NS1_I72A2
ID NS1_I72A2 Reviewed; 237 AA.
AC P03495; Q1K9D5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 138.
DE RecName: Full=Non-structural protein 1 {ECO:0000255|HAMAP-Rule:MF_04066};
DE Short=NS1 {ECO:0000255|HAMAP-Rule:MF_04066};
DE AltName: Full=NS1A {ECO:0000255|HAMAP-Rule:MF_04066};
GN Name=NS {ECO:0000255|HAMAP-Rule:MF_04066};
OS Influenza A virus (strain A/Udorn/307/1972 H3N2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=381517;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9721; Cetacea (whales).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9709; Phocidae (true seals).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7407920; DOI=10.1016/0092-8674(80)90484-5;
RA Lamb R.A., Lai C.-J.;
RT "Sequence of interrupted and uninterrupted mRNAs and cloned DNA coding for
RT the two overlapping nonstructural proteins of influenza virus.";
RL Cell 21:475-485(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Mbawuike I.N., Zhang Y., Yamada R.E., Nino D., Bui H.-H., Sette A.,
RA Couch R.B.;
RT "Complete genome sequencing and analysis of selected influenza virus
RT vaccine strains spanning six decades (1933-1999).";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP MUTAGENESIS OF 7-SER-SER-8; 19-ARG-PHE-20; 31-PRO-PHE-32; 35-ARG--ARG-38;
RP 39-ASP-GLN-40; 48-SER-THR-49; 62-LYS-GLN-63; 73-SER-ASP-74; 87-SER-ARG-88;
RP 99-SER-ARG-100; 116-CYS-ILE-117; 134-PHE--VAL-136; LEU-141; LEU-144;
RP LEU-146; 150-PHE-THR-151; 160-ILE-SER-161; 175-LYS-ASN-176;
RP 199-GLN-ARG-200; 205-SER-SER-206 AND 219-LYS-LYS-221.
RX PubMed=8139028; DOI=10.1128/jvi.68.4.2433-2441.1994;
RA Qian X.Y., Alonso-Caplen F., Krug R.M.;
RT "Two functional domains of the influenza virus NS1 protein are required for
RT regulation of nuclear export of mRNA.";
RL J. Virol. 68:2433-2441(1994).
RN [4]
RP DIMERIZATION.
RX PubMed=7571411; DOI=10.1006/viro.1995.1499;
RA Nemeroff M.E., Qian X.Y., Krug R.M.;
RT "The influenza virus NS1 protein forms multimers in vitro and in vivo.";
RL Virology 212:422-428(1995).
RN [5]
RP RNA-BINDING.
RX PubMed=8806538; DOI=10.1006/viro.1996.0453;
RA Wang W., Krug R.M.;
RT "The RNA-binding and effector domains of the viral NS1 protein are
RT conserved to different extents among influenza A and B viruses.";
RL Virology 223:41-50(1996).
RN [6]
RP FUNCTION, AND INTERACTION WITH HUMAN CPSF4.
RX PubMed=9651582; DOI=10.1016/s1097-2765(00)80099-4;
RA Nemeroff M.E., Barabino S.M.L., Li Y., Keller W., Krug R.M.;
RT "Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of
RT CPSF and inhibits 3'end formation of cellular pre-mRNAs.";
RL Mol. Cell 1:991-1000(1998).
RN [7]
RP INTERACTION WITH HUMAN EIF2AK2/PKR.
RX PubMed=9781815; DOI=10.1089/jir.1998.18.757;
RA Tan S.L., Katze M.G.;
RT "Biochemical and genetic evidence for complex formation between the
RT influenza A virus NS1 protein and the interferon-induced PKR protein
RT kinase.";
RL J. Interferon Cytokine Res. 18:757-766(1998).
RN [8]
RP FUNCTION.
RX PubMed=9560194; DOI=10.1073/pnas.95.9.4864;
RA Li Y., Yamakita Y., Krug R.M.;
RT "Regulation of a nuclear export signal by an adjacent inhibitory sequence:
RT the effector domain of the influenza virus NS1 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4864-4869(1998).
RN [9]
RP INTERACTION WITH HUMAN PABPN1.
RX PubMed=10205180; DOI=10.1093/emboj/18.8.2273;
RA Chen Z., Li Y., Krug R.M.;
RT "Influenza A virus NS1 protein targets poly(A)-binding protein II of the
RT cellular 3'-end processing machinery.";
RL EMBO J. 18:2273-2283(1999).
RN [10]
RP MUTAGENESIS OF 186-GLU-TRP-187; 201-PHE--TRP-203 AND 212-PRO-PRO-213.
