DCL1_ARATH
ID DCL1_ARATH Reviewed; 1909 AA.
AC Q9SP32; Q9FDY6; Q9MAN0;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Endoribonuclease Dicer homolog 1;
DE EC=3.1.26.-;
DE AltName: Full=Dicer-like protein 1;
DE Short=AtDCL1;
DE AltName: Full=Protein ABNORMAL SUSPENSOR 1;
DE AltName: Full=Protein CARPEL FACTORY;
DE AltName: Full=Protein SHORT INTEGUMENTS 1;
DE AltName: Full=Protein SUSPENSOR 1;
GN Name=DCL1; Synonyms=ASU1, CAF SIN1, SUS1; OrderedLocusNames=At1g01040;
GN ORFNames=T25K16.4;
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], TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 1837-ASN--LYS-1843 AND 1844-ASN--SER-1909.
RC STRAIN=cv. Wassilewskija;
RX PubMed=10556049; DOI=10.1242/dev.126.23.5231;
RA Jacobsen S.E., Running M.P., Meyerowitz E.M.;
RT "Disruption of an RNA helicase/RNase III gene in Arabidopsis causes
RT unregulated cell division in floral meristems.";
RL Development 126:5231-5243(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-415 AND ILE-431.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12376646; DOI=10.1104/pp.003491;
RA Golden T.A., Schauer S.E., Lang J.D., Pien S., Mushegian A.R.,
RA Grossniklaus U., Meinke D.W., Ray A.;
RT "SHORT INTEGUMENTS1/SUSPENSOR1/CARPEL FACTORY, a Dicer homolog, is a
RT maternal effect gene required for embryo development in Arabidopsis.";
RL Plant Physiol. 130:808-822(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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.
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, SUBCELLULAR LOCATION, AND INTERACTION WITH DRB1; DRB2 AND DRB5.
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 [7]
RP FUNCTION, AND INTERACTION WITH DRB1.
RX PubMed=16428603; DOI=10.1261/rna.2146906;
RA Kurihara Y., Takashi Y., Watanabe Y.;
RT "The interaction between DCL1 and HYL1 is important for efficient and
RT precise processing of pri-miRNA in plant microRNA biogenesis.";
RL RNA 12:206-212(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17442570; DOI=10.1016/j.cub.2007.04.005;
RA Fang Y., Spector D.L.;
RT "Identification of nuclear dicing bodies containing proteins for microRNA
RT biogenesis in living Arabidopsis plants.";
RL Curr. Biol. 17:818-823(2007).
RN [9]
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 [10]
RP FUNCTION.
RX PubMed=17579240; DOI=10.1534/genetics.107.070649;
RA Schmitz R.J., Hong L., Fitzpatrick K.E., Amasino R.M.;
RT "DICER-LIKE 1 and DICER-LIKE 3 redundantly act to promote flowering via
RT repression of FLOWERING LOCUS C in Arabidopsis thaliana.";
RL Genetics 176:1359-1362(2007).
RN [11]
RP FUNCTION.
RX PubMed=18632569; DOI=10.1073/pnas.0803356105;
RA Dong Z., Han M.-H., Fedoroff N.;
RT "The RNA-binding proteins HYL1 and SE promote accurate in vitro processing
RT of pri-miRNA by DCL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9970-9975(2008).
RN [12]
RP INTERACTION WITH DDL.
RX PubMed=18632581; DOI=10.1073/pnas.0804218105;
RA Yu B., Bi L., Zheng B., Ji L., Chevalier D., Agarwal M., Ramachandran V.,
RA Li W., Lagrange T., Walker J.C., Chen X.;
RT "The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act in
RT small RNA biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10073-10078(2008).
RN [13]
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 [14]
RP MUTAGENESIS OF GLU-395.
RX PubMed=19155326; DOI=10.1261/rna.1297109;
RA Tagami Y., Motose H., Watanabe Y.;
RT "A dominant mutation in DCL1 suppresses the hyl1 mutant phenotype by
RT promoting the processing of miRNA.";
RL RNA 15:450-458(2009).
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).
