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ENC_DROME
ID   ENC_DROME               Reviewed;        1818 AA.
AC   Q8MSX1; A8JNK0; B6IDK9; Q5BIH9; Q7KV61; Q9NGQ6; Q9VZM1;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Protein encore;
GN   Name=enc; ORFNames=CG10847;
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] (ISOFORM 2).
RX   PubMed=11044391; DOI=10.1242/dev.127.22.4753;
RA   Van Buskirk C., Hawkins N.C., Schuepbach T.;
RT   "Encore is a member of a novel family of proteins and affects multiple
RT   processes in Drosophila oogenesis.";
RL   Development 127:4753-4762(2000).
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, 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Booth B., Carlson J.W., Chavez C., Frise E., George R.A.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1191-1818 (ISOFORM B).
RC   STRAIN=Berkeley; TISSUE=Embryo;
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   [6]
RP   FUNCTION.
RX   PubMed=9428416; DOI=10.1242/dev.124.23.4801;
RA   Hawkins N.C., Van Buskirk C., Grossniklaus U., Schuepbach T.;
RT   "Post-transcriptional regulation of gurken by encore is required for axis
RT   determination in Drosophila.";
RL   Development 124:4801-4810(1997).
RN   [7]
RP   INTERACTION WITH HFP.
RX   PubMed=11879639; DOI=10.1016/s1534-5807(02)00128-4;
RA   Van Buskirk C., Schuepbach T.;
RT   "Half pint regulates alternative splice site selection in Drosophila.";
RL   Dev. Cell 2:343-353(2002).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH CYCE; CUL1 AND THE SCF-PROTEASOME COMPLEX.
RX   PubMed=14623823; DOI=10.1242/dev.00855;
RA   Ohlmeyer J.T., Schuepbach T.;
RT   "Encore facilitates SCF-Ubiquitin-proteasome-dependent proteolysis during
RT   Drosophila oogenesis.";
RL   Development 130:6339-6349(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; SER-270; SER-336 AND
RP   SER-535, 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: Required for the regulation of germline mitosis, karyosome
CC       formation, and establishment of dorsoventral (DS) polarity of the egg
CC       and embryo. Involved in proper grk mRNA localization and translation in
CC       the oocyte. May control germline mitosis by facilitating the cyclin E
CC       (CycE) proteolysis by the SCF-ubiquitin-proteasome complex.
CC       {ECO:0000269|PubMed:14623823, ECO:0000269|PubMed:9428416}.
CC   -!- SUBUNIT: Interacts with hfp; however, given the nuclear localization of
CC       hfp, the relevance of such interaction is unclear. Interacts with CycE,
CC       Cul1, and the SCF-proteasome complex. {ECO:0000269|PubMed:11879639,
CC       ECO:0000269|PubMed:14623823}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Colocalizes with grk.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=B; Synonyms=D;
CC         IsoId=Q8MSX1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8MSX1-2; Sequence=VSP_009327;
CC       Name=A;
CC         IsoId=Q8MSX1-3; Sequence=VSP_032690;
CC   -!- TISSUE SPECIFICITY: Expressed in all germline cells of the germarium
CC       including the stem cells and dividing cystocytes.
CC   -!- DEVELOPMENTAL STAGE: In the germarium, it begins to accumulate
CC       preferentially within the future oocyte shortly after formation of the
CC       16-cell cyst. In midoogenesis, it can be seen transiently at the
CC       posterior edge of the oocyte, but by stage 9 assumes an anterior
CC       localization, and appears to be more concentrated at the dorsal side of
CC       the oocyte, above the oocyte nucleus. This pattern of localization is
CC       similar to that seen for grk mRNA and protein, though not tightly
CC       restricted to the dorsal side.
CC   -!- MISCELLANEOUS: [Isoform 2]: Splicing donor and acceptor sites between
CC       exon 10 and exon 11 are not canonical. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-143 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF68440.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAM49887.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF243382; AAF68440.1; ALT_INIT; mRNA.
DR   EMBL; AE014296; AAF47799.2; -; Genomic_DNA.
DR   EMBL; AE014296; AAS64963.1; -; Genomic_DNA.
DR   EMBL; AE014296; ABW08455.1; -; Genomic_DNA.
DR   EMBL; BT021245; AAX33393.1; -; mRNA.
DR   EMBL; BT050449; ACJ13156.1; -; mRNA.
