DCL4_ARATH
ID DCL4_ARATH Reviewed; 1702 AA.
AC P84634; Q3SA53;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Dicer-like protein 4;
DE EC=3.1.26.-;
GN Name=DCL4; OrderedLocusNames=At5g20320; ORFNames=F5O24.210;
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 [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia; TISSUE=Shoot;
RX PubMed=16129836; DOI=10.1073/pnas.0506426102;
RA Xie Z., Allen E., Wilken A., Carrington J.C.;
RT "DICER-LIKE 4 functions in trans-acting small interfering RNA biogenesis
RT and vegetative phase change in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12984-12989(2005).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000269|PubMed:11130714};
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DRB4.
RX PubMed=15821876; DOI=10.1007/s11103-004-6853-5;
RA Hiraguri A., Itoh R., Kondo N., Nomura Y., Aizawa D., Murai Y., Koiwa H.,
RA Seki M., Shinozaki K., Fukuhara T.;
RT "Specific interactions between Dicer-like proteins and HYL1/DRB-family
RT dsRNA-binding proteins in Arabidopsis thaliana.";
RL Plant Mol. Biol. 57:173-188(2005).
RN [5]
RP FUNCTION.
RX PubMed=16040244; DOI=10.1016/j.cub.2005.07.024;
RA Gasciolli V., Mallory A.C., Bartel D.P., Vaucheret H.;
RT "Partially redundant functions of Arabidopsis DICER-like enzymes and a role
RT for DCL4 in producing trans-acting siRNAs.";
RL Curr. Biol. 15:1494-1500(2005).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=16273107; DOI=10.1038/ng1675;
RA Dunoyer P., Himber C., Voinnet O.;
RT "DICER-LIKE 4 is required for RNA interference and produces the 21-
RT nucleotide small interfering RNA component of the plant cell-to-cell
RT silencing signal.";
RL Nat. Genet. 37:1356-1360(2005).
RN [8]
RP FUNCTION.
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 [9]
RP FUNCTION.
RX PubMed=16810317; DOI=10.1038/sj.emboj.7601217;
RA Bouche N., Lauressergues D., Gasciolli V., Vaucheret H.;
RT "An antagonistic function for Arabidopsis DCL2 in development and a new
RT function for DCL4 in generating viral siRNAs.";
RL EMBO J. 25:3347-3356(2006).
RN [10]
RP FUNCTION.
RX PubMed=18003861; DOI=10.1101/gad.1595107;
RA Katiyar-Agarwal S., Gao S., Vivian-Smith A., Jin H.;
RT "A novel class of bacteria-induced small RNAs in Arabidopsis.";
RL Genes Dev. 21:3123-3134(2007).
RN [11]
RP FUNCTION.
RX PubMed=17586651; DOI=10.1105/tpc.106.047449;
RA Diaz-Pendon J.A., Li F., Li W.X., Ding S.W.;
RT "Suppression of antiviral silencing by cucumber mosaic virus 2b protein in
RT Arabidopsis is associated with drastically reduced accumulation of three
RT classes of viral small interfering RNAs.";
RL Plant Cell 19:2053-2063(2007).
RN [12]
RP FUNCTION.
RX PubMed=17592042; DOI=10.1261/rna.541307;
RA Moissiard G., Parizotto E.A., Himber C., Voinnet O.;
RT "Transitivity in Arabidopsis can be primed, requires the redundant action
RT of the antiviral Dicer-like 4 and Dicer-like 2, and is compromised by
RT viral-encoded suppressor proteins.";
RL RNA 13:1268-1278(2007).
RN [13]
RP FUNCTION.
RX PubMed=18353962; DOI=10.1128/jvi.00272-08;
RA Donaire L., Barajas D., Martinez-Garcia B., Martinez-Priego L., Pagan I.,
RA Llave C.;
RT "Structural and genetic requirements for the biogenesis of tobacco rattle
RT virus-derived small interfering RNAs.";
RL J. Virol. 82:5167-5177(2008).
