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 03-AUG-2022, entry version 102.
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.
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; 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 MEROPS; S50.001; -.
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 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 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 REGION 797..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 BINDING 26
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="ligand shared between trimeric 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:0007829|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
