ID SPNE_DROME Reviewed; 1434 AA.
AC Q9VF26; A2RVD0; Q26453;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=Probable ATP-dependent RNA helicase spindle-E;
DE EC=3.6.4.13;
DE AltName: Full=Homeless;
GN Name=spn-E; Synonyms=hls; ORFNames=CG3158;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Canton-S; TISSUE=Ovary;
RX PubMed=7590230; DOI=10.1101/gad.9.20.2495;
RA Gillespie D.E., Berg C.A.;
RT "Homeless is required for RNA localization in Drosophila oogenesis and
RT encodes a new member of the DE-H family of RNA-dependent ATPases.";
RL Genes Dev. 9:2495-2508(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=11513298; DOI=10.1007/s004120100136;
RA Stapleton W., Das S., McKee B.D.;
RT "A role of the Drosophila homeless gene in repression of Stellate in male
RT meiosis.";
RL Chromosoma 110:228-240(2001).
RN [6]
RP FUNCTION.
RX PubMed=11470406; DOI=10.1016/s0960-9822(01)00299-8;
RA Aravin A.A., Naumova N.M., Tulin A.V., Vagin V.V., Rozovsky Y.M.,
RA Gvozdev V.A.;
RT "Double-stranded RNA-mediated silencing of genomic tandem repeats and
RT transposable elements in the D. melanogaster germline.";
RL Curr. Biol. 11:1017-1027(2001).
RN [7]
RP FUNCTION.
RX PubMed=12154120; DOI=10.1101/gad.990802;
RA Kennerdell J.R., Yamaguchi S., Carthew R.W.;
RT "RNAi is activated during Drosophila oocyte maturation in a manner
RT dependent on aubergine and spindle-E.";
RL Genes Dev. 16:1884-1889(2002).
RN [8]
RP FUNCTION.
RX PubMed=15254241; DOI=10.1128/mcb.24.15.6742-6750.2004;
RA Aravin A.A., Klenov M.S., Vagin V.V., Bantignies F., Cavalli G.,
RA Gvozdev V.A.;
RT "Dissection of a natural RNA silencing process in the Drosophila
RT melanogaster germ line.";
RL Mol. Cell. Biol. 24:6742-6750(2004).
RN [9]
RP FUNCTION.
RX PubMed=17194939;
RA Vagin V.V., Klenov M.S., Kalmykova A.I., Stolyarenko A.D., Kotelnikov R.N.,
RA Gvozdev V.A.;
RT "The RNA interference proteins and vasa locus are involved in the silencing
RT of retrotransposons in the female germline of Drosophila melanogaster.";
RL RNA Biol. 1:54-58(2004).
RN [10]
RP FUNCTION.
RX PubMed=14752161; DOI=10.1126/science.1092653;
RA Pal-Bhadra M., Leibovitch B.A., Gandhi S.G., Rao M., Bhadra U.,
RA Birchler J.A., Elgin S.C.R.;
RT "Heterochromatic silencing and HP1 localization in Drosophila are dependent
RT on the RNAi machinery.";
RL Science 303:669-672(2004).
RN [11]
RP FUNCTION.
RX PubMed=16452506; DOI=10.1101/gad.370206;
RA Savitsky M., Kwon D., Georgiev P., Kalmykova A., Gvozdev V.;
RT "Telomere elongation is under the control of the RNAi-based mechanism in
RT the Drosophila germline.";
RL Genes Dev. 20:345-354(2006).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16809489; DOI=10.1126/science.1129333;
RA Vagin V.V., Sigova A., Li C., Seitz H., Gvozdev V., Zamore P.D.;
RT "A distinct small RNA pathway silences selfish genetic elements in the
RT germline.";
RL Science 313:320-324(2006).
RN [13]
RP FUNCTION.
RX PubMed=17603126; DOI=10.1534/genetics.106.066746;
RA Simmons M.J., Ryzek D.F., Lamour C., Goodman J.W., Kummer N.E.,
RA Merriman P.J.;
RT "Cytotype regulation by telomeric P elements in Drosophila melanogaster:
RT evidence for involvement of an RNA interference gene.";
RL Genetics 176:1945-1955(2007).
RN [14]
RP FUNCTION.
RX PubMed=17941712; DOI=10.1371/journal.pgen.0030158;
RA Josse T., Teysset L., Todeschini A.L., Sidor C.M., Anxolabehere D.,
RA Ronsseray S.;
RT "Telomeric trans-silencing: an epigenetic repression combining RNA
RT silencing and heterochromatin formation.";
RL PLoS Genet. 3:1633-1643(2007).
RN [15]
RP FUNCTION.
RX PubMed=17428915; DOI=10.1073/pnas.0701920104;
RA Lim A.K., Kai T.;
RT "Unique germ-line organelle, nuage, functions to repress selfish genetic
RT elements in Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:6714-6719(2007).
RN [16]
RP ERRATUM OF PUBMED:17428915.
RA Lim A.K., Kai T.;
RL Proc. Natl. Acad. Sci. U.S.A. 104:20143-20143(2007).
