DCR1_DROME
ID DCR1_DROME Reviewed; 2249 AA.
AC Q9VCU9; Q961S7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Endoribonuclease Dcr-1;
DE Short=Protein dicer-1;
DE EC=3.1.26.-;
GN Name=Dcr-1 {ECO:0000312|EMBL:AAF56056.1}; ORFNames=CG4792;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF56056.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF56056.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAK84929.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1338-2249.
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=11201747; DOI=10.1038/35053110;
RA Bernstein E., Caudy A.A., Hammond S.M., Hannon G.J.;
RT "Role for a bidentate ribonuclease in the initiation step of RNA
RT interference.";
RL Nature 409:363-366(2001).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH AGO2.
RX PubMed=11498593; DOI=10.1126/science.1064023;
RA Hammond S.M., Boettcher S., Caudy A.A., Kobayashi R., Hannon G.J.;
RT "Argonaute2, a link between genetic and biochemical analyses of RNAi.";
RL Science 293:1146-1150(2001).
RN [6] {ECO:0000305}
RP INTERACTION WITH FMR1.
RX PubMed=12368261; DOI=10.1101/gad.1022002;
RA Ishizuka A., Siomi M.C., Siomi H.;
RT "A Drosophila fragile X protein interacts with components of RNAi and
RT ribosomal proteins.";
RL Genes Dev. 16:2497-2508(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH PIWI AND VAS.
RX PubMed=16949822; DOI=10.1016/j.cub.2006.08.051;
RA Megosh H.B., Cox D.N., Campbell C., Lin H.;
RT "The role of PIWI and the miRNA machinery in Drosophila germline
RT determination.";
RL Curr. Biol. 16:1884-1894(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1423; SER-1877 AND SER-1880,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Essential for RNA interference (RNAi); double-stranded RNA
CC (dsRNA) induces potent and specific gene silencing. RNAi is mediated by
CC the RNA-induced silencing complex (RISC), a sequence-specific,
CC multicomponent nuclease that destroys or silences messenger RNAs
CC homologous to the silencing trigger. May carry out the initiation step
CC of RNAi by cleaving dsRNA to produce 22 bp dsRNAs (siRNAs) which target
CC the selective destruction of homologous RNAs. During embryogenesis,
CC involved in germline fate determination. {ECO:0000269|PubMed:11201747,
CC ECO:0000269|PubMed:11498593, ECO:0000269|PubMed:16949822}.
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 AGO2 and Fmr1 to form the RNA-induced silencing
CC complex (RISC), a ribonucleoprotein (RNP) complex involved in
CC translation regulation; other components of the complex are RpL5,
CC RpL11, AGO2 and Rm62 (PubMed:11498593, PubMed:12368261). Interacts with
CC piwi and vas; these interactions occur in the polar granules
CC (PubMed:16949822). {ECO:0000269|PubMed:11498593,
CC ECO:0000269|PubMed:12368261, ECO:0000269|PubMed:16949822}.
CC -!- INTERACTION:
CC Q9VCU9; Q8IP72: loqs; NbExp=4; IntAct=EBI-112170, EBI-162836;
CC Q9VCU9; Q9VJY9: loqs; NbExp=12; IntAct=EBI-112170, EBI-638074;
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00657}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK84929.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF56056.1; -; Genomic_DNA.
DR EMBL; AY050230; AAK84929.1; ALT_INIT; mRNA.
DR RefSeq; NP_524453.1; NM_079729.3.
DR AlphaFoldDB; Q9VCU9; -.
DR SMR; Q9VCU9; -.
DR BioGRID; 67642; 24.
DR DIP; DIP-23028N; -.
DR IntAct; Q9VCU9; 11.
DR STRING; 7227.FBpp0083717; -.
DR iPTMnet; Q9VCU9; -.
DR PaxDb; Q9VCU9; -.
DR PRIDE; Q9VCU9; -.
DR EnsemblMetazoa; FBtr0084324; FBpp0083717; FBgn0039016.
DR GeneID; 42693; -.
DR KEGG; dme:Dmel_CG4792; -.
DR UCSC; CG4792-RA; d. melanogaster.
DR CTD; 42693; -.
DR FlyBase; FBgn0039016; Dcr-1.