DR   EMBL; AY118518; AAM49887.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001097496.1; NM_001104026.2. [Q8MSX1-1]
DR   RefSeq; NP_524765.2; NM_080026.3. [Q8MSX1-1]
DR   RefSeq; NP_995992.1; NM_206270.2. [Q8MSX1-3]
DR   AlphaFoldDB; Q8MSX1; -.
DR   SMR; Q8MSX1; -.
DR   BioGRID; 69121; 31.
DR   IntAct; Q8MSX1; 2.
DR   STRING; 7227.FBpp0305410; -.
DR   iPTMnet; Q8MSX1; -.
DR   PaxDb; Q8MSX1; -.
DR   EnsemblMetazoa; FBtr0073152; FBpp0073011; FBgn0004875. [Q8MSX1-1]
DR   EnsemblMetazoa; FBtr0073153; FBpp0089267; FBgn0004875. [Q8MSX1-3]
DR   EnsemblMetazoa; FBtr0112844; FBpp0111757; FBgn0004875. [Q8MSX1-1]
DR   GeneID; 44543; -.
DR   KEGG; dme:Dmel_CG10847; -.
DR   UCSC; CG10847-RA; d. melanogaster. [Q8MSX1-1]
DR   CTD; 104374; -.
DR   FlyBase; FBgn0004875; enc.
DR   VEuPathDB; VectorBase:FBgn0004875; -.
DR   eggNOG; KOG2953; Eukaryota.
DR   GeneTree; ENSGT00940000168363; -.
DR   InParanoid; Q8MSX1; -.
DR   SignaLink; Q8MSX1; -.
DR   BioGRID-ORCS; 44543; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 44543; -.
DR   PRO; PR:Q8MSX1; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0004875; Expressed in brain and 22 other tissues.
DR   ExpressionAtlas; Q8MSX1; baseline and differential.
DR   Genevisible; Q8MSX1; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0007282; P:cystoblast division; IMP:FlyBase.
DR   GO; GO:0048134; P:germ-line cyst formation; TAS:FlyBase.
DR   GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
DR   GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
DR   GO; GO:0007310; P:oocyte dorsal/ventral axis specification; TAS:FlyBase.
DR   GO; GO:0030717; P:oocyte karyosome formation; TAS:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR   GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; TAS:FlyBase.
DR   Gene3D; 3.30.1370.50; -; 1.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   InterPro; IPR024771; SUZ.
DR   Pfam; PF01424; R3H; 1.
DR   Pfam; PF12752; SUZ; 1.
DR   SMART; SM00393; R3H; 1.
DR   SUPFAM; SSF82708; SSF82708; 1.
DR   PROSITE; PS51061; R3H; 1.
DR   PROSITE; PS51673; SUZ; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW   Oogenesis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1818
FT                   /note="Protein encore"
FT                   /id="PRO_0000086973"
FT   DOMAIN          444..508
FT                   /note="R3H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT   DOMAIN          510..576
FT                   /note="SUZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01009"
FT   REGION          47..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          936..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1176..1249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1332..1648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1684..1709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..354
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..573
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..788
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..916
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1176..1234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1344..1359
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1376..1390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1400..1446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1489..1521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1577..1631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         535
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         414
FT                   /note="R -> RVFHQS (in isoform A)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_032690"
FT   VAR_SEQ         1612..1800
FT                   /note="SNNSPNSIVGSQSNSAANTPNAAAPPPPQPQPTLVSHSGGFVVLDQTTGAAM
