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 02-SEP-2026, entry version 148. DE RecName: Full=Polymerase acidic protein {ECO:0000255|HAMAP-Rule:MF_04063}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04063, ECO:0000269|PubMed:19194459}; 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; OC Alphainfluenzavirus influenzae; Influenza A virus. 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 FUNCTION, COFACTOR, AND CATALYTIC ACTIVITY. 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 [8] 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 [9] RP INTERACTION WITH PB1. RX PubMed=28169297; DOI=10.1038/ncomms13876; RA Wang L., Fu B., Li W., Patil G., Liu L., Dorf M.E., Li S.; RT "Comparative influenza protein interactomes identify the role of RT plakophilin 2 in virus restriction."; RL Nat. Commun. 8:13876-13876(2017). 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:19194459, ECO:0000269|PubMed:22001919}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_04063, ECO:0000269|PubMed:19194459, 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 ECO:0000269|PubMed:28169297}. 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:22001919, CC 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 PDB; 7XGC; X-ray; 1.60 A; A=1-50, A=73-197. DR MDposit; P03433; -. 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 OrthoDB; 495at10239; -. 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 Reactome; R-HSA-9943962; CHD6, CHD7, CHD8, CHD9 subfamily. DR EvolutionaryTrace; P03433; -. DR Proteomes; UP000009255; 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:0016787; F:hydrolase 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:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR GO; GO:0039657; P:symbiont-mediated suppression of host gene expression; IEA:UniProtKB-KW. DR GO; GO:0039523; P:symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity; IEA:UniProtKB-UniRule. DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro. DR GO; GO:0075523; P:viral translational frameshifting; IEA:UniProtKB-KW. DR DisProt; DP03571; -. DR FunFam; 3.40.91.90:FF:000001; Polymerase acidic protein; 1. DR Gene3D; 3.40.91.90; Influenza RNA-dependent RNA polymerase subunit PA, endonuclease domain; 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. 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 PDBsum; 7XGC; -. 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 /ligand_note="catalytic" 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 /ligand_note="catalytic" 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 /ligand_note="catalytic" 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 /ligand_note="catalytic" 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 /ligand_note="catalytic" 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 /ligand_note="catalytic" 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:7XGC" FT HELIX 11..23 FT /evidence="ECO:0007829|PDB:7XGC" FT TURN 28..30 FT /evidence="ECO:0007829|PDB:7XGC" FT HELIX 32..50 FT /evidence="ECO:0007829|PDB:7XGC" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:7XGC" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:7XGC" FT HELIX 84..98 FT /evidence="ECO:0007829|PDB:7XGC" FT HELIX 100..103 FT /evidence="ECO:0007829|PDB:7XGC" FT STRAND 108..111 FT /evidence="ECO:0007829|PDB:7XGC" FT TURN 112..115 FT /evidence="ECO:0007829|PDB:7XGC" FT STRAND 116..125 FT /evidence="ECO:0007829|PDB:7XGC" FT HELIX 127..138 FT /evidence="ECO:0007829|PDB:7XGC" FT STRAND 144..152 FT /evidence="ECO:0007829|PDB:7XGC" FT STRAND 154..156 FT /evidence="ECO:0007829|PDB:7XGC" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:7XGC" FT HELIX 165..184 FT /evidence="ECO:0007829|PDB:7XGC" FT HELIX 188..193 FT /evidence="ECO:0007829|PDB:7XGC" FT HELIX 268..272 FT /evidence="ECO:0007829|PDB:2ZNL" 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 TURN 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 //