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Polymerase basic protein 2 (RNA-directed RNA polymerase subunit P3)

 PB2_I34A1               Reviewed;         759 AA.
P03428; A4GXH0; Q20N28; Q8JUU8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 2.
23-MAY-2018, entry version 121.
RecName: Full=Polymerase basic protein 2 {ECO:0000255|HAMAP-Rule:MF_04062};
AltName: Full=RNA-directed RNA polymerase subunit P3 {ECO:0000255|HAMAP-Rule:MF_04062};
Name=PB2 {ECO:0000255|HAMAP-Rule:MF_04062};
Influenza A virus (strain A/Puerto Rico/8/1934 H1N1).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Alphainfluenzavirus.
NCBI_TaxID=211044;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7060132; DOI=10.1016/0092-8674(82)90348-8;
Fields S., Winter G.;
"Nucleotide sequences of influenza virus segments 1 and 3 reveal
mosaic structure of a small viral RNA segment.";
Cell 28:303-313(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=11779399; DOI=10.1098/rstb.2001.0979;
Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L.,
Garcia-Sastre A., Palese P.;
"Plasmid-only rescue of influenza A virus vaccine candidates.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND REVERSE GENETICS.
PubMed=15163504; DOI=10.1016/j.virusres.2004.02.028;
de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F.,
Osterhaus A.D.M.E., Fouchier R.A.M.;
"Efficient generation and growth of influenza virus A/PR/8/34 from
eight cDNA fragments.";
Virus Res. 103:155-161(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
"The NIAID influenza genome sequencing project.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[5]
SUBCELLULAR LOCATION.
STRAIN=A/WSN/33;
PubMed=15308710; DOI=10.1128/JVI.78.17.9144-9153.2004;
Fodor E., Smith M.;
"The PA subunit is required for efficient nuclear accumulation of the
PB1 subunit of the influenza A virus RNA polymerase complex.";
J. Virol. 78:9144-9153(2004).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=A/WSN/33;
PubMed=16242167; DOI=10.1016/j.virol.2005.08.041;
Carr S.M., Carnero E., Garcia-Sastre A., Brownlee G.G., Fodor E.;
"Characterization of a mitochondrial-targeting signal in the PB2
protein of influenza viruses.";
Virology 344:492-508(2006).
[7]
FUNCTION.
PubMed=17030872; DOI=10.1099/vir.0.82199-0;
Deng T., Sharps J.L., Brownlee G.G.;
"Role of the influenza virus heterotrimeric RNA polymerase complex in
the initiation of replication.";
J. Gen. Virol. 87:3373-3377(2006).
[8]
FUNCTION, INTERACTION WITH HOST MAVS, AND SUBCELLULAR LOCATION.
PubMed=20538852; DOI=10.1128/JVI.00879-10;
Graef K.M., Vreede F.T., Lau Y.F., McCall A.W., Carr S.M.,
Subbarao K., Fodor E.;
"The PB2 subunit of the influenza virus RNA polymerase affects
virulence by interacting with the mitochondrial antiviral signaling
protein and inhibiting expression of beta interferon.";
J. Virol. 84:8433-8445(2010).
[9]
FUNCTION, AND INTERACTION WITH NUCLEOPROTEIN NP.
PubMed=22570712; DOI=10.1371/journal.pone.0036415;
Ng A.K., Chan W.H., Choi S.T., Lam M.K., Lau K.F., Chan P.K., Au S.W.,
Fodor E., Shaw P.C.;
"Influenza polymerase activity correlates with the strength of
interaction between nucleoprotein and PB2 through the host-specific
residue K/E627.";
PLoS ONE 7:E36415-E36415(2012).
[10]
FUNCTION, AND INTERACTION WITH HOST MAVS.
STRAIN=A/WSN/33;
PubMed=23246644; DOI=10.1016/j.virusres.2012.12.003;
Patel D., Schultz L.W., Umland T.C.;
"Influenza A polymerase subunit PB2 possesses overlapping binding
sites for polymerase subunit PB1 and human MAVS proteins.";
Virus Res. 172:75-80(2013).
[11]
FUNCTION, AND INTERACTION WITH NUCLEOPROTEIN NP.
STRAIN=A/WSN/193;
PubMed=25043584; DOI=10.1016/j.virol.2014.06.033;
Gui X., Li R., Zhang X., Shen C., Yu H., Guo X., Kang Y., Chen J.,
Chen H., Chen Y., Xia N.;
"An important amino acid in nucleoprotein contributes to influenza A
virus replication by interacting with polymerase PB2.";
Virology 464:11-20(2014).
[12]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 535-759.
