RDR6_ARATH
ID RDR6_ARATH Reviewed; 1196 AA.
AC Q9SG02; A0A1I9LSW2; Q9LKP0;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=RNA-dependent RNA polymerase 6;
DE Short=AtRDRP6;
DE EC=2.7.7.48;
DE AltName: Full=Protein SILENCING DEFECTIVE 1;
DE AltName: Full=Protein SUPPRESSOR OF GENE SILENCING 2;
DE AltName: Full=RNA-directed RNA polymerase 6;
GN Name=RDR6; Synonyms=RDRP6, SDE1, SGS2; OrderedLocusNames=At3g49500;
GN ORFNames=T1G12.20, T9C5.95;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLU-429; GLU-453; GLY-825; ASP-826; SER-860 AND GLY-866.
RC STRAIN=cv. Columbia;
RX PubMed=10850495; DOI=10.1016/s0092-8674(00)80863-6;
RA Mourrain P., Beclin C., Elmayan T., Feuerbach F., Godon C., Morel J.-B.,
RA Jouette D., Lacombe A.-M., Nikic S., Picault N., Remoue K., Sanial M.,
RA Vo T.-A., Vaucheret H.;
RT "Arabidopsis SGS2 and SGS3 genes are required for posttranscriptional gene
RT silencing and natural virus resistance.";
RL Cell 101:533-542(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10850496; DOI=10.1016/s0092-8674(00)80864-8;
RA Dalmay T., Hamilton A., Rudd S., Angell S., Baulcombe D.C.;
RT "An RNA-dependent RNA polymerase gene in Arabidopsis is required for
RT posttranscriptional gene silencing mediated by a transgene but not by a
RT virus.";
RL Cell 101:543-553(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-866.
RX PubMed=15466488; DOI=10.1101/gad.1231804;
RA Peragine A., Yoshikawa M., Wu G., Albrecht H.L., Poethig R.S.;
RT "SGS3 and SGS2/SDE1/RDR6 are required for juvenile development and the
RT production of trans-acting siRNAs in Arabidopsis.";
RL Genes Dev. 18:2368-2379(2004).
RN [6]
RP FUNCTION.
RX PubMed=15165191; DOI=10.1111/j.1365-313x.2004.02103.x;
RA Muangsan N., Beclin C., Vaucheret H., Robertson D.;
RT "Geminivirus VIGS of endogenous genes requires SGS2/SDE1 and SGS3 and
RT defines a new branch in the genetic pathway for silencing in plants.";
RL Plant J. 38:1004-1014(2004).
RN [7]
RP FUNCTION.
RX PubMed=16377568; DOI=10.1016/j.cell.2005.11.035;
RA Borsani O., Zhu J., Verslues P.E., Sunkar R., Zhu J.-K.;
RT "Endogenous siRNAs derived from a pair of natural cis-antisense transcripts
RT regulate salt tolerance in Arabidopsis.";
RL Cell 123:1279-1291(2005).
RN [8]
RP FUNCTION.
RX PubMed=16131612; DOI=10.1101/gad.1352605;
RA Yoshikawa M., Peragine A., Park M.Y., Poethig R.S.;
RT "A pathway for the biogenesis of trans-acting siRNAs in Arabidopsis.";
RL Genes Dev. 19:2164-2175(2005).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16006579; DOI=10.1105/tpc.105.033449;
RA Li H., Xu L., Wang H., Yuan Z., Cao X., Yang Z., Zhang D., Xu Y., Huang H.;
RT "The Putative RNA-dependent RNA polymerase RDR6 acts synergistically with
RT ASYMMETRIC LEAVES1 and 2 to repress BREVIPEDICELLUS and MicroRNA165/166 in
RT Arabidopsis leaf development.";
RL Plant Cell 17:2157-2171(2005).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF PRO-611 AND ASP-826.
RX PubMed=16682354; DOI=10.1016/j.cub.2006.03.035;
RA Adenot X., Elmayan T., Lauressergues D., Boutet S., Bouche N.,
RA Gasciolli V., Vaucheret H.;
RT "DRB4-dependent TAS3 trans-acting siRNAs control leaf morphology through
RT AGO7.";
RL Curr. Biol. 16:927-932(2006).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17384170; DOI=10.1105/tpc.106.045724;
RA Luo Z., Chen Z.;
RT "Improperly terminated, unpolyadenylated mRNA of sense transgenes is
RT targeted by RDR6-mediated RNA silencing in Arabidopsis.";
RL Plant Cell 19:943-958(2007).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF ASP-867.
RX PubMed=18063577; DOI=10.1074/jbc.m708983200;
RA Curaba J., Chen X.;
RT "Biochemical activities of Arabidopsis RNA-dependent RNA polymerase 6.";
RL J. Biol. Chem. 283:3059-3066(2008).