CC -!- FUNCTION: Ribonuclease (RNase) III involved in RNA-mediated post-
CC transcriptional gene silencing (PTGS). Functions in the microRNAs
CC (miRNAs) biogenesis pathway by cleaving primary miRNAs (pri-miRNAs) and
CC precursor miRNAs (pre-miRNAs). Functions with DRB1/HYL1 and SERRATE
CC proteins for accurate pri-miRNAs to miRNAs processing. Indirectly
CC involved in the production of trans-acting small interfering RNAs (ta-
CC siRNAs) derived from the TAS1, TAS2 or TAS3 endogenous transcripts by
CC participating in the production of their initiating miRNAs. Involved in
CC the processing of natural siRNAs (nat-siRNAs, derived from cis-natural
CC antisense transcripts) by cleaving 24 nucleotide nat-siRNAs into 21
CC nucleotide nat-siRNAs. Can produce RDR6-dependent endogenous ta-siRNAs
CC derived from TAS1 and TAS2. Required for the production of 30-40
CC nucleotide bacterial-induced long siRNAs (lsiRNA). Acts redundantly
CC with DICER-LIKE 3 (DCL3) to promote flowering via repression of
CC FLOWERING LOCUS C (FLC). Represses antiviral RNA silencing through
CC negative regulation of the expression of DCL4 and DCL3.
CC {ECO:0000269|PubMed:15821876, ECO:0000269|PubMed:16040244,
CC ECO:0000269|PubMed:16428603, ECO:0000269|PubMed:17579240,
CC ECO:0000269|PubMed:18003861, ECO:0000269|PubMed:18632569,
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 (via N-terminus) with DDL. Interacts (via DRBM
CC domains) with DRB1, DRB2 and DRB5. May interact with AGO1 or AGO10
CC through their common PAZ domains (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9SP32; Q8W4D8: DDL; NbExp=2; IntAct=EBI-632627, EBI-2015534;
CC Q9SP32; O04492: DRB1; NbExp=3; IntAct=EBI-632627, EBI-632620;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15821876,
CC ECO:0000269|PubMed:17442570}. Note=Localizes to nuclear dicing body
CC (also named D body), a nuclear body distributed throughout the
CC nucleoplasm and involved in miRNA processing.
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=Q9SP32-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers and seeds and detected
CC in leaves and stems. Found in ovule integuments, inflorescence and
CC floral meristems, stigma of flowers until just before pollination,
CC vasculature of the funiculus, and embryo. {ECO:0000269|PubMed:10556049,
CC ECO:0000269|PubMed:12376646}.
CC -!- DEVELOPMENTAL STAGE: Detected in the embryo, but not in the suspensor,
CC up to the globular stage. {ECO:0000269|PubMed:12376646}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality in sus-1 mutant. Weaker
CC mutant (caf-1) also exists. Mutant caf-1 produces extra whorls of
CC stamens, indefinite number of carpels and show an absence of axillary
CC inflorescence meristems and abnormally shaped leaves and floral organs.
CC {ECO:0000269|PubMed:10556049, ECO:0000269|PubMed:12376646}.
CC -!- MISCELLANEOUS: Expression in the early embryo is from the maternally
CC contributed genome.
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26461.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF187317; AAF03534.1; -; mRNA.
DR EMBL; AF292940; AAG38019.1; -; mRNA.
DR EMBL; AF292941; AAG38020.1; -; Genomic_DNA.
DR EMBL; AC007323; AAF26461.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27220.1; -; Genomic_DNA.
DR RefSeq; NP_171612.1; NM_099986.4. [Q9SP32-1]
DR PDB; 2LRS; NMR; -; A=1837-1907.
DR PDB; 7ELD; EM; 4.60 A; A=1-1909.
DR PDB; 7ELE; EM; 4.90 A; A=1-1909.
DR PDBsum; 2LRS; -.
DR PDBsum; 7ELD; -.
DR PDBsum; 7ELE; -.
DR AlphaFoldDB; Q9SP32; -.
DR BMRB; Q9SP32; -.
DR SMR; Q9SP32; -.
DR BioGRID; 24809; 10.
DR DIP; DIP-33454N; -.
DR IntAct; Q9SP32; 6.
DR STRING; 3702.AT1G01040.2; -.
DR PaxDb; Q9SP32; -.
DR PRIDE; Q9SP32; -.
DR ProteomicsDB; 222753; -. [Q9SP32-1]
DR EnsemblPlants; AT1G01040.1; AT1G01040.1; AT1G01040. [Q9SP32-1]
DR GeneID; 839574; -.