RN [14]
RP FUNCTION.
RX PubMed=18799732; DOI=10.1073/pnas.0805760105;
RA Qu F., Ye X., Morris T.J.;
RT "Arabidopsis DRB4, AGO1, AGO7, and RDR6 participate in a DCL4-initiated
RT antiviral RNA silencing pathway negatively regulated by DCL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:14732-14737(2008).
RN [15]
RP GENE FAMILY.
RX PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA Xu R., Zhang S., Huang J., Zheng C.;
RT "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT sativa.";
RL PLoS ONE 8:E78982-E78982(2013).
RN [16]
RP STRUCTURE BY NMR OF 651-752.
RX PubMed=20106953; DOI=10.1261/rna.1965310;
RA Qin H., Chen F., Huan X., Machida S., Song J., Yuan Y.A.;
RT "Structure of the Arabidopsis thaliana DCL4 DUF283 domain reveals a
RT noncanonical double-stranded RNA-binding fold for protein-protein
RT interaction.";
RL RNA 16:474-481(2010).
CC -!- FUNCTION: Ribonuclease (RNase) III involved in RNA-mediated post-
CC transcriptional gene silencing (PTGS). Functions in the biogenesis of
CC trans-acting small interfering RNAs (ta-siRNAs, derived from the TAS1,
CC TAS2 or TAS3 endogenous transcripts) by cleaving small dsRNAs into 21-
CC 24 nucleotide ta-siRNAs. Functions with the dsRNA-binding protein DRB4
CC in ta-siRNAs processing. Acts in the RDR6/SGS3/DCL4/AGO7 ta-siRNA
CC pathway involved in leaf developmental timing. Plays a role in
CC transitive silencing of transgenes by processing secondary siRNAs. This
CC pathway, which requires DCL2 and RDR6, amplifies silencing by using the
CC target RNA as substrate to generate secondary siRNAs, providing an
CC efficient mechanism for long-distance silencing. Required for the
CC production of the 30-40 nucleotide bacterial-induced long siRNAs
CC (lsiRNA). May participate with DCL3 in the production of 24 nucleotide
CC repeat-associated siRNAs (ra-siRNAs) which derive from heterochromatin
CC and DNA repeats such as transposons. Plays an important role in
CC antiviral RNA silencing. Involved in the production of viral siRNAs
CC derived from the cucumber mosaic virus (CMV), turnip crinkle virus
CC (TCV) and tobacco rattle virus (TRV). Targeted by the viral silencing
CC suppressor (VSR) protein 2b of the cucumber mosaic virus (CMV) that
CC inactivates DCL4 function in RNA silencing. Does not seem to be
CC involved in microRNAs (miRNAs) processing.
CC {ECO:0000269|PubMed:16040244, ECO:0000269|PubMed:16129836,
CC ECO:0000269|PubMed:16131612, ECO:0000269|PubMed:16273107,
CC ECO:0000269|PubMed:16682354, ECO:0000269|PubMed:16810317,
CC ECO:0000269|PubMed:17586651, ECO:0000269|PubMed:17592042,
CC ECO:0000269|PubMed:18003861, ECO:0000269|PubMed:18353962,
CC ECO:0000269|PubMed:18799732}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with DRB4. {ECO:0000269|PubMed:15821876}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15821876}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P84634-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00657}.
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DR EMBL; DQ118423; AAZ80387.1; -; mRNA.
DR EMBL; AF296825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92830.1; -; Genomic_DNA.
DR RefSeq; NP_197532.3; NM_122039.5. [P84634-1]
DR PDB; 2KOU; NMR; -; A=651-752.
DR PDBsum; 2KOU; -.
DR AlphaFoldDB; P84634; -.
DR BMRB; P84634; -.
DR SMR; P84634; -.
DR BioGRID; 17430; 4.
DR IntAct; P84634; 2.
