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Q703G9

- POLS_IPNVS

UniProt

Q703G9 - POLS_IPNVS

Protein

Structural polyprotein

Gene
N/A
Organism
Infectious pancreatic necrosis virus (strain Sp) (IPNV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    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 similarity.By similarity
    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.By similarity
    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.PROSITE-ProRule annotation
    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.By similarity
    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.By similarity
    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.By similarity
    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi26 – 261Divalent metal cation; shared with trimeric partnersBy similarity
    Sitei442 – 4432Cleavage; by protease VP4
    Sitei486 – 4872Cleavage; by protease VP4
    Sitei495 – 4962Cleavage; by protease VP4
    Sitei508 – 5092Cleavage; by protease VP4
    Active sitei633 – 6331Nucleophile1 PublicationPROSITE-ProRule annotation
    Active sitei674 – 67411 PublicationPROSITE-ProRule annotation
    Sitei715 – 7162Cleavage; by protease VP4; subsidiary
    Sitei734 – 7352Cleavage; by protease VP4

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. serine-type peptidase activity Source: UniProtKB-KW
    3. structural molecule activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Ligandi

    Metal-binding

    Protein family/group databases

    MEROPSiS50.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Structural polyprotein
    Short name:
    PP
    Cleaved into the following 7 chains:
    Precursor of VP2
    Short name:
    Pre-VP2
    Structural peptide 1
    Short name:
    p1
    Structural peptide 2
    Short name:
    p2
    Structural peptide 3
    Short name:
    p3
    Alternative name(s):
    Non-structural protein VP4
    Short name:
    NS
    OrganismiInfectious pancreatic necrosis virus (strain Sp) (IPNV)
    Taxonomic identifieri11005 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesBirnaviridaeAquabirnavirus
    Virus hostiOncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) [TaxID: 8022]
    Salmo [TaxID: 8028]
    ProteomesiUP000007213: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell
    2. virion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cytoplasm, Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi508 – 5092AS → QL: Complete loss of pVP2-VP4 cleavage.
    Mutagenesisi547 – 5471H → S: Strongly reduced VP4-VP3 cleavage. No effect on pVP2-VP4 cleavage. 1 Publication
    Mutagenesisi573 – 5731D → Q: No effect on polyprotein processing. 1 Publication
    Mutagenesisi585 – 5851D → I: No effect on polyprotein processing. 1 Publication
    Mutagenesisi595 – 5951D → L: No effect on polyprotein processing. 1 Publication
    Mutagenesisi601 – 6011D → S: No effect on polyprotein processing. 1 Publication
    Mutagenesisi633 – 6331S → A, Q or T: Complete loss of protease activity. 1 Publication
    Mutagenesisi633 – 6331S → C: Partial loss of protease activity. 1 Publication
    Mutagenesisi644 – 6441D → I: No effect on polyprotein processing. 1 Publication
    Mutagenesisi660 – 6612DD → GS: No effect on polyprotein processing.
    Mutagenesisi672 – 6721D → N: No effect on polyprotein processing. 1 Publication
    Mutagenesisi674 – 6741K → A, D, H, Q or R: Complete loss of protease activity. 1 Publication
    Mutagenesisi675 – 6751A → D: 60% loss of pVP2-VP4 and VP4-VP3 cleavages. 1 Publication
    Mutagenesisi676 – 6761I → A: No effect on polyprotein processing. 1 Publication
    Mutagenesisi677 – 6771A → D: 60% loss of pVP2-VP4. Complete loss of VP4-VP3 cleavage. 1 Publication
    Mutagenesisi678 – 6781A → S: No effect on polyprotein processing. 1 Publication
    Mutagenesisi679 – 6791H → L: Strongly reduced VP4-VP3 cleavage. No effect on pVP2-VP4 cleavage. 1 Publication
    Mutagenesisi680 – 6801E → M: No effect on polyprotein processing. 1 Publication
    Mutagenesisi682 – 6821G → L: No effect on polyprotein processing. 1 Publication
    Mutagenesisi683 – 6831L → A: 60% loss of pVP2-VP4 and VP4-VP3 cleavages. 1 Publication
    Mutagenesisi684 – 6841P → Q: No effect on polyprotein processing. 1 Publication
    Mutagenesisi685 – 6851L → A: 60% loss of pVP2-VP4 and VP4-VP3 cleavages. 1 Publication
    Mutagenesisi686 – 6861I → A: 20% loss of pVP2-VP4 and VP4-VP3 cleavages. 1 Publication
    Mutagenesisi687 – 6871G → A: 20% loss of pVP2-VP4 and VP4-VP3 cleavages. 1 Publication
    Mutagenesisi689 – 6891Q → I: No effect on polyprotein processing. 1 Publication
    Mutagenesisi693 – 6931D → L: Strongly reduced VP4-VP3 cleavage. No effect on pVP2-VP4 cleavage. 1 Publication
    Mutagenesisi704 – 7041H → S: No effect on polyprotein processing. 1 Publication
    Mutagenesisi734 – 7352AS → LE: Complete loss of VP4-VP3 cleavage.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 508508Precursor of VP2PRO_0000392599Add
    BLAST
    Chaini1 – 442442Capsid protein VP2PRO_0000227873Add
    BLAST
    Peptidei443 – 48644Structural peptide 11 PublicationPRO_0000227874Add
    BLAST
    Peptidei487 – 4959Structural peptide 21 PublicationPRO_0000227875
    Peptidei496 – 50813Structural peptide 31 PublicationPRO_0000227876Add
    BLAST
    Chaini509 – 734226Protease VP4PRO_0000227877Add
    BLAST
    Chaini735 – 972238Capsid protein VP3PRO_0000227878Add
    BLAST