PubMed=19144639; DOI=10.1074/jbc.C800224200;
Kuzuhara T., Kise D., Yoshida H., Horita T., Murazaki Y.,
Nishimura A., Echigo N., Utsunomiya H., Tsuge H.;
"Structural basis of the influenza A virus RNA polymerase PB2 RNA-
binding domain containing the pathogenicity-determinant lysine 627
residue.";
J. Biol. Chem. 284:6855-6860(2009).
[13]
X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 318-483.
PubMed=23436652; DOI=10.1074/jbc.M112.392878;
Liu Y., Qin K., Meng G., Zhang J., Zhou J., Zhao G., Luo M., Zheng X.;
"Structural and functional characterization of K339T substitution
identified in the PB2 subunit cap-binding pocket of influenza A
virus.";
J. Biol. Chem. 288:11013-11023(2013).
[14]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 318-484.
PubMed=24312396; DOI=10.1371/journal.pone.0082020;
Tsurumura T., Qiu H., Yoshida T., Tsumori Y., Hatakeyama D.,
Kuzuhara T., Tsuge H.;
"Conformational polymorphism of m7GTP in crystal structure of the PB2
middle domain from human influenza A virus.";
PLoS ONE 8:E82020-E82020(2013).
[15]
X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 318-484.
PubMed=24419622; DOI=10.1107/S2053230X13032603;
Tsurumura T., Qiu H., Yoshida T., Tsumori Y., Tsuge H.;
"Crystallization and preliminary X-ray diffraction studies of a
surface mutant of the middle domain of PB2 from human influenza A
(H1N1) virus.";
Acta Crystallogr. F 70:72-75(2014).
-!- FUNCTION: Plays an essential role in transcription initiation and
cap-stealing mechanism, in which cellular capped pre-mRNAs are
used to generate primers for viral transcription. Recognizes and
binds the 7-methylguanosine-containing cap of the target pre-RNA
which is subsequently cleaved after 10-13 nucleotides by the viral
protein PA. Plays a role in the initiation of the viral genome
replication and modulates the activity of the ribonucleoprotein
(RNP) complex. In addition, participates in the inhibition of type
I interferon induction through interaction with and inhibition of
the host mitochondrial antiviral signaling protein MAVS.
{ECO:0000255|HAMAP-Rule:MF_04062, ECO:0000269|PubMed:16242167,
ECO:0000269|PubMed:17030872, ECO:0000269|PubMed:20538852,
ECO:0000269|PubMed:22570712, ECO:0000269|PubMed:23246644,
ECO:0000269|PubMed:25043584}.
-!- SUBUNIT: Influenza RNA polymerase is composed of three subunits:
PB1, PB2 and PA. Interacts (via N-terminus) with PB1 (via C-
terminus). Interacts with nucleoprotein NP (via N-terminus).
Interacts (via N-terminus) with host MAVS (via N-terminus); this
interaction inhibits host innate immune response.
{ECO:0000255|HAMAP-Rule:MF_04062, ECO:0000269|PubMed:20538852,
ECO:0000269|PubMed:22570712, ECO:0000269|PubMed:23246644,
ECO:0000269|PubMed:25043584}.
-!- INTERACTION:
P03466:NP; NbExp=3; IntAct=EBI-2547475, EBI-2547640;
P03431:PB1; NbExp=3; IntAct=EBI-2547475, EBI-2547514;
-!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04062}.
Host nucleus {ECO:0000255|HAMAP-Rule:MF_04062,
ECO:0000269|PubMed:15308710, ECO:0000269|PubMed:20538852}. Host
mitochondrion {ECO:0000255|HAMAP-Rule:MF_04062,
ECO:0000269|PubMed:15308710, ECO:0000269|PubMed:16242167,
ECO:0000269|PubMed:20538852}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Polymerase basic protein 2;
IsoId=P03428-1; Sequence=Displayed;
Name=PB2-S1 {ECO:0000250|UniProtKB:P03427};
IsoId=P0DOG6-1; Sequence=External;
-!- SIMILARITY: Belongs to the influenza viruses PB2 family.
{ECO:0000255|HAMAP-Rule:MF_04062, ECO:0000305}.
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EMBL; V00603; CAA23855.1; -; Unassigned_RNA.
EMBL; AF389115; AAM75155.1; -; Genomic_RNA.
EMBL; EF467818; ABO21705.1; -; Genomic_RNA.
EMBL; CY009451; ABD77685.1; -; Genomic_RNA.
RefSeq; NP_040987.1; NC_002023.1.
PDB; 2ZTT; X-ray; 2.10 A; B/D=1-37.
PDB; 3A1G; X-ray; 1.70 A; B/D=1-37.
PDB; 3CW4; X-ray; 2.70 A; A=535-759.
PDB; 3WI0; X-ray; 2.00 A; A=318-484.
PDB; 3WI1; X-ray; 1.93 A; A=318-484.