RN [13]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SGS3.
RX PubMed=19332064; DOI=10.1016/j.febslet.2009.03.055;
RA Kumakura N., Takeda A., Fujioka Y., Motose H., Takano R., Watanabe Y.;
RT "SGS3 and RDR6 interact and colocalize in cytoplasmic SGS3/RDR6-bodies.";
RL FEBS Lett. 583:1261-1266(2009).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19308254; DOI=10.1371/journal.pone.0004971;
RA Qi X., Bao F.S., Xie Z.;
RT "Small RNA deep sequencing reveals role for Arabidopsis thaliana RNA-
RT dependent RNA polymerases in viral siRNA biogenesis.";
RL PLoS ONE 4:E4971-E4971(2009).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20208518; DOI=10.1038/nature08828;
RA Olmedo-Monfil V., Duran-Figueroa N., Arteaga-Vazquez M., Demesa-Arevalo E.,
RA Autran D., Grimanelli D., Slotkin R.K., Martienssen R.A.,
RA Vielle-Calzada J.P.;
RT "Control of female gamete formation by a small RNA pathway in
RT Arabidopsis.";
RL Nature 464:628-632(2010).
RN [16]
RP FUNCTION.
RX PubMed=20562854; DOI=10.1038/nsmb.1866;
RA Cuperus J.T., Carbonell A., Fahlgren N., Garcia-Ruiz H., Burke R.T.,
RA Takeda A., Sullivan C.M., Gilbert S.D., Montgomery T.A., Carrington J.C.;
RT "Unique functionality of 22-nt miRNAs in triggering RDR6-dependent siRNA
RT biogenesis from target transcripts in Arabidopsis.";
RL Nat. Struct. Mol. Biol. 17:997-1003(2010).
CC -!- FUNCTION: RNA-dependent RNA polymerase involved in post-transcriptional
CC gene silencing (PTGS). Possesses ssRNA and ssDNA-dependent polymerase
CC activity, but does not have priming activity. Possesses in vitro 3'
CC nucleotidyltransferase activity in the presence of UTP as single
CC nucleotide. Required for the production of 21 nucleotide trans-acting
CC small interfering RNAs (ta-siRNAs) derived from TAS1, TAS2 and TAS3
CC endogenous transcripts. Acts in the RDR6/SGS3/DCL4/AGO7 ta-siRNA
CC pathway involved in leaf developmental timing. Required for the
CC production of natural siRNAs (nat-siRNAs) derived from cis-natural
CC antisense transcripts. Required for the production of 24 nucleotide
CC nat-siRNAs derived from the stress-related P5CDH-SRO5 antisense gene
CC pair. Required for PTGS induced by transgene direct repeats. Plays an
CC essential role in transitive silencing of transgenes by processing
CC secondary siRNAs. This pathway, which requires DCL2 and DCL4, amplifies
CC silencing by using the target RNA as substrate to generate secondary
CC siRNAs, providing an efficient mechanism for long-distance silencing.
CC Involved in the biogenesis of secondary siRNAs which require 22
CC nucleotide miRNAs associated to AGO1. Participates synergistically with
CC AS1 and AS2 to proper plant development by repressing the miR165 and
CC miR166 microRNAs (independently of AGO10) that may lead to mRNA
CC degradation of genes in the class III HD-ZIP family. Required for the
CC production of some small RNAs derived from the crucifer-infecting
CC tobamovirus (TMV-cg). Required for sense virus-induced post-
CC transcriptional gene silencing (S-PTGS). {ECO:0000269|PubMed:10850495,
CC ECO:0000269|PubMed:10850496, ECO:0000269|PubMed:15165191,
CC ECO:0000269|PubMed:15466488, ECO:0000269|PubMed:16006579,
CC ECO:0000269|PubMed:16131612, ECO:0000269|PubMed:16377568,
CC ECO:0000269|PubMed:16682354, ECO:0000269|PubMed:17384170,
CC ECO:0000269|PubMed:18063577, ECO:0000269|PubMed:19308254,
CC ECO:0000269|PubMed:20208518, ECO:0000269|PubMed:20562854}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48;
CC -!- SUBUNIT: Interacts with SGS3. {ECO:0000269|PubMed:19332064}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule
CC {ECO:0000269|PubMed:19332064}. Nucleus {ECO:0000269|PubMed:17384170}.
CC Note=Colocalize with SGS3 in cytoplasmic granules distinct from P-
CC bodies. {ECO:0000269|PubMed:19332064}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16006579}.
CC -!- DISRUPTION PHENOTYPE: First leaves are elongated and curl downward.
CC Presence of stigmatic tissue in the middle of the septum at the apical
CC end of the carpels. Altered post-transcriptional gene silencing (PTGS).