RN [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19651888; DOI=10.1083/jcb.200904063;
RA Lim A.K., Tao L., Kai T.;
RT "piRNAs mediate posttranscriptional retroelement silencing and localization
RT to pi-bodies in the Drosophila germline.";
RL J. Cell Biol. 186:333-342(2009).
CC -!- FUNCTION: Probable ATP-binding RNA helicase which plays a central role
CC during spermatogenesis and oogenesis by repressing transposable
CC elements and preventing their mobilization, which is essential for the
CC germline integrity. Acts via the piRNA metabolic process, which
CC mediates the repression of transposable elements during meiosis by
CC forming complexes composed of piRNAs and Piwi and govern the
CC methylation and subsequent repression of transposons. Involved in the
CC repression of LTR retrotransposon copia. Also involved in telomere
CC regulation by repressing specialized telomeric retroelements HeT-A,
CC TAHRE, and TART; Drosophila telomeres being maintained by transposition
CC of specialized telomeric retroelements. Involved in telomeric trans-
CC silencing, a repression mechanism by which a transposon or a transgene
CC inserted in subtelomeric heterochromatin has the capacity to repress in
CC trans in the female germline, a homologous transposon, or transgene
CC located in euchromatin. Involved in the repression of testis-expressed
CC Stellate genes by the homologous Su(Ste) repeats. Required for
CC anteroposterior and dorsoventral axis formation during oogenesis.
CC {ECO:0000269|PubMed:11470406, ECO:0000269|PubMed:11513298,
CC ECO:0000269|PubMed:12154120, ECO:0000269|PubMed:14752161,
CC ECO:0000269|PubMed:15254241, ECO:0000269|PubMed:16452506,
CC ECO:0000269|PubMed:16809489, ECO:0000269|PubMed:17194939,
CC ECO:0000269|PubMed:17428915, ECO:0000269|PubMed:17603126,
CC ECO:0000269|PubMed:17941712, ECO:0000269|PubMed:19651888,
CC ECO:0000269|PubMed:7590230}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Component of the
CC nuage, also named P granule, a germ-cell-specific organelle required to
CC repress transposon during meiosis. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Egg chambers for females lacking spn-E display
CC startmispositioned oocytes. At a low frequency, females generate early
CC egg chambers in which the oocyte is positioned incorrectly within the
CC cyst. At a high frequency, late-stage egg chambers exhibit a
CC ventralized chorion. Flies show transposable elements derepression, an
CC aberrant piRNA profile and a reduction of H3 'Lys-9' methylation and
CC delocalization of HP1 and HP2. {ECO:0000269|PubMed:16809489,
CC ECO:0000269|PubMed:19651888, ECO:0000269|PubMed:7590230}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB35476.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; S79915; AAB35476.2; ALT_FRAME; mRNA.
DR EMBL; AE014297; AAF55235.1; -; Genomic_DNA.
DR EMBL; BT029921; ABM92795.1; -; mRNA.
DR EMBL; BT100306; ACZ52618.1; -; mRNA.
DR PIR; T13889; T13889.
DR RefSeq; NP_476741.1; NM_057393.4.
DR AlphaFoldDB; Q9VF26; -.
DR SMR; Q9VF26; -.
DR BioGRID; 66977; 8.
DR IntAct; Q9VF26; 2.
DR STRING; 7227.FBpp0082637; -.
DR PaxDb; 7227-FBpp0082637; -.
DR DNASU; 41919; -.
DR EnsemblMetazoa; FBtr0083183; FBpp0082637; FBgn0003483.
DR GeneID; 41919; -.
DR KEGG; dme:Dmel_CG3158; -.
DR UCSC; CG3158-RA; d. melanogaster.
DR AGR; FB:FBgn0003483; -.
DR CTD; 41919; -.
DR FlyBase; FBgn0003483; spn-E.
DR VEuPathDB; VectorBase:FBgn0003483; -.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000157035; -.
DR HOGENOM; CLU_002601_1_0_1; -.
DR InParanoid; Q9VF26; -.
DR OMA; FWMHYIF; -.
DR OrthoDB; 21853at2759; -.
DR PhylomeDB; Q9VF26; -.
DR BioGRID-ORCS; 41919; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41919; -.
DR PRO; PR:Q9VF26; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003483; Expressed in egg cell and 15 other cell types or tissues.
DR ExpressionAtlas; Q9VF26; baseline and differential.
DR Genevisible; Q9VF26; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; TAS:FlyBase.
DR GO; GO:0004386; F:helicase activity; ISS:FlyBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; TAS:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IGI:FlyBase.
DR GO; GO:0098795; P:global gene silencing by mRNA cleavage; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin formation; IMP:FlyBase.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
DR GO; GO:0030720; P:oocyte localization involved in germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0001556; P:oocyte maturation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; IMP:FlyBase.
DR GO; GO:0009951; P:polarity specification of dorsal/ventral axis; IMP:FlyBase.
DR GO; GO:0007315; P:pole plasm assembly; NAS:FlyBase.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:FlyBase.
DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0010526; P:retrotransposon silencing; IMP:FlyBase.