RX PubMed=11421366; DOI=10.1017/s1355838201010226;
RA Li Y., Chen Z.Y., Wang W., Baker C.C., Krug R.M.;
RT "The 3'-end-processing factor CPSF is required for the splicing of single-
RT intron pre-mRNAs in vivo.";
RL RNA 7:920-931(2001).
RN [11]
RP REVIEW.
RX PubMed=12758165; DOI=10.1016/s0042-6822(03)00119-3;
RA Krug R.M., Yuan W., Noah D.L., Latham A.G.;
RT "Intracellular warfare between human influenza viruses and human cells: the
RT roles of the viral NS1 protein.";
RL Virology 309:181-189(2003).
RN [12]
RP FUNCTION, AND INTERACTION WITH HOST CPSF4.
RX PubMed=16571812; DOI=10.1128/jvi.80.8.3957-3965.2006;
RA Twu K.Y., Noah D.L., Rao P., Kuo R.L., Krug R.M.;
RT "The CPSF30 binding site on the NS1A protein of influenza A virus is a
RT potential antiviral target.";
RL J. Virol. 80:3957-3965(2006).
RN [13]
RP STRUCTURE BY NMR OF 1-73.
RX PubMed=9360601; DOI=10.1038/nsb1197-891;
RA Chien C.Y., Tejero R., Huang Y., Zimmerman D.E., Rios C.B., Krug R.M.,
RA Montelione G.T.;
RT "A novel RNA-binding motif in influenza A virus non-structural protein 1.";
RL Nat. Struct. Biol. 4:891-895(1997).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-72.
RX PubMed=9360602; DOI=10.1038/nsb1197-896;
RA Liu J., Lynch P.A., Chien C.Y., Montelione G.T., Krug R.M., Berman H.M.;
RT "Crystal structure of the unique RNA-binding domain of the influenza virus
RT NS1 protein.";
RL Nat. Struct. Biol. 4:896-899(1997).
CC -!- FUNCTION: Inhibits post-transcriptional processing of cellular pre-
CC mRNA, by binding and inhibiting two cellular proteins that are required
CC for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage
CC and polyadenylation specificity factor/CPSF4 and the poly(A)-binding
CC protein 2/PABPN1. In turn, unprocessed 3' end pre-mRNAs accumulate in
CC the host nucleus and are no longer exported to the cytoplasm. Cellular
CC protein synthesis is thereby shut off very early after virus infection.
CC Viral protein synthesis is not affected by the inhibition of the
CC cellular 3' end processing machinery because the poly(A) tails of viral
CC mRNAs are produced by the viral polymerase through a stuttering
CC mechanism. {ECO:0000255|HAMAP-Rule:MF_04066,
CC ECO:0000269|PubMed:16571812, ECO:0000269|PubMed:9560194,
CC ECO:0000269|PubMed:9651582}.
CC -!- FUNCTION: Prevents the establishment of the cellular antiviral state by
CC inhibiting TRIM25-mediated DDX58 ubiquitination, which normally
CC triggers the antiviral transduction signal that leads to the activation
CC of type I IFN genes by transcription factors IRF3 and IRF7. Prevents
CC human EIF2AK2/PKR activation, either by binding double-strand RNA, or
CC by interacting directly with EIF2AK2/PKR. This function may be
CC important at the very beginning of the infection, when NS1 is mainly
CC present in the cytoplasm. Also binds poly(A) and U6 snRNA.
CC {ECO:0000255|HAMAP-Rule:MF_04066}.
CC -!- SUBUNIT: Homodimer. Interacts with host TRIM25 (via coiled coil); this
CC interaction specifically inhibits TRIM25 multimerization and TRIM25-
CC mediated DDX58 CARD ubiquitination. Interacts with human EIF2AK2/PKR,
CC CPSF4, IVNS1ABP and PABPN1. {ECO:0000255|HAMAP-Rule:MF_04066,
CC ECO:0000269|PubMed:10205180, ECO:0000269|PubMed:16571812,
CC ECO:0000269|PubMed:9651582, ECO:0000269|PubMed:9781815}.