DR Gramene; AT1G01040.1; AT1G01040.1; AT1G01040. [Q9SP32-1]
DR KEGG; ath:AT1G01040; -.
DR Araport; AT1G01040; -.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_4_4_1; -.
DR InParanoid; Q9SP32; -.
DR PhylomeDB; Q9SP32; -.
DR PRO; PR:Q9SP32; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SP32; baseline and differential.
DR Genevisible; Q9SP32; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; IEA:UniProt.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IEA:UniProt.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
DR CDD; cd00593; RIBOc; 2.
DR DisProt; DP01467; -.
DR Gene3D; 1.10.1520.10; -; 2.
DR Gene3D; 3.30.160.380; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00104; RNase_III; 1.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF04851; ResIII; 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; SSF101690; SSF101690; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF69065; SSF69065; 2.
DR PROSITE; PS51327; DICER_DSRBF; 1.
DR PROSITE; PS50137; DS_RBD; 2.
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; Manganese; Metal-binding; Nuclease;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..1909
FT /note="Endoribonuclease Dicer homolog 1"
FT /id="PRO_0000180472"
FT DOMAIN 256..433
FT /note="Helicase ATP-binding"
FT DOMAIN 651..812
FT /note="Helicase C-terminal"
FT DOMAIN 840..935
FT /note="Dicer dsRNA-binding fold"
FT DOMAIN 1180..1318
FT /note="PAZ"
FT DOMAIN 1342..1518
FT /note="RNase III 1"
FT DOMAIN 1559..1707
FT /note="RNase III 2"
FT DOMAIN 1733..1796
FT /note="DRBM 1"
FT DOMAIN 1831..1906
FT /note="DRBM 2"
FT REGION 99..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1801..1831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 378..381
FT /note="DECH box"
FT COMPBIAS 104..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1812..1831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 269..276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 1597
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1693
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1696
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 1689
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MUTAGEN 395
FT /note="E->K: In dcl1-13; early-flowering and decreased
FT number of leaves. Suppresses hyl1 mutant phenotype."
FT /evidence="ECO:0000269|PubMed:19155326"
FT MUTAGEN 415
FT /note="P->S: In sin1-1; impaired reproductive development."
FT /evidence="ECO:0000269|PubMed:12376646"
FT MUTAGEN 431
FT /note="I->K: In sin1-2; impaired reproductive development."
FT /evidence="ECO:0000269|PubMed:12376646"
FT MUTAGEN 1837..1843
FT /note="NDICLRK->IAEIDPG: In caf-1; converts the floral
FT meristem to an indeterminate state."
FT /evidence="ECO:0000269|PubMed:10556049"
FT MUTAGEN 1844..1909
FT /note="Missing: In caf-1; converts the floral meristem to