    Post-translational modificationi

    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.By similarity

    Interactioni

    Subunit structurei

    Capsid protein VP2 is a homotrimer. A central divalent metal stabilizes the VP2 trimer, possibly cobalt By similarity. Capsid protein VP3 is a homodimer. Capsid protein VP3 interacts (via C-terminus) with VP1 in the cytoplasm Capsid VP3 interacts with VP2 By similarity.By similarity

    Structurei

    Secondary structure

    1
    972
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 157
    Helixi17 – 193
    Beta strandi32 – 4413
    Beta strandi51 – 555
    Beta strandi60 – 7011
    Beta strandi74 – 8411
    Helixi89 – 913
    Beta strandi93 – 10715
    Beta strandi120 – 1289
    Helixi130 – 1323
    Helixi140 – 1434
    Helixi148 – 1503
    Beta strandi151 – 1566
    Turni157 – 1593
    Beta strandi161 – 1644
    Beta strandi202 – 2087
    Beta strandi210 – 2123
    Beta strandi223 – 23210
    Beta strandi236 – 24813
    Beta strandi254 – 26310
    Beta strandi271 – 28010
    Turni282 – 2865
    Beta strandi287 – 2926
    Helixi298 – 3003
    Beta strandi305 – 3139
    Helixi317 – 3193
    Beta strandi324 – 3263
    Helixi327 – 3293
    Beta strandi332 – 3387
    Turni339 – 3424
    Turni344 – 3463
    Beta strandi350 – 3578
    Beta strandi363 – 37614
    Helixi378 – 3814
    Helixi395 – 40410
    Turni405 – 4106
    Beta strandi413 – 4164
    Helixi417 – 4226
    Helixi425 – 4273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PNLX-ray2.21A/B/C/D/E/F/G/H/I/J514-716[»]
    2PNMX-ray2.30A524-716[»]
    3IDEX-ray3.35A/B/C/D/E1-442[»]
    ProteinModelPortaliQ703G9.
    SMRiQ703G9. Positions 514-716.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ703G9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini509 – 734226Peptidase S50PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 peptidase S50 domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di2.60.120.20. 2 hits.
    InterProiIPR002662. Birna_VP2.
    IPR002663. Birna_VP3.
    IPR025775. Birna_VP4_Prtase_dom.
    IPR029053. Viral_coat.
    [Graphical view]
    PfamiPF01766. Birna_VP2. 1 hit.
    PF01767. Birna_VP3. 1 hit.
    PF01768. Birna_VP4. 1 hit.
    [Graphical view]
    PROSITEiPS51548. BIRNAVIRUS_VP4_PRO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q703G9-1 [UniParc]FASTAAdd to Basket

