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

 PB2_I33A0               Reviewed;         759 AA.
P03427;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
30-AUG-2017, entry version 92.
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/Wilson-Smith/1933 H1N1) (Influenza A virus
(strain A/WS/1933 H1N1)).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Orthomyxoviridae; Influenzavirus A.
NCBI_TaxID=381518;
NCBI_TaxID=8782; Aves.
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7045393;
Kaptein J.S., Nayak D.P.;
"Complete nucleotide sequence of the polymerase 3 gene of human
influenza virus A/WSN/33.";
J. Virol. 42:55-63(1982).
[2]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-736; ARG-737; LYS-738 AND
ARG-739.
PubMed=1985200;
Mukaigawa J., Nayak D.P.;
"Two signals mediate nuclear localization of influenza virus
(A/WSN/33) polymerase basic protein 2.";
J. Virol. 65:245-253(1991).
[3]
MUTAGENESIS OF TRP-49; TRP-78; PHE-130; ARG-142 AND LYS-190.
PubMed=12692212; DOI=10.1128/JVI.77.9.5098-5108.2003;
Gastaminza P., Perales B., Falcon A.M., Ortin J.;
"Mutations in the N-terminal region of influenza virus PB2 protein
affect virus RNA replication but not transcription.";
J. Virol. 77:5098-5108(2003).
[4]
FUNCTION, AND INTERACTION WITH PB1 AND NP.
PubMed=15033571; DOI=10.1016/j.virol.2003.12.022;
Poole E., Elton D., Medcalf L., Digard P.;
"Functional domains of the influenza A virus PB2 protein:
identification of NP- and PB1-binding sites.";
Virology 321:120-133(2004).
[5]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-7 AND LEU-10.
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).
[6]
ALTERNATIVE SPLICING (PB2-S1).
PubMed=26491155; DOI=10.1128/JVI.02175-15;
Yamayoshi S., Watanabe M., Goto H., Kawaoka Y.;
"Identification of a novel viral protein expressed from the PB2
segment of Influenza A virus.";
J. Virol. 90:444-456(2015).
-!- 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}.
-!- 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:15033571}.
-!- INTERACTION:
P49411:TUFM (xeno); NbExp=9; IntAct=EBI-8430745, EBI-359097;
-!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04062}.
Host nucleus {ECO:0000255|HAMAP-Rule:MF_04062}. Host mitochondrion
{ECO:0000255|HAMAP-Rule:MF_04062, ECO:0000269|PubMed:16242167,
ECO:0000269|PubMed:1985200}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P03427-1; Sequence=Displayed;
Name=PB2-S1 {ECO:0000303|PubMed:26491155};
IsoId=P0DOG3-1; Sequence=External;
-!- SIMILARITY: Belongs to the influenza viruses PB2 family.
{ECO:0000255|HAMAP-Rule:MF_04062, ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; J02179; AAA43611.1; -; Genomic_RNA.
ProteinModelPortal; P03427; -.
SMR; P03427; -.
IntAct; P03427; 169.
MINT; MINT-8081619; -.
OrthoDB; VOG0900002O; -.
PRO; PR:P03427; -.
GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
GO; GO:0075526; P:cap snatching; IEA:UniProtKB-KW.
GO; GO:0039689; P:negative stranded viral RNA replication; IDA:UniProtKB.
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.
HAMAP; MF_04062; INV_PB2; 1.
InterPro; IPR001591; RNA_pol_PB2_orthomyxovir.
Pfam; PF00604; Flu_PB2; 1.
ProDom; PD001667; RNA_pol_PB2_orthomyxovir; 1.
1: Evidence at protein level;
Alternative splicing; Cap snatching;
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; Viral immunoevasion; Viral transcription; Virion.
CHAIN 1 759 Polymerase basic protein 2.
/FTId=PRO_0000078841.
MOTIF 736 739 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_04062}.
SITE 627 627 Mammalian adaptation. {ECO:0000255|HAMAP-
Rule:MF_04062}.
MUTAGEN 7 7 L->A: Complete loss of mitochondrial
localization.
{ECO:0000269|PubMed:16242167}.
MUTAGEN 10 10 L->A: Complete loss of mitochondrial
localization.
{ECO:0000269|PubMed:16242167}.
MUTAGEN 49 49 W->A: Partial loss of replication. No
effect on transcription.
{ECO:0000269|PubMed:12692212}.
MUTAGEN 78 78 W->A: Complete loss of protein
expression.
{ECO:0000269|PubMed:12692212}.
MUTAGEN 130 130 F->A: Complete loss of replication. No
effect on transcription.
{ECO:0000269|PubMed:12692212}.
MUTAGEN 130 130 F->Y: Enhances viral replication.
{ECO:0000269|PubMed:12692212}.
MUTAGEN 142 142 R->A: Partial loss of replication. No
effect on transcription.
{ECO:0000269|PubMed:12692212}.
MUTAGEN 142 142 R->K: Partial loss of replication. No
effect on transcription.
{ECO:0000269|PubMed:12692212}.
MUTAGEN 190 190 K->A: No effect on replication or
transcription.
{ECO:0000269|PubMed:12692212}.
MUTAGEN 736 736 K->Q: Partial loss of nuclear
localization.
{ECO:0000269|PubMed:1985200}.
MUTAGEN 737 737 R->Q: Complete loss of nuclear
localization.
{ECO:0000269|PubMed:1985200}.
MUTAGEN 738 738 K->Q: Complete loss of nuclear
localization.
{ECO:0000269|PubMed:1985200}.
MUTAGEN 739 739 R->Q: Partial loss of nuclear
localization.
{ECO:0000269|PubMed:1985200}.
SEQUENCE 759 AA; 85796 MW; E7FA3844C44EB62D CRC64;
MERIKELRNL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPALRMKWM MAMKYPITAD
KRITEMIPER NEQGQTLWSK MNDAGSDRVM VSPLAVTWWN RNGPVTSTVH YPKIYKTYFE
KVERLKHGTF GPVHFRNQVK IRRRVDINPG HADLSAKEAQ DVIMEVVFPN EVGARILTSE
SQLTTTKEKK EELQGCKISP LMVAYMLERE LVRKTRFLPV AGGTSSVYIE VLHLTQGTCW
EQMYTPGGEA RNDDVDQSLI IAARNIVRRA TVSADPLASL LEMCHSTQIG GIRMVNILRQ
NPTEEQAVDI CKAAMGLRIS SSFSFGGFTF KRTSGSSVKR EEEVLTGNLQ TLKIRVHEGY
EEFTMVGRRA TAILRKATRR LIQLIVSGRD EQSIAEAIIV AMVFSQEDCM IKAVRGDLNF
VNRANQRLNP MHQLLRHFQK DAKALFQNWG IESIDNVMGM IGILPDMTPS TEMSMRGVRI
SKMGVDEYSS AEKIVVSIDR FLRVRDQRGN VLLSPEEVSE TQGTEKLTIT YSSSMMWEIN
GPESVLVNTY QWIIRNWETV KIQWSQNPTM LYNKMEFEPF QSLVPKAVRG QYSGFVRTLF
QQMRDVLGTF DTAQIIKLLP FAAAPPKQSG MQFSSLTINV RGSGMRILVR GNSPIFNYNK
TTKRLTVLGK DAGPLTEDPD EGTAGVESAV LRGFLILGKE DRRYGPALSI NELSNLAKGE
KANVLIGQGD VVLVMKRKRN SSILTDSQTA TKRIRMAIN


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