CC Accumulation of ARF4 mRNA (targeted by TAS3-derived siRNAs). Upon
CC infection, over-accumulation of CMV RNA and enhanced susceptibility to
CC cucumber mosaic virus (CMV). Reduced levels of TMV-cg-derived small
CC RNAs. {ECO:0000269|PubMed:10850495, ECO:0000269|PubMed:10850496,
CC ECO:0000269|PubMed:15466488, ECO:0000269|PubMed:17384170,
CC ECO:0000269|PubMed:19308254, ECO:0000269|PubMed:20208518}.
CC -!- SIMILARITY: Belongs to the RdRP family. {ECO:0000305}.
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DR EMBL; AF239718; AAF73959.1; -; Genomic_DNA.
DR EMBL; AF268093; AAF74208.1; -; Genomic_DNA.
DR EMBL; AC012329; AAG52184.1; -; Genomic_DNA.
DR EMBL; AL132964; CAB71285.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78550.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65667.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65668.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65669.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65670.1; -; Genomic_DNA.
DR RefSeq; NP_001327617.1; NM_001339423.1.
DR RefSeq; NP_001327618.1; NM_001339424.1.
DR RefSeq; NP_001327619.1; NM_001339425.1.
DR RefSeq; NP_001327620.1; NM_001339426.1.
DR RefSeq; NP_190519.1; NM_114810.3.
DR AlphaFoldDB; Q9SG02; -.
DR SMR; Q9SG02; -.
DR BioGRID; 9430; 1.
DR IntAct; Q9SG02; 1.
DR MINT; Q9SG02; -.
DR STRING; 3702.AT3G49500.1; -.
DR PaxDb; Q9SG02; -.
DR PRIDE; Q9SG02; -.
DR ProteomicsDB; 236991; -.
DR EnsemblPlants; AT3G49500.1; AT3G49500.1; AT3G49500.
DR EnsemblPlants; AT3G49500.2; AT3G49500.2; AT3G49500.
DR EnsemblPlants; AT3G49500.3; AT3G49500.3; AT3G49500.
DR EnsemblPlants; AT3G49500.4; AT3G49500.4; AT3G49500.
DR EnsemblPlants; AT3G49500.5; AT3G49500.5; AT3G49500.
DR GeneID; 824112; -.
DR Gramene; AT3G49500.1; AT3G49500.1; AT3G49500.
DR Gramene; AT3G49500.2; AT3G49500.2; AT3G49500.
DR Gramene; AT3G49500.3; AT3G49500.3; AT3G49500.
DR Gramene; AT3G49500.4; AT3G49500.4; AT3G49500.
DR Gramene; AT3G49500.5; AT3G49500.5; AT3G49500.
DR KEGG; ath:AT3G49500; -.
DR Araport; AT3G49500; -.
DR TAIR; locus:2114633; AT3G49500.
DR eggNOG; KOG0988; Eukaryota.
DR HOGENOM; CLU_001366_3_1_1; -.
DR InParanoid; Q9SG02; -.
DR OMA; HPKWVKK; -.
DR OrthoDB; 63910at2759; -.
DR PhylomeDB; Q9SG02; -.
DR BRENDA; 2.7.7.48; 399.
DR PRO; PR:Q9SG02; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SG02; baseline and differential.
DR Genevisible; Q9SG02; AT.
DR GO; GO:0031380; C:nuclear RNA-directed RNA polymerase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; ISS:TAIR.
DR GO; GO:0051607; P:defense response to virus; IMP:TAIR.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:TAIR.
DR GO; GO:0048467; P:gynoecium development; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IGI:TAIR.
DR GO; GO:0010492; P:maintenance of shoot apical meristem identity; IEA:EnsemblPlants.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:TAIR.
DR GO; GO:0048544; P:recognition of pollen; IMP:TAIR.
DR GO; GO:0009616; P:RNAi-mediated antiviral immune response; IMP:TAIR.
DR GO; GO:0030422; P:siRNA processing; IEP:TAIR.
DR GO; GO:0010267; P:ta-siRNA processing; IMP:TAIR.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR007855; RNA-dep_RNA_pol_euk-typ.
DR PANTHER; PTHR23079; PTHR23079; 1.
DR Pfam; PF05183; RdRP; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW DNA-directed DNA polymerase; Nucleotidyltransferase; Nucleus;
KW Plant defense; Reference proteome; RNA-binding;
KW RNA-directed RNA polymerase; RNA-mediated gene silencing; Transferase.
FT CHAIN 1..1196
FT /note="RNA-dependent RNA polymerase 6"
FT /id="PRO_0000404677"
FT MUTAGEN 429
FT /note="E->K: Alters post-transcriptional gene silencing."
FT /evidence="ECO:0000269|PubMed:10850495"
FT MUTAGEN 453
FT /note="E->K: Alters post-transcriptional gene silencing."