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    MNTNKATATY LKSIMLPETG PASIPDDITE RHILKQETSS YNLEVSESGS    50
    GVLVCFPGAP GSRIGAHYRW NANQTGLEFD QWLETSQDLK KAFNYGRLIS 100
    RKYDIQSSTL PAGLYALNGT LNAATFEGSL SEVESLTYNS LMSLTTNPQD 150
    KVNNQLVTKG VTVLNLPTGF DKPYVRLEDE TPQGLQSMNG AKMRCTAAIA 200
    PRRYEIDLPS QRLPPVPATG TLTTLYEGNA DIVNSTTVTG DINFSLAEQP 250
    ADETKFDFQL DFMGLDNDVP VVTVVSSVLA TNDNYRGVSA KMTQSIPTEN 300
    ITKPITRVKL SYKINQQTAI GNVATLGTMG PASVSFSSGN GNVPGVLRPI 350
    TLVAYEKMTP LSILTVAGVS NYELIPNPEL LKNMVTRYGK YDPEGLNYAK 400
    MILSHREELD IRTVWRTEEY KERTRVFNEI TDFSSDLPTS KAWGWRDIVR 450
    GIRKVAAPVL STLFPMAAPL IGMADQFIGD LTKTNAAGGR YHSMAAGGRY 500
    KDVLESWASG GPDGKFSRAL KNRLESANYE EVELPPPSKG VIVPVVHTVK 550
    SAPGEAFGSL AIIIPGEYPE LLDANQQVLS HFANDTGSVW GIGEDIPFEG 600
    DNMCYTALPL KEIKRNGNIV VEKIFAGPIM GPSAQLGLSL LVNDIEDGVP 650
    RMVFTGEIAD DEETIIPICG VDIKAIAAHE QGLPLIGNQP GVDEEVRNTS 700
    LAAHLIQTGT LPVQRAKGSN KRIKYLGELM ASNASGMDEE LQRLLNATMA 750
    RAKEVQDAEI YKLLKLMAWT RKNDLTDHMY EWSKEDPDAL KFGKLISTPP 800
    KHPEKPKGPD QHHAQEARAT RISLDAVRAG ADFATPEWVA LNNYRGPSPG 850
    QFKYYLITGR EPEPGDEYED YIKQPIVKPT DMNKIRRLAN SVYGLPHQEP 900
    APEEFYDAVA AVFAQNGGRG PDQDQMQDLR ELARQMKRRP RNADAPRRTR 950
    APAEPAPPGR SRFTPSGDNA EV 972
    Length:972
    Mass (Da):106,646
    Last modified:July 5, 2004 - v1
    Checksum:i7B1448E99800E3C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti883 – 8831N → Y in AAR10446. (PubMed:15584407)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361Q → P in strain: Isolate Mason.
    Natural varianti46 – 461S → P in strain: Isolate Mason.
    Natural varianti52 – 521V → I in strain: Isolate Mason, Isolate Tseng, Isolate Blake, Isolate Sp103, Isolate Sp116, Isolate Sp122, Isolate NVI-001, Isolate NVI-011, Isolate NVI-013, Isolate NVI-015, Isolate NVI-016, Isolate NVI-020 and NVI-023.
    Natural varianti54 – 541V → I in strain: Isolate NVI-010.
    Natural varianti82 – 854WLET → CWRA in strain: Isolate Mason.
    Natural varianti152 – 1521V → A in strain: Isolate Mason, Isolate Blake and Isolate Tseng.
    Natural varianti192 – 1921K → R in strain: Isolate Mason, Isolate Blake and Isolate Tseng.
    Natural varianti199 – 1991I → T in strain: Isolate Sp103 and Isolate Sp122.
    Natural varianti212 – 2121R → S in strain: Isolate Mason, Isolate Blake and Isolate Tseng.
    Natural varianti217 – 2171P → T in strain: Isolate Sp122, Isolate NVI-001, Isolate NVI-011, Isolate NVI-013, Isolate NVI-015, Isolate NVI-020 and Isolate NVI-023.
    Natural varianti219 – 2191T → I in strain: Isolate NVI-010.
    Natural varianti221 – 2211T → A in strain: Isolate NVI-001, Isolate NVI-013, Isolate NVI-015, Isolate Sp116 and Isolate NVI-023.
    Natural varianti222 – 2221L → P in strain: Isolate NVI-011.
    Natural varianti234 – 2341N → S in strain: Isolate Tseng.
    Natural varianti247 – 2471A → T in strain: Isolate Sp122, Isolate NVI-001, Isolate NVI-013, Isolate NVI-015 and Isolate NVI-023.
    Natural varianti249 – 2491Q → R in strain: Isolate Tseng.
    Natural varianti252 – 2521D → N in strain: Isolate Mason, Isolate Tseng, Isolate Blake, Isolate Sp103, Isolate NVI-010 and Isolate NVI-016.
    Natural varianti252 – 2521D → V in strain: Isolate NVI-001, Isolate NVI-011, Isolate NVI-013, Isolate NVI-015, Isolate NVI-020, Isolate NVI-023, Isolate Sp116 and Isolate Sp122.
    Natural varianti255 – 2551K → R in strain: Isolate Mason, Isolate Blake and Isolate Tseng.
    Natural varianti262 – 2621F → L in strain: Isolate Mason.
    Natural varianti288 – 2881V → A in strain: Isolate Sp116.