FT an indeterminate state."
FT /evidence="ECO:0000269|PubMed:10556049"
FT CONFLICT 148
FT /note="S -> F (in Ref. 1; AAF03534)"
FT /evidence="ECO:0000305"
FT CONFLICT 988
FT /note="Y -> H (in Ref. 1; AAF03534)"
FT /evidence="ECO:0000305"
FT HELIX 1838..1842
FT /evidence="ECO:0007829|PDB:2LRS"
FT STRAND 1849..1854
FT /evidence="ECO:0007829|PDB:2LRS"
FT STRAND 1864..1869
FT /evidence="ECO:0007829|PDB:2LRS"
FT TURN 1873..1875
FT /evidence="ECO:0007829|PDB:2LRS"
FT STRAND 1886..1888
FT /evidence="ECO:0007829|PDB:2LRS"
FT HELIX 1889..1903
FT /evidence="ECO:0007829|PDB:2LRS"
FT HELIX 1904..1906
FT /evidence="ECO:0007829|PDB:2LRS"
SQ SEQUENCE 1909 AA; 213574 MW; EAA944F0C0C81D4C CRC64;
MVMEDEPREA TIKPSYWLDA CEDISCDLID DLVSEFDPSS VAVNESTDEN GVINDFFGGI
DHILDSIKNG GGLPNNGVSD TNSQINEVTV TPQVIAKETV KENGLQKNGG KRDEFSKEEG
DKDRKRARVC SYQSERSNLS GRGHVNNSRE GDRFMNRKRT RNWDEAGNNK KKRECNNYRR
DGRDREVRGY WERDKVGSNE LVYRSGTWEA DHERDVKKVS GGNRECDVKA EENKSKPEER
KEKVVEEQAR RYQLDVLEQA KAKNTIAFLE TGAGKTLIAI LLIKSVHKDL MSQNRKMLSV
FLVPKVPLVY QQAEVIRNQT CFQVGHYCGE MGQDFWDSRR WQREFESKQV LVMTAQILLN
ILRHSIIRME TIDLLILDEC HHAVKKHPYS LVMSEFYHTT PKDKRPAIFG MTASPVNLKG
VSSQVDCAIK IRNLETKLDS TVCTIKDRKE LEKHVPMPSE IVVEYDKAAT MWSLHETIKQ
MIAAVEEAAQ ASSRKSKWQF MGARDAGAKD ELRQVYGVSE RTESDGAANL IHKLRAINYT
LAELGQWCAY KVGQSFLSAL QSDERVNFQV DVKFQESYLS EVVSLLQCEL LEGAAAEKVA
AEVGKPENGN AHDEMEEGEL PDDPVVSGGE HVDEVIGAAV ADGKVTPKVQ SLIKLLLKYQ
HTADFRAIVF VERVVAALVL PKVFAELPSL SFIRCASMIG HNNSQEMKSS QMQDTISKFR
DGHVTLLVAT SVAEEGLDIR QCNVVMRFDL AKTVLAYIQS RGRARKPGSD YILMVERGNV
SHAAFLRNAR NSEETLRKEA IERTDLSHLK DTSRLISIDA VPGTVYKVEA TGAMVSLNSA
VGLVHFYCSQ LPGDRYAILR PEFSMEKHEK PGGHTEYSCR LQLPCNAPFE ILEGPVCSSM
RLAQQAVCLA ACKKLHEMGA FTDMLLPDKG SGQDAEKADQ DDEGEPVPGT ARHREFYPEG
VADVLKGEWV SSGKEVCESS KLFHLYMYNV RCVDFGSSKD PFLSEVSEFA ILFGNELDAE
VLSMSMDLYV ARAMITKASL AFKGSLDITE NQLSSLKKFH VRLMSIVLDV DVEPSTTPWD
PAKAYLFVPV TDNTSMEPIK GINWELVEKI TKTTAWDNPL QRARPDVYLG TNERTLGGDR
REYGFGKLRH NIVFGQKSHP TYGIRGAVAS FDVVRASGLL PVRDAFEKEV EEDLSKGKLM
MADGCMVAED LIGKIVTAAH SGKRFYVDSI CYDMSAETSF PRKEGYLGPL EYNTYADYYK
QKYGVDLNCK QQPLIKGRGV SYCKNLLSPR FEQSGESETV LDKTYYVFLP PELCVVHPLS
GSLIRGAQRL PSIMRRVESM LLAVQLKNLI SYPIPTSKIL EALTAASCQE TFCYERAELL
GDAYLKWVVS RFLFLKYPQK HEGQLTRMRQ QMVSNMVLYQ FALVKGLQSY IQADRFAPSR
WSAPGVPPVF DEDTKDGGSS FFDEEQKPVS EENSDVFEDG EMEDGELEGD LSSYRVLSSK
TLADVVEALI GVYYVEGGKI AANHLMKWIG IHVEDDPDEV DGTLKNVNVP ESVLKSIDFV
GLERALKYEF KEKGLLVEAI THASRPSSGV SCYQRLEFVG DAVLDHLITR HLFFTYTSLP
PGRLTDLRAA AVNNENFARV AVKHKLHLYL RHGSSALEKQ IREFVKEVQT ESSKPGFNSF
GLGDCKAPKV LGDIVESIAG AIFLDSGKDT TAAWKVFQPL LQPMVTPETL PMHPVRELQE
RCQQQAEGLE YKASRSGNTA TVEVFIDGVQ VGVAQNPQKK MAQKLAARNA LAALKEKEIA
ESKEKHINNG NAGEDQGENE NGNKKNGHQP FTRQTLNDIC LRKNWPMPSY RCVKEGGPAH
AKRFTFGVRV NTSDRGWTDE CIGEPMPSVK KAKDSAAVLL LELLNKTFS