PDB; 4ENF; X-ray; 1.32 A; A=318-483.
PDB; 4J2R; X-ray; 2.42 A; A/B=318-484.
PDB; 4U6O; X-ray; 1.30 A; A/B=318-483.
PDBsum; 2ZTT; -.
PDBsum; 3A1G; -.
PDBsum; 3CW4; -.
PDBsum; 3WI0; -.
PDBsum; 3WI1; -.
PDBsum; 4ENF; -.
PDBsum; 4J2R; -.
PDBsum; 4U6O; -.
ProteinModelPortal; P03428; -.
SMR; P03428; -.
DIP; DIP-43997N; -.
IntAct; P03428; 172.
MINT; P03428; -.
BindingDB; P03428; -.
ChEMBL; CHEMBL3317339; -.
GeneID; 956536; -.
KEGG; vg:956536; -.
KO; K19388; -.
OrthoDB; VOG0900002O; -.
Reactome; R-HSA-168255; Influenza Life Cycle.
Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis.
Reactome; R-HSA-168288; Fusion of the Influenza Virion to the Host Cell Endosome.
Reactome; R-HSA-168298; Release.
Reactome; R-HSA-168302; Budding.
Reactome; R-HSA-168303; Packaging of Eight RNA Segments.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-168330; Viral RNP Complexes in the Host Cell Nucleus.
Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
Reactome; R-HSA-168336; Uncoating of the Influenza Virion.
Reactome; R-HSA-192814; vRNA Synthesis.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-192869; cRNA Synthesis.
Reactome; R-HSA-192905; vRNP Assembly.
EvolutionaryTrace; P03428; -.
PRO; PR:P03428; -.
Proteomes; UP000009255; Genome.
Proteomes; UP000116373; Genome.
Proteomes; UP000170967; Genome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
GO; GO:0075526; P:cap snatching; IEA:UniProtKB-KW.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; TAS:Reactome.
GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
GO; GO:0039523; P:suppression by virus of host RNA polymerase II activity; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
GO; GO:0046761; P:viral budding from plasma membrane; TAS:Reactome.
GO; GO:0019070; P:viral genome maturation; TAS:Reactome.
GO; GO:0019072; P:viral genome packaging; TAS:Reactome.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
GO; GO:0019062; P:virion attachment to host cell; TAS:Reactome.
Gene3D; 3.30.30.90; -; 1.
HAMAP; MF_04062; INV_PB2; 1.
InterPro; IPR001591; INV_PB2.
InterPro; IPR037258; PDB2_C.
Pfam; PF00604; Flu_PB2; 1.
ProDom; PD001667; RNA_pol_PB2_orthomyxovir; 1.
SUPFAM; SSF160453; SSF160453; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cap snatching; Complete proteome;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host transcription shutoff by virus;
Host gene expression shutoff by virus; Host mitochondrion;
Host nucleus; Host-virus interaction;
Inhibition of host innate immune response by virus;
Inhibition of host MAVS by virus;
Inhibition of host RLR pathway by virus;
Inhibition of host RNA polymerase II by virus; mRNA capping;
mRNA processing; Reference proteome; Viral immunoevasion;
Viral transcription; Virion.
CHAIN 1 759 Polymerase basic protein 2.
/FTId=PRO_0000078834.
MOTIF 736 739 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_04062}.
SITE 627 627 Mammalian adaptation. {ECO:0000255|HAMAP-
Rule:MF_04062}.
CONFLICT 105 105 I -> M (in Ref. 1; ABD77685).
{ECO:0000305}.
CONFLICT 251 251 R -> K (in Ref. 1; ABD77685).
{ECO:0000305}.
CONFLICT 299 299 R -> K (in Ref. 1; ABD77685).
{ECO:0000305}.
CONFLICT 309 309 D -> G (in Ref. 1; ABD77685).
{ECO:0000305}.
CONFLICT 504 504 I -> V (in Ref. 1; ABD77685).
{ECO:0000305}.
CONFLICT 701 701 D -> N (in Ref. 2; ABO21705).
{ECO:0000305}.
CONFLICT 702 702 K -> R (in Ref. 1; ABD77685).
{ECO:0000305}.
HELIX 1 10 {ECO:0000244|PDB:3A1G}.
HELIX 14 22 {ECO:0000244|PDB:3A1G}.
HELIX 27 33 {ECO:0000244|PDB:3A1G}.
STRAND 323 325 {ECO:0000244|PDB:4U6O}.
STRAND 328 335 {ECO:0000244|PDB:4U6O}.
STRAND 338 345 {ECO:0000244|PDB:4U6O}.
STRAND 351 359 {ECO:0000244|PDB:4U6O}.
STRAND 361 366 {ECO:0000244|PDB:4U6O}.
STRAND 368 377 {ECO:0000244|PDB:4U6O}.
