PA_I34A1
ID PA_I34A1 Reviewed; 716 AA.
AC P03433; A4GXH3; Q20N31; Q8JUU6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Polymerase acidic protein {ECO:0000255|HAMAP-Rule:MF_04063};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04063};
DE AltName: Full=RNA-directed RNA polymerase subunit P2 {ECO:0000255|HAMAP-Rule:MF_04063};
GN Name=PA {ECO:0000255|HAMAP-Rule:MF_04063};
OS Influenza A virus (strain A/Puerto Rico/8/1934 H1N1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=211044;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7060132; DOI=10.1016/0092-8674(82)90348-8;
RA Fields S., Winter G.;
RT "Nucleotide sequences of influenza virus segments 1 and 3 reveal mosaic
RT structure of a small viral RNA segment.";
RL Cell 28:303-313(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11779399; DOI=10.1098/rstb.2001.0979;
RA Schickli J.H., Flandorfer A., Nakaya T., Martinez-Sobrido L.,
RA Garcia-Sastre A., Palese P.;
RT "Plasmid-only rescue of influenza A virus vaccine candidates.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 356:1965-1973(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND REVERSE GENETICS.
RX PubMed=15163504; DOI=10.1016/j.virusres.2004.02.028;
RA de Wit E., Spronken M.I.J., Bestebroer T.M., Rimmelzwaan G.F.,
RA Osterhaus A.D.M.E., Fouchier R.A.M.;
RT "Efficient generation and growth of influenza virus A/PR/8/34 from eight
RT cDNA fragments.";
RL Virus Res. 103:155-161(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Ghedin E., Spiro D., Miller N., Zaborsky J., Feldblyum T., Subbu V.,
RA Shumway M., Sparenborg J., Groveman L., Halpin R., Sitz J., Koo H.,
RA Salzberg S.L., Webster R.G., Hoffmann E., Krauss S., Naeve C., Bao Y.,
RA Bolotov P., Dernovoy D., Kiryutin B., Lipman D.J., Tatusova T.;
RT "The NIAID influenza genome sequencing project.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=A/Victoria/3/75;
RX PubMed=8113737; DOI=10.1099/0022-1317-75-1-29;
RA Nieto A., de la Luna S., Barcena J., Portela A., Ortin J.;
RT "Complex structure of the nuclear translocation signal of influenza virus
RT polymerase PA subunit.";
RL J. Gen. Virol. 75:29-36(1994).
RN [6]
RP PHOSPHORYLATION.
RC STRAIN=A/Victoria/3/75;
RX PubMed=9519825; DOI=10.1099/0022-1317-79-3-471;
RA Sanz-Ezquerro J.J., Fernandez-Santaren J., Sierra T., Aragon T., Ortega J.,
RA Ortin J., Smith G.L., Nieto A.;
RT "The PA influenza virus polymerase subunit is a phosphorylated protein.";
RL J. Gen. Virol. 79:471-478(1998).
RN [7]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=A/WSN/33;
RX PubMed=15308710; DOI=10.1128/jvi.78.17.9144-9153.2004;
RA Fodor E., Smith M.;
RT "The PA subunit is required for efficient nuclear accumulation of the PB1
RT subunit of the influenza A virus RNA polymerase complex.";
RL J. Virol. 78:9144-9153(2004).
RN [8]
RP FUNCTION.
RC STRAIN=A/Victoria/3/1975;
RX PubMed=19194459; DOI=10.1038/nature07745;
RA Dias A., Bouvier D., Crepin T., McCarthy A.A., Hart D.J., Baudin F.,
RA Cusack S., Ruigrok R.W.;
RT "The cap-snatching endonuclease of influenza virus polymerase resides in
RT the PA subunit.";
RL Nature 458:914-918(2009).
RN [9]
RP INTERACTION WITH PB1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22001919; DOI=10.1016/j.bbrc.2011.09.142;
RA Suzuki T., Ainai A., Nagata N., Sata T., Sawa H., Hasegawa H.;
RT "A novel function of the N-terminal domain of PA in assembly of influenza A
RT virus RNA polymerase.";
RL Biochem. Biophys. Res. Commun. 414:719-726(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 239-716.
