ATX2_DROME
ID ATX2_DROME Reviewed; 1084 AA.
AC Q8SWR8; Q8IHA4; Q8IHF7; Q8INE0; Q8T081; Q95U80; Q9VF64;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ataxin-2 homolog;
DE Short=Datx2;
GN Name=Atx2 {ECO:0000312|FlyBase:FBgn0041188}; ORFNames=CG5166;
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:AAN13663.1}
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:AAN13663.1}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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:AAM12250.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B), AND RNA EDITING
RP OF POSITIONS 381 AND 398.
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL39639.1},
RC Head {ECO:0000312|EMBL:AAM12250.1}, and
RC Testis {ECO:0000312|EMBL:AAN71095.1};
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, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12524342; DOI=10.1093/genetics/162.4.1687;
RA Satterfield T.F., Jackson S.M., Pallanck L.J.;
RT "A Drosophila homolog of the polyglutamine disease gene SCA2 is a dosage-
RT sensitive regulator of actin filament formation.";
RL Genetics 162:1687-1702(2002).
RN [5] {ECO:0000305}
RP RNA EDITING OF POSITIONS 381 AND 398.
RX PubMed=17018572; DOI=10.1261/rna.254306;
RA Stapleton M., Carlson J.W., Celniker S.E.;
RT "RNA editing in Drosophila melanogaster: new targets and functional
RT consequences.";
RL RNA 12:1922-1932(2006).
RN [6] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-211 AND SER-221, AND
RP 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).
RN [8]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH TYF; PABP AND LSM12A,
RP IDENTIFICATION IN A COMPLEX WITH TYF; PABP AND ME31B, INTERACTION WITH TYF;
RP PABP; ME31B AND LSM12A, AND DOMAIN.
RX PubMed=28388438; DOI=10.1016/j.molcel.2017.03.004;
RA Lee J., Yoo E., Lee H., Park K., Hur J.H., Lim C.;
RT "LSM12 and ME31B/DDX6 Define Distinct Modes of Posttranscriptional
RT Regulation by ATAXIN-2 Protein Complex in Drosophila Circadian Pacemaker
RT Neurons.";
RL Mol. Cell 66:129-140(2017).
CC -!- FUNCTION: RNA binding protein that regulates various processes
CC including circadian behaviors, actin filament formation, eye
CC development and oocyte formation (PubMed:12524342, PubMed:28388438).
CC Forms a complex with tyf and pAbp which functions in adult circadian
CC pacemaker neurons to sustain circadian rhythms likely by switching
CC between activator and repressor modes of post-transcriptional
CC regulation via interaction with Lsm12a or me31B (PubMed:28388438).
CC Forms an activator complex (Atx2-tyf activator complex) via association
CC with Lsm12a and activates the TYF-dependent translation of per to
CC maintain 24 hour periodicity in circadian locomotor behaviors
CC (PubMed:28388438). Forms a repressor complex (Atx2-Not1 repressor
CC complex) via the me31B-dependent association with Not1 to promote Not1-
CC dependent post-transcriptional gene silencing and support high-
CC amplitude circadian rhythms in a per-independent manner
CC (PubMed:28388438). Regulates actin filament formation, though it does
CC not directly assemble with actin filaments (PubMed:12524342). Required
CC for oocyte specification and oocyte positioning in the female germline
CC (PubMed:12524342). Also required for normal eye development and bristle
CC morphology (PubMed:12524342). {ECO:0000269|PubMed:12524342,
CC ECO:0000269|PubMed:28388438}.
CC -!- SUBUNIT: Homodimer (PubMed:28388438). In the circadian pacemaker
CC neurons, core component of the Atx2-tyf activator complex composed of
CC at least Atx2, tyf, pAbp, Lsm12a (PubMed:28388438). In the circadian
CC pacemaker neurons, also a core component of the Atx2-Not1 repressor
CC complex composed of at least Atx2, tyf, pAbp, me31B (PubMed:28388438).
CC Interacts (via PAM2 motif) with pAbp (PubMed:28388438). Interacts (via
CC N-terminus) with tyf independently of pAbp (PubMed:28388438). Forms a
CC subcomplex composed of Atx2 and pAbP which can associate with the 5'
CC cap of pre-mRNAs independently of tyf, Lsm12a or me31B
CC (PubMed:28388438). Interacts with Lsm12a and me31B (PubMed:28388438).