DR MINT; P84634; -.
DR STRING; 3702.AT5G20320.1; -.
DR iPTMnet; P84634; -.
DR PaxDb; P84634; -.
DR ProteomicsDB; 224171; -. [P84634-1]
DR EnsemblPlants; AT5G20320.1; AT5G20320.1; AT5G20320. [P84634-1]
DR GeneID; 832154; -.
DR Gramene; AT5G20320.1; AT5G20320.1; AT5G20320. [P84634-1]
DR KEGG; ath:AT5G20320; -.
DR Araport; AT5G20320; -.
DR TAIR; locus:2149259; AT5G20320.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_4_4_1; -.
DR InParanoid; P84634; -.
DR OrthoDB; 1337630at2759; -.
DR PhylomeDB; P84634; -.
DR EvolutionaryTrace; P84634; -.
DR PRO; PR:P84634; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P84634; baseline and differential.
DR Genevisible; P84634; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IMP:TAIR.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IMP:TAIR.
DR GO; GO:0010599; P:lsiRNA processing; IMP:TAIR.
DR GO; GO:0010216; P:maintenance of DNA methylation; IMP:TAIR.
DR GO; GO:0010492; P:maintenance of shoot apical meristem identity; IEA:EnsemblPlants.
DR GO; GO:0009944; P:polarity specification of adaxial/abaxial axis; IEA:EnsemblPlants.
DR GO; GO:0048608; P:reproductive structure development; IEA:EnsemblPlants.
DR GO; GO:0009616; P:RNAi-mediated antiviral immune response; IGI:TAIR.
DR GO; GO:0051214; P:RNAi-mediated antiviral immunity against RNA virus; IGI:TAIR.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
DR GO; GO:0010267; P:ta-siRNA processing; IMP:TAIR.
DR GO; GO:0010050; P:vegetative phase change; IMP:TAIR.
DR CDD; cd00593; RIBOc; 2.
DR DisProt; DP01543; -.
DR Gene3D; 1.10.1520.10; -; 2.
DR Gene3D; 3.30.160.380; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF00636; Ribonuclease_3; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00535; RIBOc; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF69065; SSF69065; 2.
DR PROSITE; PS51327; DICER_DSRBF; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Endonuclease; Helicase;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleotide-binding; Nucleus;
KW Plant defense; Reference proteome; Repeat; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..1702
FT /note="Dicer-like protein 4"
FT /id="PRO_0000180475"
FT DOMAIN 131..307
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 475..629
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 656..748
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 927..1054
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 1083..1251
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1292..1436
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1462..1528
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 1621..1697
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 251..254
FT /note="DECH box"