RX PubMed=18660801; DOI=10.1038/nature07225;
RA Obayashi E., Yoshida H., Kawai F., Shibayama N., Kawaguchi A., Nagata K.,
RA Tame J.R., Park S.Y.;
RT "The structural basis for an essential subunit interaction in influenza
RT virus RNA polymerase.";
RL Nature 454:1127-1131(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 1-50 AND 73-197 IN COMPLEX WITH
RP MANGANESE, AND COFACTOR.
RX PubMed=26252962; DOI=10.1016/j.bmc.2015.07.046;
RA Fudo S., Yamamoto N., Nukaga M., Odagiri T., Tashiro M., Neya S.,
RA Hoshino T.;
RT "Structural and computational study on inhibitory compounds for
RT endonuclease activity of influenza virus polymerase.";
RL Bioorg. Med. Chem. 23:5466-5475(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-50 AND 73-197 IN COMPLEX WITH
RP MANGANESE, AND COFACTOR.
RX PubMed=27088785; DOI=10.1021/acs.biochem.5b01087;
RA Fudo S., Yamamoto N., Nukaga M., Odagiri T., Tashiro M., Hoshino T.;
RT "Two distinctive binding modes of endonuclease inhibitors to the N-terminal
RT region of Influenza virus polymerase acidic subunit.";
RL Biochemistry 55:2646-2660(2016).
CC -!- FUNCTION: Plays an essential role in viral RNA transcription and
CC replication by forming the heterotrimeric polymerase complex together
CC with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using
CC a unique mechanism called cap-snatching. It consists in the hijacking
CC and cleavage of host capped pre-mRNAs. These short capped RNAs are then
CC used as primers for viral mRNAs. The PB2 subunit is responsible for the
CC binding of the 5' cap of cellular pre-mRNAs which are subsequently
CC cleaved after 10-13 nucleotides by the PA subunit that carries the
CC endonuclease activity. {ECO:0000255|HAMAP-Rule:MF_04063,
CC ECO:0000269|PubMed:15308710, ECO:0000269|PubMed:19194459,
CC ECO:0000269|PubMed:22001919}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04063,
CC ECO:0000269|PubMed:26252962, ECO:0000269|PubMed:27088785};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_04063, ECO:0000269|PubMed:26252962,
CC ECO:0000269|PubMed:27088785};
CC -!- SUBUNIT: Influenza RNA polymerase is composed of three subunits: PB1,
CC PB2 and PA. Interacts (via C-terminus) with PB1 (via N-terminus).
CC {ECO:0000255|HAMAP-Rule:MF_04063, ECO:0000269|PubMed:22001919}.
CC -!- INTERACTION:
CC P03433; P03485: M; NbExp=2; IntAct=EBI-2547616, EBI-2547543;
CC P03433; P03466: NP; NbExp=3; IntAct=EBI-2547616, EBI-2547640;
CC P03433; P03431: PB1; NbExp=6; IntAct=EBI-2547616, EBI-2547514;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04063}.
CC Host nucleus {ECO:0000255|HAMAP-Rule:MF_04063}. Note=PB1 and PA are
CC transported in the host nucleus as a complex. {ECO:0000255|HAMAP-
CC Rule:MF_04063, ECO:0000269|PubMed:15308710,
CC ECO:0000269|PubMed:22001919, ECO:0000269|PubMed:8113737}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=PA;
CC IsoId=P03433-1; Sequence=Displayed;
CC Name=PA-X;
CC IsoId=P0CK64-1; Sequence=External;
CC -!- PTM: Phosphorylated on serines and threonines by host kinases,
CC including human casein kinase II. {ECO:0000255|HAMAP-Rule:MF_04063,
CC ECO:0000269|PubMed:9519825}.
CC -!- SIMILARITY: Belongs to the influenza viruses PA family.
CC {ECO:0000255|HAMAP-Rule:MF_04063}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; V01106; CAA24295.1; -; Genomic_RNA.
DR EMBL; AF389117; AAM75157.1; -; Genomic_RNA.
DR EMBL; EF467820; ABO21708.1; -; Genomic_RNA.
DR EMBL; CY009449; ABD77682.1; -; Genomic_RNA.
DR RefSeq; NP_040986.1; NC_002022.1.