DR VEuPathDB; VectorBase:FBgn0039016; -.
DR eggNOG; KOG0701; Eukaryota.
DR GeneTree; ENSGT00940000156287; -.
DR HOGENOM; CLU_000907_4_4_1; -.
DR InParanoid; Q9VCU9; -.
DR OMA; TTYLYCT; -.
DR OrthoDB; 1337630at2759; -.
DR PhylomeDB; Q9VCU9; -.
DR Reactome; R-DME-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-DME-426486; Small interfering RNA (siRNA) biogenesis.
DR SignaLink; Q9VCU9; -.
DR BioGRID-ORCS; 42693; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42693; -.
DR PRO; PR:Q9VCU9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039016; Expressed in eye disc (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q9VCU9; baseline and differential.
DR Genevisible; Q9VCU9; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0016442; C:RISC complex; ISS:UniProtKB.
DR GO; GO:0070578; C:RISC-loading complex; IPI:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016443; F:bidentate ribonuclease III activity; IDA:FlyBase.
DR GO; GO:0004530; F:deoxyribonuclease I activity; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070883; F:pre-miRNA binding; IDA:FlyBase.
DR GO; GO:0004525; F:ribonuclease III activity; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:FlyBase.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0033227; P:dsRNA transport; IMP:FlyBase.
DR GO; GO:0042078; P:germ-line stem cell division; IMP:FlyBase.
DR GO; GO:0030727; P:germarium-derived female germ-line cyst formation; IMP:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
DR GO; GO:0035196; P:miRNA processing; IMP:FlyBase.
DR GO; GO:0045448; P:mitotic cell cycle, embryonic; IMP:FlyBase.
DR GO; GO:0007279; P:pole cell formation; IMP:FlyBase.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:FlyBase.
DR GO; GO:0031054; P:pre-miRNA processing; IDA:FlyBase.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR GO; GO:0070922; P:RISC complex assembly; IMP:FlyBase.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GO_Central.
DR GO; GO:0007367; P:segment polarity determination; IGI:FlyBase.
DR GO; GO:0030422; P:siRNA processing; IDA:UniProtKB.
DR CDD; cd10843; DSRM_DICER; 1.
DR CDD; cd00593; RIBOc; 2.
DR Gene3D; 1.10.1520.10; -; 2.
DR Gene3D; 3.30.160.380; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR044441; DICER_DSRM.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
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; PF00636; Ribonuclease_3; 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; 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 ATP-binding; Endonuclease; Helicase; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nuclease; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..2249
FT /note="Endoribonuclease Dcr-1"
FT /id="PRO_0000180474"
FT DOMAIN 485..648
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 825..920
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 1099..1246
FT /note="PAZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00142"
FT DOMAIN 1698..1919
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1993..2150
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 2175..2241
