GenomeNet

Database: UniProt
Entry: Q9VF26
LinkDB: Q9VF26
Original site: Q9VF26 
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   16-OCT-2019, entry version 161.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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
RT   male 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.,
RA   Kotelnikov R.N., Gvozdev V.A.;
RT   "The RNA interference proteins and vasa locus are involved in the
RT   silencing of retrotransposons in the female germline of Drosophila
RT   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
RT   dependent 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
RT   in 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
RT   melanogaster: 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
RT   genetic elements in Drosophila melanogaster.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:6714-6719(2007).
RN   [16]
RP   ERRATUM.
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
RT   localization 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
CC       role during spermatogenesis and oogenesis by repressing
CC       transposable elements and preventing their mobilization, which is
CC       essential for the germline integrity. Acts via the piRNA metabolic
CC       process, which mediates the repression of transposable elements
CC       during meiosis by forming complexes composed of piRNAs and Piwi
CC       and govern the methylation and subsequent repression of
CC       transposons. Involved in the repression of LTR retrotransposon
CC       copia. Also involved in telomere regulation by repressing
CC       specialized telomeric retroelements HeT-A, TAHRE, and TART;
CC       Drosophila telomeres being maintained by transposition of
CC       specialized telomeric retroelements. Involved in telomeric trans-
CC       silencing, a repression mechanism by which a transposon or a
CC       transgene inserted in subtelomeric heterochromatin has the
CC       capacity to repress in trans in the female germline, a homologous
CC       transposon, or transgene located in euchromatin. Involved in the
CC       repression of testis-expressed Stellate genes by the homologous
CC       Su(Ste) repeats. Required for anteroposterior and dorsoventral
CC       axis formation during oogenesis. {ECO:0000269|PubMed:11470406,
CC       ECO:0000269|PubMed:11513298, ECO:0000269|PubMed:12154120,
CC       ECO:0000269|PubMed:14752161, ECO:0000269|PubMed:15254241,
CC       ECO:0000269|PubMed:16452506, ECO:0000269|PubMed:16809489,
CC       ECO:0000269|PubMed:17194939, ECO:0000269|PubMed:17428915,
CC       ECO:0000269|PubMed:17603126, ECO:0000269|PubMed:17941712,
CC       ECO:0000269|PubMed:19651888, 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
CC       the nuage, also named P granule, a germ-cell-specific organelle
CC       required to repress transposon during meiosis. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Egg chambers for females lacking spn-E
CC       display startmispositioned oocytes. At a low frequency, females
CC       generate early egg chambers in which the oocyte is positioned
CC       incorrectly within the cyst. At a high frequency, late-stage egg
CC       chambers exhibit a ventralized chorion. Flies show transposable
CC       elements derepression, an aberrant piRNA profile and a reduction
CC       of H3 'Lys-9' methylation and delocalization of HP1 and HP2.
CC       {ECO:0000269|PubMed:16809489, ECO:0000269|PubMed:19651888,
CC       ECO:0000269|PubMed:7590230}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB35476.2; Type=Frameshift; Evidence={ECO:0000305};
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   SMR; Q9VF26; -.
DR   BioGrid; 66977; 7.
DR   IntAct; Q9VF26; 2.
DR   STRING; 7227.FBpp0082637; -.
DR   PaxDb; Q9VF26; -.
DR   PRIDE; Q9VF26; -.
DR   EnsemblMetazoa; FBtr0083183; FBpp0082637; FBgn0003483.
DR   GeneID; 41919; -.
DR   KEGG; dme:Dmel_CG3158; -.
DR   UCSC; CG3158-RA; d. melanogaster.
DR   CTD; 41919; -.
DR   FlyBase; FBgn0003483; spn-E.
DR   eggNOG; KOG0920; Eukaryota.
DR   eggNOG; COG1643; LUCA.
DR   GeneTree; ENSGT00940000157035; -.
DR   InParanoid; Q9VF26; -.
DR   KO; K18408; -.
DR   OMA; DPCRTVY; -.
DR   OrthoDB; 278674at2759; -.
DR   PhylomeDB; Q9VF26; -.
DR   GenomeRNAi; 41919; -.
DR   PRO; PR:Q9VF26; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0003483; Expressed in 17 organ(s), highest expression level in egg cell.
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: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:0008186; F:RNA-dependent ATPase activity; TAS:FlyBase.
DR   GO; GO:0006342; P:chromatin silencing; IMP: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:0008298; P:intracellular mRNA localization; IMP:FlyBase.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IMP:FlyBase.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
DR   GO; GO:0010529; P:negative regulation of transposition; IMP:FlyBase.
DR   GO; GO:0000335; P:negative regulation of transposition, DNA-mediated; 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:0016246; P:RNA interference; TAS:FlyBase.
DR   GO; GO:0006403; P:RNA localization; TAS:FlyBase.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; IMP:FlyBase.
DR   Gene3D; 2.40.50.90; -; 1.
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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 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; SSF52540; 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; Complete proteome; Cytoplasm; Developmental protein;
KW   Differentiation; Helicase; Hydrolase; Meiosis; Nucleotide-binding;
KW   Oogenesis; Reference proteome; RNA-mediated gene silencing;
KW   Spermatogenesis.
FT   CHAIN         1   1434       Probable ATP-dependent RNA helicase
FT                                spindle-E.
FT                                /FTId=PRO_0000391916.
FT   DOMAIN      125    292       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      354    526       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      938   1001       Tudor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   NP_BIND     138    145       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       238    241       DEAH box.
FT   CONFLICT     47     47       L -> M (in Ref. 1; AAB35476).
FT                                {ECO:0000305}.
FT   CONFLICT    156    156       A -> G (in Ref. 1; AAB35476).
FT                                {ECO:0000305}.
FT   CONFLICT    325    325       Q -> H (in Ref. 1; AAB35476).
FT                                {ECO:0000305}.
FT   CONFLICT    326    326       V -> G (in Ref. 4; ABM92795).
FT                                {ECO:0000305}.
FT   CONFLICT    401    401       R -> G (in Ref. 1; AAB35476).
FT                                {ECO:0000305}.
FT   CONFLICT    542    542       N -> D (in Ref. 1; AAB35476).
FT                                {ECO:0000305}.
FT   CONFLICT    668    668       S -> SAIRWAK (in Ref. 1; AAB35476).
FT                                {ECO:0000305}.
FT   CONFLICT   1109   1110       QR -> HG (in Ref. 1; AAB35476).
FT                                {ECO:0000305}.
FT   CONFLICT   1415   1415       L -> LQ (in Ref. 1; AAB35476).
FT                                {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
//
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