DR PDB; 2ZNL; X-ray; 2.30 A; A=239-716.
DR PDB; 4YYL; X-ray; 1.91 A; A=1-50, A=73-197.
DR PDB; 4ZHZ; X-ray; 2.50 A; A=1-50, A=73-197.
DR PDB; 4ZI0; X-ray; 1.80 A; A=1-50, A=73-197.
DR PDB; 4ZQQ; X-ray; 1.80 A; A=1-50, A=73-197.
DR PDB; 5FDD; X-ray; 2.51 A; A=1-50, A=73-197.
DR PDB; 5FDG; X-ray; 2.10 A; A=1-50, A=73-197.
DR PDB; 5I13; X-ray; 2.15 A; A=1-50, A=73-197.
DR PDB; 5JHT; X-ray; 1.75 A; A=1-50, A=73-197.
DR PDB; 5JHV; X-ray; 2.75 A; A/B=1-50, A/B=73-197.
DR PDBsum; 2ZNL; -.
DR PDBsum; 4YYL; -.
DR PDBsum; 4ZHZ; -.
DR PDBsum; 4ZI0; -.
DR PDBsum; 4ZQQ; -.
DR PDBsum; 5FDD; -.
DR PDBsum; 5FDG; -.
DR PDBsum; 5I13; -.
DR PDBsum; 5JHT; -.
DR PDBsum; 5JHV; -.
DR SMR; P03433; -.
DR DIP; DIP-43996N; -.
DR IntAct; P03433; 57.
DR MINT; P03433; -.
DR BindingDB; P03433; -.
DR ChEMBL; CHEMBL1169598; -.
DR DrugBank; DB13997; Baloxavir marboxil.
DR DrugCentral; P03433; -.
DR MEROPS; S62.001; -.
DR GeneID; 956535; -.
DR KEGG; vg:956535; -.
DR BRENDA; 2.7.7.48; 7479.
DR Reactome; R-HSA-168255; Influenza Infection.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis.
DR Reactome; R-HSA-168288; Fusion of the Influenza Virion to the Host Cell Endosome.
DR Reactome; R-HSA-168298; Release.
DR Reactome; R-HSA-168302; Budding.
DR Reactome; R-HSA-168303; Packaging of Eight RNA Segments.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-168330; Viral RNP Complexes in the Host Cell Nucleus.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-168336; Uncoating of the Influenza Virion.
DR Reactome; R-HSA-192814; vRNA Synthesis.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-192869; cRNA Synthesis.
DR Reactome; R-HSA-192905; vRNP Assembly.
DR EvolutionaryTrace; P03433; -.
DR Proteomes; UP000009255; Genome.
DR Proteomes; UP000116373; Genome.
DR Proteomes; UP000170967; Genome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0075526; P:cap snatching; IEA:UniProtKB-UniRule.
DR GO; GO:0039523; P:suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 3.40.91.90; -; 1.
DR HAMAP; MF_04063; INFV_PA; 1.
DR InterPro; IPR037534; INFV_PA.
DR InterPro; IPR001009; PA/PA-X.
DR InterPro; IPR038372; PA/PA-X_sf.
DR Pfam; PF00603; Flu_PA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cap snatching; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host transcription shutoff by virus; Host cytoplasm;
KW Host gene expression shutoff by virus; Host nucleus;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host RNA polymerase II by virus; Manganese; Metal-binding;
KW Nuclease; Phosphoprotein; Reference proteome; Ribosomal frameshifting.
