP KHQEKPKGPD QHTAQEAKAT RISLDAVKAG ADFASPEWIA
     ENNYRGPSPG QFKYYMITGR VPNPGEEYED YVRKPITRPT DMDKIRRLAN SVYGLPHQEP
     APDDFYQAVV EVFAENGGRG PDQDQMQDLR DLARQMKRRP RPAETRRQTK TPPRAATSSG
     SRFTPSGDDG EV
//
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