DR GO; GO:0006403; P:RNA localization; TAS:FlyBase.
DR GO; GO:0140965; P:secondary piRNA processing; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd17988; DEXHc_TDRD9; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.40.50.90; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF113; ATP-DEPENDENT RNA HELICASE TDRD9; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00567; TUDOR; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Developmental protein; Differentiation; Helicase;
KW Hydrolase; Meiosis; Nucleotide-binding; Oogenesis; Reference proteome;
KW RNA-mediated gene silencing; Spermatogenesis.
FT CHAIN 1..1434
FT /note="Probable ATP-dependent RNA helicase spindle-E"
FT /id="PRO_0000391916"
FT DOMAIN 125..292
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 354..526
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 938..1001
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT MOTIF 238..241
FT /note="DEAH box"
FT BINDING 138..145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 47
FT /note="L -> M (in Ref. 1; AAB35476)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="A -> G (in Ref. 1; AAB35476)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="Q -> H (in Ref. 1; AAB35476)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="V -> G (in Ref. 4; ABM92795)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="R -> G (in Ref. 1; AAB35476)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="N -> D (in Ref. 1; AAB35476)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="S -> SAIRWAK (in Ref. 1; AAB35476)"
FT /evidence="ECO:0000305"
FT CONFLICT 1109..1110
FT /note="QR -> HG (in Ref. 1; AAB35476)"
FT /evidence="ECO:0000305"
FT CONFLICT 1415
FT /note="L -> LQ (in Ref. 1; AAB35476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1434 AA; 164510 MW; 67E8CD39F1484B13 CRC64;
MDQEVMDFFD FSKELKRVAA APQGYISSDP RLMATKFKSS EVPNRELIGT DYVSKIVAKE
KCLLNGTLLN EQPQGKRIRT LDDLDTDDEG EETEIRRDDE YYKKFRFNLN RDKNLSIYAK
REEILAAINA HPVVIIKGET GCGKTTQVPQ YILDEAYKSG KYCNIVVTQP RRIAAISIAN
RVCQEREWQQ NTVCSFQVGL HRPNSLEDTR LLYCTTGVLL NNLINNKTLT HYTHIVLDEV
HERDQNMDFL LIVVRRLLAT NSRHVKIILM SATIDAKELS DYFTTTNSIP PVITTNHRRK
HSIEKFYRDQ LGSIIWNEED VGHQQVPEIN KHGYRAAVKI IVIIDNMERK AAIQSRQSYD
EALRYGAVLI FLPGIYEIDT MAENLTCMLE NDPNIKVSIV RCFSLMTPEN QRDVFNPPPP
GFRKIILTTN IAESSITVPD VSYVIDFCLA KVKVTDTASS FSSLRLTWAS KANCRQRAGR
VGRLRSGRVY RMVNKHFYQR EMPEFGIPEM LRLPLQNSVL KAKVLNMGSP VEILALALSP
PNLSDIHNTI LLLKEVGALY LTVDGIYDPL DGDLTYWGTI MSRLPLDTRQ SRLIILGYIF
NMLEEAIIIA AGLSTPGLFA HEGGRSQLGD SFWMHYIFSD GSGSDLVAIW RVYLTYLNIV
ENGHDQESAI RWAKRFHVSL RSLKEIHLLV QELRVRCTHL GLIPFPVNPN QMMDDREKAI
MLKVIIAGAF YPNYFTRSKE SCADTDRNIY QTISGHDPCR TVYFTNFKPA YMGELYTRRI
KELFQEVRIP PENMDVTFQE GSQKVFVTFK QDDWIEGSSK YVPVSGRVQS EVYKAVMMRQ
NRVERPIHIM NPSAFMSYVQ QRGIGDVIEG RWIPPTKPLN VELLALPSVF DKTISGSITC
IVNCGKFFFQ PQSFEECIRN MSEIFNAPQQ LRNYVTNASA IAKGMMVLAK RDSYFQRATV
IRPENQSNRQ PMFYVRFIDY GNCTLLPMQL MRLMPRELTE QYGDLPPRVF ECRLAMVQPS
SVVSGNNRWS TAANDMLKTV AQCGLIDIEV YSLFNNVAAV LIHMRDGIIN DKLVELMLCR
RSDEDYMSRK DHDFRLRRQE SARNLSTAQR QQINEEYLRS CQLPQDHDLP PPPLEKCKTV
VMLKGPNSPL ECTMRSITRV GLSKRVNIDH LSVNALLLDA DPQDHHDHLI VAHEIAESRN
GQTLTARGTT LMPNVQGFGA LMVMLFSPTM QLKCNKEGTS YVSVLGGLGC DPDTNEPYFA
EHDVLINLDV NILEDDVILI NQIRYYIDSV FFNFKEENNP AVSVNERVSI YTQLRSLINR
LLCKDRRYIE RNMSNADFEW ETNPELPLPN EPFGKRAIFP MHSLTELQEE DTGRLVQLRE
NCSMLHKWRN FEGTLPHMTC KLCNQLLESV PQLRLHLLTI LHRDREKQID YCNQ
//