FT CHAIN 1..716
FT /note="Polymerase acidic protein"
FT /id="PRO_0000078796"
FT MOTIF 124..139
FT /note="Nuclear localization signal 1 (NLS1)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063,
FT ECO:0000269|PubMed:8113737"
FT MOTIF 184..247
FT /note="Nuclear localization signal 2 (NLS2)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063,
FT ECO:0000269|PubMed:8113737"
FT BINDING 41
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063,
FT ECO:0000269|PubMed:26252962, ECO:0000269|PubMed:27088785,
FT ECO:0007744|PDB:4YYL, ECO:0007744|PDB:4ZI0,
FT ECO:0007744|PDB:4ZQQ"
FT BINDING 80
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063,
FT ECO:0000269|PubMed:27088785, ECO:0007744|PDB:4YYL,
FT ECO:0007744|PDB:4ZI0, ECO:0007744|PDB:4ZQQ"
FT BINDING 108
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063,
FT ECO:0000269|PubMed:27088785, ECO:0007744|PDB:4YYL,
FT ECO:0007744|PDB:4ZI0, ECO:0007744|PDB:4ZQQ"
FT BINDING 108
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063,
FT ECO:0000269|PubMed:27088785, ECO:0007744|PDB:4YYL,
FT ECO:0007744|PDB:4ZI0, ECO:0007744|PDB:4ZQQ"
FT BINDING 119
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063,
FT ECO:0000269|PubMed:27088785, ECO:0007744|PDB:4YYL,
FT ECO:0007744|PDB:4ZI0, ECO:0007744|PDB:4ZQQ"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04063,
FT ECO:0000269|PubMed:26252962, ECO:0000269|PubMed:27088785,
FT ECO:0007744|PDB:4YYL, ECO:0007744|PDB:4ZI0,
FT ECO:0007744|PDB:4ZQQ"
FT CONFLICT 550
FT /note="I -> L (in Ref. 1; CAA24295)"
FT HELIX 1..8
FT /evidence="ECO:0007829|PDB:5JHT"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:5JHT"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:5JHT"
FT HELIX 32..50
FT /evidence="ECO:0007829|PDB:5JHT"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:5JHT"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:5JHT"
FT HELIX 84..98
FT /evidence="ECO:0007829|PDB:5JHT"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:5JHT"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:5JHT"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:5JHT"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:5JHT"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:5JHT"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:5JHT"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:5JHT"
FT HELIX 165..184
FT /evidence="ECO:0007829|PDB:5JHT"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:5JHT"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:2ZNL"
FT TURN 298..301
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 331..345
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 406..414
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 437..450
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 454..474
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 481..490
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 496..506
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 517..526
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 530..532
FT /evidence="ECO:0007829|PDB:2ZNL"
FT TURN 534..539
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 541..548
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 559..571
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 572..579
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 583..602
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 608..613
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 619..624
FT /evidence="ECO:0007829|PDB:2ZNL"
FT STRAND 627..631
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 633..649
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 653..674
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 686..691
FT /evidence="ECO:0007829|PDB:2ZNL"
FT HELIX 698..714
FT /evidence="ECO:0007829|PDB:2ZNL"
SQ SEQUENCE 716 AA; 82588 MW; 8829F53525814394 CRC64;
MEDFVRQCFN PMIVELAEKT MKEYGEDLKI ETNKFAAICT HLEVCFMYSD FHFINEQGES
IIVELGDPNA LLKHRFEIIE GRDRTMAWTV VNSICNTTGA EKPKFLPDLY DYKENRFIEI
GVTRREVHIY YLEKANKIKS EKTHIHIFSF TGEEMATKAD YTLDEESRAR IKTRLFTIRQ
EMASRGLWDS FRQSERGEET IEERFEITGT MRKLADQSLP PNFSSLENFR AYVDGFEPNG
YIEGKLSQMS KEVNARIEPF LKTTPRPLRL PNGPPCSQRS KFLLMDALKL SIEDPSHEGE
GIPLYDAIKC MRTFFGWKEP NVVKPHEKGI NPNYLLSWKQ VLAELQDIEN EEKIPKTKNM
KKTSQLKWAL GENMAPEKVD FDDCKDVGDL KQYDSDEPEL RSLASWIQNE FNKACELTDS
SWIELDEIGE DVAPIEHIAS MRRNYFTSEV SHCRATEYIM KGVYINTALL NASCAAMDDF
QLIPMISKCR TKEGRRKTNL YGFIIKGRSH LRNDTDVVNF VSMEFSLTDP RLEPHKWEKY
CVLEIGDMLI RSAIGQVSRP MFLYVRTNGT SKIKMKWGME MRRCLLQSLQ QIESMIEAES
SVKEKDMTKE FFENKSETWP IGESPKGVEE SSIGKVCRTL LAKSVFNSLY ASPQLEGFSA
ESRKLLLIVQ ALRDNLEPGT FDLGGLYEAI EECLINDPWV LLNASWFNSF LTHALS