FT COMPBIAS 15..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1422
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1425
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 1418
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT HELIX 655..664
FT /evidence="ECO:0007829|PDB:2KOU"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:2KOU"
FT STRAND 678..683
FT /evidence="ECO:0007829|PDB:2KOU"
FT HELIX 686..688
FT /evidence="ECO:0007829|PDB:2KOU"
FT STRAND 690..695
FT /evidence="ECO:0007829|PDB:2KOU"
FT STRAND 705..708
FT /evidence="ECO:0007829|PDB:2KOU"
FT HELIX 713..731
FT /evidence="ECO:0007829|PDB:2KOU"
FT TURN 735..737
FT /evidence="ECO:0007829|PDB:2KOU"
FT HELIX 741..744
FT /evidence="ECO:0007829|PDB:2KOU"
FT TURN 748..750
FT /evidence="ECO:0007829|PDB:2KOU"
SQ SEQUENCE 1702 AA; 191279 MW; 7AA7647A6BA7F24D CRC64;
MRDEVDLSLT IPSKLLGKRD REQKNCEEEK NKNKKAKKQQ KDPILLHTSA ATHKFLPPPL
TMPYSEIGDD LRSLDFDHAD VSSDLHLTSS SSVSSFSSSS SSLFSAAGTD DPSPKMEKDP
RKIARRYQVE LCKKATEENV IVYLGTGCGK THIAVMLIYE LGHLVLSPKK SVCIFLAPTV
ALVEQQAKVI ADSVNFKVAI HCGGKRIVKS HSEWEREIAA NEVLVMTPQI LLHNLQHCFI
KMECISLLIF DECHHAQQQS NHPYAEIMKV FYKSESLQRP RIFGMTASPV VGKGSFQSEN
LSKSINSLEN LLNAKVYSVE SNVQLDGFVS SPLVKVYYYR SALSDASQST IRYENMLEDI
KQRCLASLKL LIDTHQTQTL LSMKRLLKRS HDNLIYTLLN LGLWGAIQAA KIQLNSDHNV
QDEPVGKNPK SKICDTYLSM AAEALSSGVA KDENASDLLS LAALKEPLFS RKLVQLIKIL
SVFRLEPHMK CIIFVNRIVT ARTLSCILNN LELLRSWKSD FLVGLSSGLK SMSRRSMETI
LKRFQSKELN LLVATKVGEE GLDIQTCCLV IRYDLPETVT SFIQSRGRAR MPQSEYAFLV
DSGNEKEMDL IENFKVNEDR MNLEITYRSS EETCPRLDEE LYKVHETGAC ISGGSSISLL
YKYCSRLPHD EFFQPKPEFQ FKPVDEFGGT ICRITLPANA PISEIESSLL PSTEAAKKDA
CLKAVHELHN LGVLNDFLLP DSKDEIEDEL SDDEFDFDNI KGEGCSRGDL YEMRVPVLFK
QKWDPSTSCV NLHSYYIMFV PHPADRIYKK FGFFMKSPLP VEAETMDIDL HLAHQRSVSV
KIFPSGVTEF DNDEIRLAEL FQEIALKVLF ERGELIPDFV PLELQDSSRT SKSTFYLLLP
LCLHDGESVI SVDWVTIRNC LSSPIFKTPS VLVEDIFPPS GSHLKLANGC WNIDDVKNSL
VFTTYSKQFY FVADICHGRN GFSPVKESST KSHVESIYKL YGVELKHPAQ PLLRVKPLCH
VRNLLHNRMQ TNLEPQELDE YFIEIPPELS HLKIKGLSKD IGSSLSLLPS IMHRMENLLV
AIELKHVLSA SIPEIAEVSG HRVLEALTTE KCHERLSLER LEVLGDAFLK FAVSRHLFLH
HDSLDEGELT RRRSNVVNNS NLCRLAIKKN LQVYIRDQAL DPTQFFAFGH PCRVTCDEVA
SKEVHSLNRD LGILESNTGE IRCSKGHHWL YKKTIADVVE ALVGAFLVDS GFKGAVKFLK
WIGVNVDFES LQVQDACIAS RRYLPLTTRN NLETLENQLD YKFLHKGLLV QAFIHPSYNR
HGGGCYQRLE FLGDAVLDYL MTSYFFTVFP KLKPGQLTDL RSLSVNNEAL ANVAVSFSLK
RFLFCESIYL HEVIEDYTNF LASSPLASGQ SEGPRCPKVL GDLVESCLGA LFLDCGFNLN
HVWTMMLSFL DPVKNLSNLQ ISPIKELIEL CQSYKWDREI SATKKDGAFT VELKVTKNGC
CLTVSATGRN KREGTKKAAQ LMITNLKAHE NITTSHPLED VLKNGIRNEA KLIGYNEDPI
DVVDLVGLDV ENLNILETFG GNSERSSSYV IRRGLPQAPS KTEDRLPQKA IIKAGGPSSK
TAKSLLHETC VANCWKPPHF ECCEEEGPGH LKSFVYKVIL EVEDAPNMTL ECYGEARATK
KGAAEHAAQA AIWCLKHSGF LC