STRAND 380 390 {ECO:0000244|PDB:4U6O}.
HELIX 391 405 {ECO:0000244|PDB:4U6O}.
HELIX 408 411 {ECO:0000244|PDB:4U6O}.
TURN 418 420 {ECO:0000244|PDB:4U6O}.
HELIX 430 440 {ECO:0000244|PDB:4U6O}.
HELIX 443 449 {ECO:0000244|PDB:4U6O}.
STRAND 451 453 {ECO:0000244|PDB:4U6O}.
HELIX 456 458 {ECO:0000244|PDB:4J2R}.
STRAND 461 463 {ECO:0000244|PDB:4U6O}.
STRAND 469 475 {ECO:0000244|PDB:4U6O}.
STRAND 478 480 {ECO:0000244|PDB:4U6O}.
HELIX 536 540 {ECO:0000244|PDB:3CW4}.
HELIX 541 555 {ECO:0000244|PDB:3CW4}.
HELIX 557 566 {ECO:0000244|PDB:3CW4}.
HELIX 568 572 {ECO:0000244|PDB:3CW4}.
HELIX 575 577 {ECO:0000244|PDB:3CW4}.
HELIX 578 582 {ECO:0000244|PDB:3CW4}.
TURN 586 588 {ECO:0000244|PDB:3CW4}.
HELIX 589 605 {ECO:0000244|PDB:3CW4}.
HELIX 612 618 {ECO:0000244|PDB:3CW4}.
HELIX 619 622 {ECO:0000244|PDB:3CW4}.
STRAND 634 638 {ECO:0000244|PDB:3CW4}.
STRAND 641 643 {ECO:0000244|PDB:3CW4}.
STRAND 645 651 {ECO:0000244|PDB:3CW4}.
STRAND 656 658 {ECO:0000244|PDB:3CW4}.
STRAND 660 662 {ECO:0000244|PDB:3CW4}.
STRAND 664 674 {ECO:0000244|PDB:3CW4}.
STRAND 687 691 {ECO:0000244|PDB:3CW4}.
STRAND 694 699 {ECO:0000244|PDB:3CW4}.
HELIX 702 704 {ECO:0000244|PDB:3CW4}.
HELIX 710 714 {ECO:0000244|PDB:3CW4}.
STRAND 721 727 {ECO:0000244|PDB:3CW4}.
STRAND 730 736 {ECO:0000244|PDB:3CW4}.
SEQUENCE 759 AA; 86095 MW; 10D2D1608AE536D2 CRC64;
MERIKELRNL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPALRMKWM MAMKYPITAD
KRITEMIPER NEQGQTLWSK MNDAGSDRVM VSPLAVTWWN RNGPITNTVH YPKIYKTYFE
RVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE
SQLTITKEKK EELQDCKISP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW
EQMYTPGGEV RNDDVDQSLI IAARNIVRRA AVSADPLASL LEMCHSTQIG GIRMVDILRQ
NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSVKR EEEVLTGNLQ TLKIRVHEGY
EEFTMVGRRA TAILRKATRR LIQLIVSGRD EQSIAEAIIV AMVFSQEDCM IKAVRGDLNF
VNRANQRLNP MHQLLRHFQK DAKVLFQNWG VEPIDNVMGM IGILPDMTPS IEMSMRGVRI
SKMGVDEYSS TERVVVSIDR FLRIRDQRGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEIN
GPESVLVNTY QWIIRNWETV KIQWSQNPTM LYNKMEFEPF QSLVPKAIRG QYSGFVRTLF
QQMRDVLGTF DTAQIIKLLP FAAAPPKQSR MQFSSFTVNV RGSGMRILVR GNSPVFNYNK
ATKRLTVLGK DAGTLTEDPD EGTAGVESAV LRGFLILGKE DKRYGPALSI NELSNLAKGE
KANVLIGQGD VVLVMKRKRD SSILTDSQTA TKRIRMAIN


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EIAAB35796 DNA-directed RNA polymerase II subunit D,DNA-directed RNA polymerase II subunit RPB4,Homo sapiens,Human,POLR2D,RNA polymerase II 16 kDa subunit,RNA polymerase II subunit B4,RPB16
EIAAB35786 DNA-directed RNA polymerase II subunit J,DNA-directed RNA polymerase II subunit RPB11,Mouse,Mus musculus,Polr2j,RNA polymerase II 13.3 kDa subunit,RNA polymerase II subunit B11,RPB14,Rpo2-4
EIAAB35827 DNA-directed RNA polymerase III subunit G,DNA-directed RNA polymerase III subunit RPC7,Homo sapiens,Human,POLR3G,RNA polymerase III 32 kDa subunit,RNA polymerase III subunit C7,RPC32


 

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