POLS_IPNVN
ID POLS_IPNVN Reviewed; 972 AA.
AC P22495;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 N1) (IPNV).
OC Viruses; Riboviria; Orthornavirae; Birnaviridae; Aquabirnavirus.
OX NCBI_TaxID=11004;
OH NCBI_TaxID=8022; Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OH NCBI_TaxID=8028; Salmo.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2307963; DOI=10.1099/0022-1317-71-2-299;
RA Havarstein L.S., Kalland K.H., Christie K.E., Endresen C.;
RT "Sequence of the large double-stranded RNA segment of the N1 strain of
RT infectious pancreatic necrosis virus: a comparison with other
RT Birnaviridae.";
RL J. Gen. Virol. 71:299-308(1990).
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 similarity).
CC {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 -!- SUBUNIT: Capsid protein VP2 is a homotrimer. A central divalent metal
CC stabilizes the VP2 trimer, possibly cobalt (By similarity). Capsid
CC protein VP3 is a homodimer. Capsid protein VP3 interacts (via C-
CC terminus) with VP1 in the cytoplasm Capsid VP3 interacts with VP2 (By
CC similarity). {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. 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; D00701; BAA00609.1; -; Genomic_RNA.
DR PIR; B34148; GNXSN1.
DR SMR; P22495; -.
DR MEROPS; S50.001; -.
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..508
FT /note="Precursor of VP2"
FT /id="PRO_0000392598"
FT CHAIN 1..442
FT /note="Capsid protein VP2"
FT /id="PRO_0000036783"
FT PEPTIDE 443..486
FT /note="Structural peptide 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227862"
FT PEPTIDE 487..495
FT /note="Structural peptide 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227863"
FT PEPTIDE 496..508
FT /note="Structural peptide 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000227864"
FT CHAIN 509..734
FT /note="Protease VP4"
FT /id="PRO_0000036784"
FT CHAIN 735..972
FT /note="Capsid protein VP3"
FT /id="PRO_0000036785"
FT DOMAIN 509..734
FT /note="Peptidase S50"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00881"
FT REGION 794..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..948
FT /note="Basic and acidic 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 /evidence="ECO:0000250"
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 715..716
FT /note="Cleavage; by protease VP4; subsidiary"
FT /evidence="ECO:0000250"
FT SITE 734..735
FT /note="Cleavage; by protease VP4"
FT /evidence="ECO:0000250"
SQ SEQUENCE 972 AA; 106670 MW; E59E9785616A2998 CRC64;
MNTNKATATY LKSIMLPETG PASIPDDITE RHILKQETSS YNLEVSESGS GILVCFPGAP
GSRIGAHYRW NANQTGLEFD QWLETSQDLK KAFNYGRLIS RKYDIQSSTL PAGLYALNGT
LNAATFEGSL SEVESLTYNS LMSLTTNPQD KVNNQLVTKG VTVLNLPTGF DKPYVRLEDE
TPQGLQSMNG AKMRCTAAIA PRRYEIDLPS QRLPPVPATG TLTTLYEGNA DIVNSTTVTG
DINFSLAEQP ANETKFDFQL DFMGLDNDVP VVTVVSSVLA TNDNYRGVSA KMTQSIPTEN
ITKPITRVKL SYKINQQTAI GNVATLGTMG PTTVSFSSGN GNVPGVLRPI TLVAYEKMTP
LSILTVAGVS NYESYPNPEL LKNMVTRYGK YDPEGLNYAK MILSHREELD IRTVWRTEEY
KERTRVFNEI TDFSSDLPTS KAWGWRDIVR GIRKVAAPVL STLFPMAAPL IGMADQFIGD
LTKTNAAGGR YHSMAAGGRH KDVLESWASG GPDGKFSRAL KNRLESANYE EVELPPPSKG
VIVPVVHTVK SAPGEAFGSL AIIIPGEYPE LLDANQQVLS HFANDTGSVW GIGEDIPFEG
DNMCYTALPL KEIKRNGNIV VEKIFAGPIM GPSAQLGLSL LVNDIEDGVP RMVFTGEIAD
DEETIIPICG VDIKAIAAHE PGLPLIGNQP GVDEEVRNTS LAAHLIQTGT LPVQRAKGSN
KRIKYLGELM ASNASGMDEE LQRLLNATMA RAKEVQDAEI YKLLKLMAWT RKNDLTDHMY
EWSKEDPDAL KFGKLISTPP KHPEKPKGPD QHHAQEARAT RISLDAVRAG ADFATPEWVA
LNNYRGPSPG QFKYYLITGR EPEPGDEYED YIKQPIVKPT DMNKIRRLAN SVYGLPHQEP
APEEFYDAVA AVFAQNGGRG PDQDQMQDLR ELARQMKRRP RNADAPRRTR APAEPAPPGR
SRFTPSGDNA EV