    Natural varianti319 – 3191A → E in strain: Isolate NVI-016.
    Natural varianti323 – 3231V → A in strain: Isolate NVI-020.
    Natural varianti323 – 3231V → F in strain: Isolate NVI-016.
    Natural varianti432 – 4343DFS → EKT in strain: Isolate Mason.
    Natural varianti455 – 4551V → I in strain: Isolate Mason.
    Natural varianti473 – 4731M → T in strain: Isolate Mason, Isolate Heppel and Isolate Blake.
    Natural varianti500 – 5001Y → H in strain: Isolate Heppel, Isolate NVI-010, Isolate NVI-011, Isolate NVI-020, Isolate Sp103 and Isolate Sp116.
    Natural varianti565 – 5651P → R in strain: Isolate Mason.
    Natural varianti570 – 5712EL → SF in strain: Isolate Mason.
    Natural varianti672 – 6721D → A in strain: Isolate NVI-016.
    Natural varianti717 – 7171K → Q in strain: Isolate NVI-016.
    Natural varianti788 – 7881D → G in strain: Isolate NVI-011.
    Natural varianti788 – 7881D → Y in strain: Isolate NVI-001.
    Natural varianti802 – 8021H → R in strain: Isolate NVI-015 and Isolate NVI-016.
    Natural varianti841 – 8411L → M in strain: Isolate NVI-016.
    Natural varianti867 – 8671E → Q in strain: Isolate Mason and Isolate Blake.
    Natural varianti875 – 8751P → S in strain: Isolate NVI-016.
    Natural varianti882 – 8821M → T in strain: Isolate Tseng.
    Natural varianti953 – 9542AE → GK in strain: Isolate Mason.
    Natural varianti959 – 9602GR → DV in strain: Isolate Mason.
    Natural varianti968 – 9681D → N in strain: Isolate Sp116.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ622822 Genomic RNA. Translation: CAF22217.1.
    U48225 Genomic RNA. Translation: AAD11535.1.
    U56907 Genomic RNA. Translation: AAB39512.1.
    AY374435 Genomic RNA. Translation: AAQ75364.1.
    AY379735 Genomic RNA. Translation: AAQ75348.1.
    AY379736 Genomic RNA. Translation: AAQ75350.1.
    AY379737 Genomic RNA. Translation: AAQ75352.1.
    AY379738 Genomic RNA. Translation: AAQ75354.1.
    AY379740 Genomic RNA. Translation: AAQ75357.1.
    AY379742 Genomic RNA. Translation: AAQ75360.1.
    AY379744 Genomic RNA. Translation: AAQ75363.1.
    AY354519 Genomic RNA. Translation: AAR10446.1.
    AY354520 Genomic RNA. Translation: AAR10449.1.
    AY354521 Genomic RNA. Translation: AAR10452.1.
    AY823632 Genomic RNA. Translation: AAX24140.1.
    AF342728 mRNA. Translation: AAK32154.1.
    L13988 Genomic RNA. Translation: AAB00986.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ622822 Genomic RNA. Translation: CAF22217.1 .
    U48225 Genomic RNA. Translation: AAD11535.1 .
    U56907 Genomic RNA. Translation: AAB39512.1 .
    AY374435 Genomic RNA. Translation: AAQ75364.1 .
    AY379735 Genomic RNA. Translation: AAQ75348.1 .
    AY379736 Genomic RNA. Translation: AAQ75350.1 .
    AY379737 Genomic RNA. Translation: AAQ75352.1 .
    AY379738 Genomic RNA. Translation: AAQ75354.1 .
    AY379740 Genomic RNA. Translation: AAQ75357.1 .
    AY379742 Genomic RNA. Translation: AAQ75360.1 .
    AY379744 Genomic RNA. Translation: AAQ75363.1 .
    AY354519 Genomic RNA. Translation: AAR10446.1 .
    AY354520 Genomic RNA. Translation: AAR10449.1 .
    AY354521 Genomic RNA. Translation: AAR10452.1 .
    AY823632 Genomic RNA. Translation: AAX24140.1 .
    AF342728 mRNA. Translation: AAK32154.1 .
    L13988 Genomic RNA. Translation: AAB00986.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PNL X-ray 2.21 A/B/C/D/E/F/G/H/I/J 514-716 [» ]
    2PNM X-ray 2.30 A 524-716 [» ]
    3IDE X-ray 3.35 A/B/C/D/E 1-442 [» ]
    ProteinModelPortali Q703G9.
    SMRi Q703G9. Positions 514-716.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S50.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q703G9.