CC {ECO:0000269|PubMed:28388438}.
CC -!- INTERACTION:
CC Q8SWR8; Q9W4M7: tyf; NbExp=3; IntAct=EBI-3486190, EBI-194676;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12524342}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B {ECO:0000269|PubMed:10731132};
CC IsoId=Q8SWR8-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:10731132};
CC IsoId=Q8SWR8-2; Sequence=VSP_052610, VSP_052611, VSP_052612;
CC Name=C {ECO:0000269|PubMed:10731132};
CC IsoId=Q8SWR8-3; Sequence=VSP_052610;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Zygotic
CC expression is seen in third larval instar, pupae, and adults.
CC {ECO:0000269|PubMed:12524342}.
CC -!- DOMAIN: The PAM2 motif, and therefore interaction with pAbp, is
CC essential for binding to the 5' cap of pre-mRNAs.
CC {ECO:0000269|PubMed:28388438}.
CC -!- RNA EDITING: Modified_positions=381 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}, 398 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}; Note=Partially edited. Target of Adar.
CC {ECO:0000269|PubMed:17018572};
CC -!- DISRUPTION PHENOTYPE: Second instar larvae lethal.
CC {ECO:0000269|PubMed:12524342}.
CC -!- SIMILARITY: Belongs to the ataxin-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39639.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAN71028.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN71028.1; Type=Miscellaneous discrepancy; Note=Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAN71095.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAN13663.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13664.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF55196.2; -; Genomic_DNA.
DR EMBL; AY058253; AAL13482.1; -; mRNA.
DR EMBL; AY069494; AAL39639.1; ALT_INIT; mRNA.
DR EMBL; AY095516; AAM12250.1; -; mRNA.
DR EMBL; BT001272; AAN71028.1; ALT_SEQ; mRNA.
DR EMBL; BT001340; AAN71095.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001287339.1; NM_001300410.1. [Q8SWR8-3]
DR RefSeq; NP_650466.2; NM_142209.3. [Q8SWR8-2]
DR RefSeq; NP_732033.1; NM_169657.3. [Q8SWR8-1]
DR RefSeq; NP_732034.2; NM_169658.3. [Q8SWR8-3]
DR AlphaFoldDB; Q8SWR8; -.
DR SMR; Q8SWR8; -.
DR BioGRID; 66945; 35.
DR DIP; DIP-61417N; -.
DR ELM; Q8SWR8; -.
DR IntAct; Q8SWR8; 5.
DR MINT; Q8SWR8; -.
DR STRING; 7227.FBpp0082555; -.
DR iPTMnet; Q8SWR8; -.
DR PaxDb; Q8SWR8; -.
DR PRIDE; Q8SWR8; -.
DR DNASU; 41883; -.
DR EnsemblMetazoa; FBtr0083099; FBpp0082555; FBgn0041188. [Q8SWR8-1]
DR EnsemblMetazoa; FBtr0083100; FBpp0082556; FBgn0041188. [Q8SWR8-3]
DR EnsemblMetazoa; FBtr0083101; FBpp0082557; FBgn0041188. [Q8SWR8-2]
DR EnsemblMetazoa; FBtr0344377; FBpp0310750; FBgn0041188. [Q8SWR8-3]
DR GeneID; 41883; -.
DR KEGG; dme:Dmel_CG5166; -.
DR UCSC; CG5166-RA; d. melanogaster. [Q8SWR8-1]
DR CTD; 41883; -.
DR FlyBase; FBgn0041188; Atx2.
DR VEuPathDB; VectorBase:FBgn0041188; -.
DR eggNOG; KOG2375; Eukaryota.
DR GeneTree; ENSGT00940000157795; -.
DR HOGENOM; CLU_282884_0_0_1; -.
DR InParanoid; Q8SWR8; -.
DR PhylomeDB; Q8SWR8; -.
DR SignaLink; Q8SWR8; -.
DR BioGRID-ORCS; 41883; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Atx2; fly.
DR GenomeRNAi; 41883; -.
DR PRO; PR:Q8SWR8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0041188; Expressed in second segment of antenna (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q8SWR8; differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:FlyBase.
DR GO; GO:0035770; C:ribonucleoprotein granule; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IDA:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:UniProtKB.
DR GO; GO:0097167; P:circadian regulation of translation; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:UniProtKB.
DR GO; GO:0042051; P:compound eye photoreceptor development; IMP:FlyBase.