CC -!- INTERACTION:
CC P03495; P03495: NS; NbExp=3; IntAct=EBI-2548993, EBI-2548993;
CC P03495; Q92934: BAD; Xeno; NbExp=2; IntAct=EBI-2548993, EBI-700771;
CC P03495; O43521: BCL2L11; Xeno; NbExp=2; IntAct=EBI-2548993, EBI-526406;
CC P03495; O95639-1: CPSF4; Xeno; NbExp=4; IntAct=EBI-2548993, EBI-15725265;
CC P03495; O60869: EDF1; Xeno; NbExp=2; IntAct=EBI-2548993, EBI-781301;
CC P03495; Q9UII4: HERC5; Xeno; NbExp=3; IntAct=EBI-2548993, EBI-2339540;
CC P03495; Q13651: IL10RA; Xeno; NbExp=2; IntAct=EBI-2548993, EBI-1031656;
CC P03495; P35568: IRS1; Xeno; NbExp=2; IntAct=EBI-2548993, EBI-517592;
CC P03495; P05161: ISG15; Xeno; NbExp=4; IntAct=EBI-2548993, EBI-746466;
CC P03495; Q9UBF8: PI4KB; Xeno; NbExp=2; IntAct=EBI-2548993, EBI-1053214;
CC P03495; P04049: RAF1; Xeno; NbExp=2; IntAct=EBI-2548993, EBI-365996;
CC P03495; P29353: SHC1; Xeno; NbExp=2; IntAct=EBI-2548993, EBI-78835;
CC P03495; Q92844: TANK; Xeno; NbExp=2; IntAct=EBI-2548993, EBI-356349;
CC P03495; P55916: UCP3; Xeno; NbExp=2; IntAct=EBI-2548993, EBI-9116865;
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04066}.
CC Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04066}. Note=In uninfected,
CC transfected cells, NS1 is localized in the nucleus. Only in virus
CC infected cells, the nuclear export signal is unveiled, presumably by a
CC viral protein, and a fraction of NS1 is exported in the cytoplasm.
CC {ECO:0000255|HAMAP-Rule:MF_04066}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=NS1;
CC IsoId=P03495-1; Sequence=Displayed;
CC Name=NEP; Synonyms=NS2;
CC IsoId=P69258-1; Sequence=External;
CC -!- DOMAIN: The dsRNA-binding region is required for suppression of RNA
CC silencing. {ECO:0000255|HAMAP-Rule:MF_04066}.
CC -!- PTM: Upon interferon induction, ISGylated via host HERC5; this results
CC in the impairment of NS1 interaction with RNA targets due to its
CC inability to form homodimers and to interact with host EIF2AK2/PKR.
CC {ECO:0000255|HAMAP-Rule:MF_04066}.
CC -!- SIMILARITY: Belongs to the influenza A viruses NS1 family.
CC {ECO:0000255|HAMAP-Rule:MF_04066}.
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DR EMBL; V01102; CAA24288.1; -; Genomic_RNA.
DR EMBL; DQ508933; ABF21224.1; -; Genomic_RNA.
DR PIR; A04088; MNIV1A.
DR PDB; 1AIL; X-ray; 1.90 A; A=1-72.
DR PDB; 1NS1; NMR; -; A/B=1-73.
DR PDB; 2KKZ; NMR; -; A=85-215.
DR PDB; 2RHK; X-ray; 1.95 A; A/B=85-215.
DR PDB; 3EE8; X-ray; 2.60 A; A/B=84-205.
DR PDB; 3EE9; X-ray; 2.14 A; A/B=84-205.
DR PDB; 3KWG; X-ray; 2.21 A; A/B=78-205.
DR PDB; 3KWI; X-ray; 2.21 A; A/B=78-205.
DR PDB; 4NW2; X-ray; 1.90 A; B/D=216-230.
DR PDB; 4O45; X-ray; 1.87 A; B=216-230.
DR PDBsum; 1AIL; -.
DR PDBsum; 1NS1; -.
DR PDBsum; 2KKZ; -.
DR PDBsum; 2RHK; -.
DR PDBsum; 3EE8; -.
DR PDBsum; 3EE9; -.
DR PDBsum; 3KWG; -.
DR PDBsum; 3KWI; -.
DR PDBsum; 4NW2; -.
DR PDBsum; 4O45; -.
DR BMRB; P03495; -.
DR SMR; P03495; -.
DR DIP; DIP-46282N; -.
DR ELM; P03495; -.
DR IntAct; P03495; 61.
DR MINT; P03495; -.
DR EvolutionaryTrace; P03495; -.
DR Proteomes; UP000153055; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; TAS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0052038; P:modulation by symbiont of host intracellular transport; IDA:BHF-UCL.
DR GO; GO:0019056; P:modulation by virus of host transcription; IDA:BHF-UCL.
DR GO; GO:0052170; P:suppression by symbiont of host innate immune response; IDA:BHF-UCL.
DR GO; GO:0046775; P:suppression by virus of host cytokine production; IDA:BHF-UCL.
DR GO; GO:0039524; P:suppression by virus of host mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0039580; P:suppression by virus of host PKR signaling; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.330; -; 1.
DR HAMAP; MF_04066; INFV_NS1; 1.
DR InterPro; IPR004208; NS1.
DR InterPro; IPR000256; NS1A.
DR InterPro; IPR038064; NS1A_effect_dom-like_sf.