    Family and domain databases

    Gene3Di 2.60.120.20. 2 hits.
    InterProi IPR002662. Birna_VP2.
    IPR002663. Birna_VP3.
    IPR025775. Birna_VP4_Prtase_dom.
    IPR029053. Viral_coat.
    [Graphical view ]
    Pfami PF01766. Birna_VP2. 1 hit.
    PF01767. Birna_VP3. 1 hit.
    PF01768. Birna_VP4. 1 hit.
    [Graphical view ]
    PROSITEi PS51548. BIRNAVIRUS_VP4_PRO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Peptides resulting from the pVP2 C-terminal processing are present in infectious pancreatic necrosis virus particles."
      Galloux M., Chevalier C., Henry C., Huet J.-C., Da Costa B., Delmas B.
      J. Gen. Virol. 85:2231-2236(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 443-457; 487-495 AND 496-508, PROTEOLYTIC PROCESSING OF POLYPROTEIN.
      Strain: 31-75.
    2. Mason C.L., Leong J.C.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Mason.
    3. Tseng C.-C., Lo C.-F., Kou G.-H.
      Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Tseng.
    4. "Identification of putative motifs involved in the virulence of infectious pancreatic necrosis virus."
      Santi N., Vakharia V.N., Evensen O.
      Virology 322:31-40(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate NVI-001, Isolate NVI-010, Isolate NVI-011, Isolate NVI-013, Isolate NVI-015, Isolate NVI-016, Isolate NVI-020 and Isolate NVI-023.
    5. "Molecular characterization of Sp serotype strains of infectious pancreatic necrosis virus exhibiting differences in virulence."
      Shivappa R.B., Song H., Yao K., Aas-Eng A., Evensen O., Vakharia V.N.
      Dis. Aquat. Organ. 61:23-32(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Sp103, Isolate Sp116 and Isolate Sp122.
    6. "Infectious pancreatic necrosis virus VP5 is dispensable for virulence and persistence."
      Santi N., Song H., Vakharia V.N., Evensen O.
      J. Virol. 79:9206-9216(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Sp103.
    7. "Phylogenetic relationships of aquatic birnaviruses based on deduced amino acid sequences of genome segment A cDNA."
      Blake S., Ma J.Y., Caporale D.A., Jairath S., Nicholson B.L.
      Dis. Aquat. Organ. 45:89-102(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-968.
      Strain: Isolate Blake.
    8. "Comparison of amino acid sequences deduced from a cDNA fragment obtained from infectious pancreatic necrosis virus (IPNV) strains of different serotypes."
      Heppell J., Berthiaume L., Corbin F., Tarrab E., Lecomte J., Arella M.
      Virology 195:840-844(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 437-539.
      Strain: Isolate Heppell.
    9. "Active residues and viral substrate cleavage sites of the protease of the birnavirus infectious pancreatic necrosis virus."
      Petit S., Lejal N., Huet J.-C., Delmas B.
      J. Virol. 74:2057-2066(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 509-515; 716-723 AND 735-740, ACTIVE SITES OF PROTEASE VP4, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF 486-ALA-ALA-487; 495-ALA-ALA-496; 508-ALA-SER-509; HIS-547; ASP-573; ASP-585; ASP-595; ASP-601; SER-633; ASP-644; 660-ASP-ASP-661; ASP-672; LYS-674; ALA-675; ILE-676; ALA-677; ALA-678; HIS-679; GLU-680; GLY-682; LEU-683; PRO-684; LEU-685; ILE-686; GLY-687; GLN-689; ASP-693; HIS-704 AND 734-ALA-SER-735.
      Strain: 31-75.
    10. "Structure of birnavirus-like particles determined by combined electron cryomicroscopy and X-ray crystallography."
      Pous J., Chevalier C., Ouldali M., Navaza J., Delmas B., Lepault J.
      J. Gen. Virol. 86:2339-2346(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY (15 ANGSTROMS) OF VIRAL PARTICLES.
      Strain: 31-75.
    11. "Crystal structure of the VP4 protease from infectious pancreatic necrosis virus reveals the acyl-enzyme complex for an intermolecular self-cleavage reaction."
      Lee J., Feldman A.R., Delmas B., Paetzel M.
      J. Biol. Chem. 282:24928-24937(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 514-716.

    Entry informationi

    Entry nameiPOLS_IPNVS
    AccessioniPrimary (citable) accession number: Q703G9
    Secondary accession number(s): P90205
    , Q4KTX8, Q69CH7, Q69CI0, Q69CI3, Q6U2N3, Q6U2N5, Q6U2N8, Q6U2P1, Q6U2P5, Q6U2P7, Q6UAY7, Q82733, Q990Q0, Q9YJV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The sequence shown is that of strain 31-75. Isolate Sp103 is VP5-deficient.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3