FT /evidence="ECO:0000269|PubMed:10850495"
FT MUTAGEN 611
FT /note="P->L: Alters post-transcriptional gene silencing."
FT /evidence="ECO:0000269|PubMed:16682354"
FT MUTAGEN 825
FT /note="G->E: Alters post-transcriptional gene silencing."
FT /evidence="ECO:0000269|PubMed:10850495"
FT MUTAGEN 826
FT /note="D->N: Alters post-transcriptional gene silencing."
FT /evidence="ECO:0000269|PubMed:10850495,
FT ECO:0000269|PubMed:16682354"
FT MUTAGEN 860
FT /note="S->F: Alters post-transcriptional gene silencing."
FT /evidence="ECO:0000269|PubMed:10850495"
FT MUTAGEN 866
FT /note="G->E: In rdr6-13; alters post-transcriptional gene
FT silencing."
FT /evidence="ECO:0000269|PubMed:10850495,
FT ECO:0000269|PubMed:15466488"
FT MUTAGEN 867
FT /note="D->A: Loss of polymerase activity."
FT /evidence="ECO:0000269|PubMed:18063577"
FT CONFLICT 597
FT /note="D -> G (in Ref. 2; AAF74208)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="F -> I (in Ref. 2; AAF74208)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="D -> V (in Ref. 2; AAF74208)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="N -> D (in Ref. 2; AAF74208)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="D -> V (in Ref. 2; AAF74208)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="T -> K (in Ref. 2; AAF74208)"
FT /evidence="ECO:0000305"
FT CONFLICT 998
FT /note="R -> P (in Ref. 2; AAF74208)"
FT /evidence="ECO:0000305"
FT CONFLICT 1044
FT /note="L -> S (in Ref. 2; AAF74208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1196 AA; 136929 MW; 812DEB9CEDC82C8F CRC64;
MGSEGNMKKS VVTQVSIGGF GESTTAKQLT DYLEDEVGIV WRCRLKTSWT PPGSYPNFEI
ADTSNIPSID EYKKVEPHAF VHFAVFESAG RAMDAAGQCN LILDGQPLKV SLGPKNPYSL
NQRRRTTVPY KLAGITLEIG TLVSRDDFFV SWRAEGVDFL VDPFDNTCKF CFRKSTAFSF
KDAVMHAVIN CDYKLELLVR DIQTVRQYKT LHGFVLILQL ASSPRVWYRT ADDDIYDTVP
GDLLDDDDPW IRTTDFTQVG AIGRCHSYRV LISPRYENKL RTALDYFRMR RVQEERVRWP
PRIRNEPCFG EPVSDHFFCI HHKEGISFEI MFLVNSVLHR GVFNQFQLTE RFFDLLRNQP
KDVNIASLKH LCTYKRPVFD AYKRLKLVQE WIQKNPKLLG SHEQSEDISE IRRLVITPTR
AYCLPPEVEL SNRVLRRYKA VAERFLRVTF MDESMQTINS NVLSYFVAPI VKDLTSSSFS
QKTYVFKRVK SILTDGFKLC GRKYSFLAFS ANQLRDRSAW FFAEDGKTRV SDIKTWMGKF
KDKNVAKCAA RMGLCFSSTY ATVDVMPHEV DTEVPDIERN GYVFSDGIGT ITPDLADEVM
EKLKLDVHYS PCAYQIRYAG FKGVVARWPS KSDGIRLALR DSMKKFFSKH TILEICSWTR
FQPGFLNRQI ITLLSVLGVP DEIFWDMQES MLYKLNRILD DTDVAFEVLT ASCAEQGNTA
AIMLSAGFKP KTEPHLRGML SSVRIAQLWG LREKSRIFVT SGRWLMGCLD EAGILEHGQC
FIQVSKPSIE NCFSKHGSRF KETKTDLEVV KGYVAIAKNP CLHPGDVRIL EAVDVPQLHH
MYDCLIFPQK GDRPHTNEAS GSDLDGDLYF VAWDQKLIPP NRKSYPAMHY DAAEEKSLGR
AVNHQDIIDF FARNLANEQL GTICNAHVVH ADRSEYGAMD EECLLLAELA ATAVDFPKTG
KIVSMPFHLK PKLYPDFMGK EDYQTYKSNK ILGRLYRRVK EVYDEDAEAS SEESTDPSAI
PYDAVLEIPG FEDLIPEAWG HKCLYDGQLI GLLGQYKVQK EEEIVTGHIW SMPKYTSKKQ
GELKERLKHS YNSLKKEFRK VFEETIPDHE NLSEEEKNIL YEKKASAWYH VTYHPEWVKK
SLELQDPDES SHAAMLSFAW IAADYLARIK IRSREMGSID SAKPVDSLAK FLAQRL
