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SPNE_DROME
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   03-AUG-2022, entry version 173.
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; Q9VF26; -.
DR   DNASU; 41919; -.
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   VEuPathDB; VectorBase:FBgn0003483; -.
DR   eggNOG; KOG0920; Eukaryota.
DR   GeneTree; ENSGT00940000157035; -.
DR   HOGENOM; CLU_002601_1_0_1; -.
DR   InParanoid; Q9VF26; -.
DR   OMA; DPCRTVY; -.
DR   OrthoDB; 278674at2759; -.
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 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 assembly; 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: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:0035194; P:post-transcriptional gene silencing by RNA; TAS:FlyBase.
DR   GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR   GO; GO:0006403; P:RNA localization; TAS:FlyBase.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   CDD; cd04508; TUDOR; 1.
DR   Gene3D; 2.40.50.90; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   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; 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
 
 
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