FT /note="DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 436..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1314..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2032
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 2136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 2139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 2132
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1423
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1877
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1880
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 1338..1339
FT /note="PT -> AI (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1345
FT /note="L -> I (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2249 AA; 255330 MW; D693F0432AC8033D CRC64;
MAFHWCDNNL HTTVFTPRDF QVELLATAYE RNTIICLGHR SSKEFIALKL LQELSRRARR
HGRVSVYLSC EVGTSTEPCS IYTMLTHLTD LRVWQEQPDM QIPFDHCWTD YHVSILRPEG
FLYLLETREL LLSSVELIVL EDCHDSAVYQ RIRPLFENHI MPAPPADRPR ILGLAGPLHS
AGCELQQLSA MLATLEQSVL CQIETASDIV TVLRYCSRPH EYIVQCAPFE MDELSLVLAD
VLNTHKSFLL DHRYDPYEIY GTDQFMDELK DIPDPKVDPL NVINSLLVVL HEMGPWCTQR
AAHHFYQCNE KLKVKTPHER HYLLYCLVST ALIQLYSLCE HAFHRHLGSG SDSRQTIERY
SSPKVRRLLQ TLRCFKPEEV HTQADGLRRM RHQVDQADFN RLSHTLESKC RMVDQMDQPP
TETRALVATL EQILHTTEDR QTNRSAARVT PTPTPAHAKP KPSSGANTAQ PRTRRRVYTR
RHHRDHNDGS DTLCALIYCN QNHTARVLFE LLAEISRRDP DLKFLRCQYT TDRVADPTTE
PKEAELEHRR QEEVLKRFRM HDCNVLIGTS VLEEGIDVPK CNLVVRWDPP TTYRSYVQCK
GRARAAPAYH VILVAPSYKS PTVGSVQLTD RSHRYICATG DTTEADSDSD DSAMPNSSGS
DPYTFGTARG TVKILNPEVF SKQPPTACDI KLQEIQDELP AAAQLDTSNS SDEAVSMSNT
SPSESSTEQK SRRFQCELSS LTEPEDTSDT TAEIDTAHSL ASTTKDLVHQ MAQYREIEQM
LLSKCANTEP PEQEQSEAER FSACLAAYRP KPHLLTGASV DLGSAIALVN KYCARLPSDT
FTKLTALWRC TRNERAGVTL FQYTLRLPIN SPLKHDIVGL PMPTQTLARR LAALQACVEL
HRIGELDDQL QPIGKEGFRA LEPDWECFEL EPEDEQIVQL SDEPRPGTTK RRQYYYKRIA
SEFCDCRPVA GAPCYLYFIQ LTLQCPIPEE QNTRGRKIYP PEDAQQGFGI LTTKRIPKLS
AFSIFTRSGE VKVSLELAKE RVILTSEQIV CINGFLNYTF TNVLRLQKFL MLFDPDSTEN
CVFIVPTVKA PAGGKHIDWQ FLELIQANGN TMPRAVPDEE RQAQPFDPQR FQDAVVMPWY
RNQDQPQYFY VAEICPHLSP LSCFPGDNYR TFKHYYLVKY GLTIQNTSQP LLDVDHTSAR
LNFLTPRYVN RKGVALPTSS EETKRAKREN LEQKQILVPE LCTVHPFPAS LWRTAVCLPC
ILYRINGLLL ADDIRKQVSA DLGLGRQQIE DEDFEWPMLD FGWSLSEVLK KSRESKQKES
LKDDTINGKD LADVEKKPTS EETQLDKDSK DDKVEKSAIE LIIEGEEKLQ EADDFIEIGT
WSNDMADDIA SFNQEDDDED DAFHLPVLPA NVKFCDQQTR YGSPTFWDVS NGESGFKGPK
SSQNKQGGKG KAKGPAKPTF NYYDSDNSLG SSYDDDDNAG PLNYMHHNYS SDDDDVADDI
DAGRIAFTSK NEAETIETAQ EVEKRQKQLS IIQATNANER QYQQTKNLLI GFNFKHEDQK
EPATIRYEES IAKLKTEIES GGMLVPHDQQ LVLKRSDAAE AQVAKVSMME LLKQLLPYVN
EDVLAKKLGD RRELLLSDLV ELNADWVARH EQETYNVMGC GDSFDNYNDH HRLNLDEKQL
KLQYERIEIE PPTSTKAITS AILPAGFSFD RQPDLVGHPG PSPSIILQAL TMSNANDGIN
LERLETIGDS FLKYAITTYL YITYENVHEG KLSHLRSKQV ANLNLYRLGR RKRLGEYMIA
TKFEPHDNWL PPCYYVPKEL EKALIEAKIP THHWKLADLL DIKNLSSVQI CEMVREKADA
LGLEQNGGAQ NGQLDDSNDS CNDFSCFIPY NLVSQHSIPD KSIADCVEAL IGAYLIECGP
RGALLFMAWL GVRVLPITRQ LDGGNQEQRI PGSTKPNAEN VVTVYGAWPT PRSPLLHFAP
NATEELDQLL SGFEEFEESL GYKFRDRSYL LQAMTHASYT PNRLTDCYQR LEFLGDAVLD
YLITRHLYED PRQHSPGALT DLRSALVNNT IFASLAVRHG FHKFFRHLSP GLNDVIDRFV
RIQQENGHCI SEEYYLLSEE ECDDAEDVEV PKALGDVFES IAGAIFLDSN MSLDVVWHVY
SNMMSPEIEQ FSNSVPKSPI RELLELEPET AKFGKPEKLA DGRRVRVTVD VFCKGTFRGI
GRNYRIAKCT AAKCALRQLK KQGLIAKKD