DR InterPro; IPR009068; S15_NS1_RNA-bd.
DR Pfam; PF00600; Flu_NS1; 1.
DR SUPFAM; SSF143021; SSF143021; 1.
DR SUPFAM; SSF47060; SSF47060; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing;
KW Eukaryotic host gene expression shutoff by virus; Host cytoplasm;
KW Host gene expression shutoff by virus; Host mRNA suppression by virus;
KW Host nucleus; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host PKR by virus;
KW Inhibition of host pre-mRNA processing by virus;
KW Inhibition of host RIG-I by virus; Inhibition of host RLR pathway by virus;
KW Interferon antiviral system evasion; RNA-binding; Ubl conjugation;
KW Viral immunoevasion.
FT CHAIN 1..237
FT /note="Non-structural protein 1"
FT /id="PRO_0000078952"
FT REGION 1..73
FT /note="RNA-binding and homodimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04066"
FT REGION 180..215
FT /note="CPSF4-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04066"
FT REGION 205..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..237
FT /note="PABPN1-binding"
FT REGION 223..230
FT /note="PABPN1-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04066"
FT MOTIF 34..38
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04066"
FT MOTIF 34..38
FT /note="Nuclear localization signal 1"
FT MOTIF 137..146
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04066"
FT MOTIF 216..221
FT /note="Nuclear localization signal 2"
FT MUTAGEN 7..8
FT /note="SS->AA: No effect on nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 7..8
FT /note="SS->DL: Complete loss of nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 19..20
FT /note="RK->AA,DL: Complete loss of nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 31..32
FT /note="PF->AA: Complete loss of nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 35..38
FT /note="RLRR->ALAA: 75% loss of nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 39..40
FT /note="DQ->AA: No effect on nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 48..49
FT /note="ST->DL: No effect on nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 62..63
FT /note="KQ->AA: No effect on nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 62..63
FT /note="KQ->DL: Complete loss of nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 73..74
FT /note="SD->DL: No effect on nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 87..88
FT /note="SR->DL: No effect on nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 99..100
FT /note="SR->DL: No effect on nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 116..117
FT /note="CI->DL: No effect on nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 134..136
FT /note="FSV->AAA,LDL: Complete loss of nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 141
FT /note="L->A: No effect on nuclear mRNA export inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 144
FT /note="L->A: Complete loss of nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 146
FT /note="L->A: Complete loss of nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 150..151
FT /note="FT->AA,DL: Complete loss of nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 160..161
FT /note="IS->AA,DL: Complete loss of nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 175..176
FT /note="KN->AA: No effect on nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 186..187
FT /note="EW->AS: Complete loss of CPSF4 binding."
FT /evidence="ECO:0000269|PubMed:11421366"
FT MUTAGEN 199..200
FT /note="QR->AA: No effect on nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 201..203
FT /note="FAW->AAA: No effect on CPSF4 binding."
FT /evidence="ECO:0000269|PubMed:11421366"
FT MUTAGEN 205..206
FT /note="SS->AA: No effect on nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT MUTAGEN 212..213
FT /note="PP->AA: No effect on CPSF4 binding."
FT /evidence="ECO:0000269|PubMed:11421366"
FT MUTAGEN 219..221
FT /note="KRK->ARA: No effect on nuclear mRNA export
FT inhibition."
FT /evidence="ECO:0000269|PubMed:8139028"
FT HELIX 3..24
FT /evidence="ECO:0007829|PDB:1AIL"
FT HELIX 30..50
FT /evidence="ECO:0007829|PDB:1AIL"
FT HELIX 54..69
FT /evidence="ECO:0007829|PDB:1AIL"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2RHK"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:2RHK"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:2RHK"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:2RHK"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:2RHK"
FT STRAND 140..151
FT /evidence="ECO:0007829|PDB:2RHK"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:2RHK"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3KWI"
FT HELIX 171..187
FT /evidence="ECO:0007829|PDB:2RHK"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:2RHK"
FT HELIX 196..201
FT /evidence="ECO:0007829|PDB:2RHK"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:2KKZ"
SQ SEQUENCE 237 AA; 26846 MW; 14D0308795627E5E CRC64;
MDSNTVSSFQ VDCFLWHVRK QVVDQELGDA PFLDRLRRDQ KSLRGRGSTL GLNIEAATHV
GKQIVEKILK EESDEALKMT MASTPASRYI TDMTIEELSR DWFMLMPKQK VEGPLCIRID
QAIMDKNIML KANFSVIFDR LETLILLRAF TEEGAIVGEI SPLPSFPGHT IEDVKNAIGV
LIGGLEWNDN TVRVSKTLQR FAWGSSNENG RPPLTPKQKR KMARTARSKV RRDKMAD