DR GO; GO:0046959; P:habituation; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0060965; P:negative regulation of miRNA-mediated gene silencing; IMP:FlyBase.
DR GO; GO:0009994; P:oocyte differentiation; IMP:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:FlyBase.
DR GO; GO:0032092; P:positive regulation of protein binding; IMP:FlyBase.
DR GO; GO:0062029; P:positive regulation of stress granule assembly; IMP:FlyBase.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0090328; P:regulation of olfactory learning; IMP:FlyBase.
DR GO; GO:0051823; P:regulation of synapse structural plasticity; IMP:FlyBase.
DR GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR009604; LsmAD_domain.
DR InterPro; IPR025852; SM_dom_ATX.
DR PANTHER; PTHR12854; PTHR12854; 1.
DR Pfam; PF06741; LsmAD; 1.
DR Pfam; PF14438; SM-ATX; 1.
DR SMART; SM01272; LsmAD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Phosphoprotein;
KW Reference proteome; RNA editing.
FT CHAIN 1..1084
FT /note="Ataxin-2 homolog"
FT /id="PRO_0000311703"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..774
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..883
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1032
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform A and isoform C)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_052610"
FT VAR_SEQ 936..949
FT /note="PPMAASQMHVSASA -> RKSILPIIKHFIFF (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_052611"
FT VAR_SEQ 950..1084
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_052612"
FT VARIANT 381
FT /note="K -> R (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
FT VARIANT 398
FT /note="K -> R (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
FT CONFLICT 368
FT /note="T -> A (in Ref. 3; AAL13482)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1084 AA; 117578 MW; 626F4A60A652E8E2 CRC64;
MNNNSKRKTR PTGGGASGGI SRYNSNDNSL RPTNNKAGAG GGNGGAAVRP SAQGVYNNTF
FMHSATALVG SVVEVRLRSG NIYEGVFRTF SGNFDIALEL PACIKSKNLP EEGKVPKHII
FPADTVVTIV AKDFDSQYAT AGAFQTDGAI SDKCNGARPD EKELEPWDSG ANGDIDIELD
SAANGWDPNE MFRKNENTFG VTSTFDDSLA SYTVPLDKGD SLEFKEAEAK AEKLAAEIEN
NPTCRDRLDL ENGDEEALFA AVERPSTEQD QRGDRGDRER NDRDREREER DRDRDRDRGN
KPRGAGDFQL RETMSSDRYI TKQTRSITGP QLSHVGMSSQ GSGRDRDTRG DGSMMMQSGG
GSGQGGSTQS TAALMLAGGL KGVGPAPSAN ASADSSSKYS GGSMVKRKTV PQGGKVMRNN
VPTGGSNVSV SQGGNGNSVG QNKGGYQPSM GMPSQYSYQG NSQIMHGSSQ YRNQSHMGGA
NKLNGDSNAN TNKPLPQRQM RQYQGSQSNS SLNYGGEPQS LGKPVHGSHG GHPGQNSNSP
PLQTAGPQQQ QQQQQQQQQQ QQQQQPPQQQ QHQNIQPQGQ NTQPARQVRT RDNQMQELRQ
FGQDFQLAPS NTSPPQQQQQ QQQQQQQHQV QQQQQRALQQ SASPPQQQQQ QQQQQQHVVL
HQVPQTHLHQ AALSQPHYVP QQQPQQAPLP QQQHVPHHMQ QKAQQQQLVE TQHQHVQKQH
QSQPQVQQPP PQLLQDPSQQ PLPIYHTMPP PQTSPVVVTS PVLLEQPPPQ PMPVVQQQQT
QQLATPKPEV SPAPPSSNTT TPTGIASTPT AGVIASAGSE KTTPAAPTPT SNSATVPTGT
AATAGGATGT TPVVKKHVLN PSAKPFTPRG PSTPNPSRPH TPQTPVPMTN IYTTTGGHVP
PAANQPIYVM QPQHPFPPQT HPQAGQPPRL RRSNYPPMAA SQMHVSASAA TGQPLITAGP
IPQFIQYGHA PHQQQFQSHT YAPMQMRVYP DQPQQLQFMT QTPQSTTPSP GQPHQQFHPP
PQPSPAGGGP QPAFTPPTQA ATYQLMCVHP QSLLANHYFP PPTPQHPQQN QQQYQIVMQQ
HQPQ