FT                   NASPPSLYGGGGGPNAGISGGAGASGAAGSNGGHQPGGGGGARSHIPTAQLHHSAAAAA
FT                   AAAAGSQQATAAVLSGVAAAAALGGYNPNGASGVYFKYGQTYFAHPSVALPNSRRSPSN
FT                   DIRPQMAQVAGMYPTMMIQ -> GYNPNGASGVYFKYGQTYFAHPSVALPNSRRSPSND
FT                   IRPQMAQVAGMYPTMMIQANDLHASLP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11044391"
FT                   /id="VSP_009327"
FT   CONFLICT        118
FT                   /note="G -> A (in Ref. 1; AAF68440)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220..221
FT                   /note="Missing (in Ref. 1; AAF68440)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        251..252
FT                   /note="KL -> NV (in Ref. 1; AAF68440)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="F -> Y (in Ref. 1; AAF68440)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        577
FT                   /note="G -> D (in Ref. 1; AAF68440)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        580
FT                   /note="D -> E (in Ref. 1; AAF68440)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        709
FT                   /note="A -> G (in Ref. 1; AAF68440)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        882
FT                   /note="G -> A (in Ref. 1; AAF68440)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1044
FT                   /note="I -> V (in Ref. 1; AAF68440)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1105
FT                   /note="A -> T (in Ref. 1; AAF68440)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1523
FT                   /note="P -> Q (in Ref. 1; AAF68440)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1761
FT                   /note="G -> V (in Ref. 4; AAX33393)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1818 AA;  188663 MW;  195C6C1333F5508A CRC64;
     MSSTKSQVAL ATNIPTNLSS AASASTAAAA AAVVVVASAN AAVASSANSS GVGSGSGPGP
     GSGAGVSGPV AAGTATAVAT GSTVTAATSV AATTSTSVAT ISTSCSSSSI NNINNNCGEE
     CQSAAGSSNL GRQNSFGNRR GNMKGKHLTR SHAMRESTSP PRTPTPRAAS EQQQQQLQGE
     QHEHNNNNNI NSSSKAQSAG RGNSPLMETP AVIVTSQQPQ QQQQQQQQQQ QSVPPKPQQN
     VPLSNEAEFP KLSPPKKSGG QHNRTNSNGS GMEFNNNNNS SNKKFVVDMK ANGLDNKPHN
     NSSTGVIFNS GMNYKAAERH DRHERHEMSS QNSNLSNNHD EEPYHYEPRG GGGGKKHRAN
     TNAKGNKPRL KNLGGSSSGS IDLGGGGGNG NCNNMSNNGQ SNNSSNNTSG FISRENSSEQ
     YTDYGGTDLL VFFRDTLNKN PKDRNILLKI EKDLIDFVQE NSRGCEYRFP PASSYNRMLI
     HRTAAFFGME HNVDTETQQC VIVAVAKNTR IPEIRFQSLV RDDARKSILK RDTHSFDEVR
     QSPYLCPLSL DRKAKSFEER EEDYDRARSR IFSRTGGNHD GYSGGGGDEE CYGGWEQQQQ
     QQKQSQPPRP KRPNGKMLQM QNSTESRDGM RSGGAVPKSH NFGNYGGPPS SGGPGNNSLP
     RGDSTNSIKS GRGGFVKQDS TGSTPWRLSP SSSGSIYHYD PSNLPPNQAL QHSGNQYQSQ
     NQGNSSSGGY NNYRKSSPHQ QQQSQQQQQS QQHHQQQLQQ PQQLHQQSSQ QYATTELSCS
     STESYAEEEA QSPGMECSEG YESYEQQSLP VQQQLSGNGD SASTKGDDCD SLASATACLS
     ITTSTSTKNY DRIEVQKYKN QATSPNIPAC CAVGEKLELE AGLPQEQEQE PMAGPSSSGS
     ATSSVGITEL PSSQTPLPMV NQVNCDLQSV SPSTTPYSQC EVKTPSQNHA PSAAVEEPKT
     TTWTYTQSYQ APDGSTVFHT TTTPNGAAPY CATTYQQGPD GSIYAVPQGM VYAAYPQPGV
     GTAGGASQPL FQLTTSSHPP AQTIFASPEA GAEIPGGTYM IPVFDPAQQP REGLIPAQAI
     YQTGPGGPGA TTVMPMATAA AYPTAQFATA APNGAPIYQA PLIYSSEPGG GAQLQQLPMA
     PYPIQYSYPY YHPISYYVPQ QAVAAAPMVA SQPQVGQAPM QQQAPHTGAG TTTGPPTVVS
     VSGQQHHQPH QQHHQQQQHS SNGSVVTSSA YGTRVKRTPG GGSIHYNPSY TPSSVAHAGG
     AHHPSAGSAQ IIAAPAASTT TYHALPTLTL AHGGPATGTD LSGAGGAHVY ALPAQHALIP
     TNIFPYAAAA AAAAGGPGGP PTTPQVVQQA PPPPPQSAPH HALITAAPFY PANGGNMDQG
     ASQSAPSTPA APGRQAPLFS TPPAPNNGSS GSSSAGGGGN SGGYHSNSST PHYYQGQNSN
     EGYTSPYEKR NHGGGASGAH SVGVRKPYHP GGYNPRHSVP LGGIPSGAKT PLLNSNNEPT
     PRASPSSVSL GGASSSGGAN SYPHRGPPPH TMGVKRDNKP NQLPLISGPP PSYAANSSPG
     VSSYESKPPV RLNAGAASFR SQKSMNQDYR RSVSQRNSPS ANGGGSGSHE SSNNSPNSIV
     GSQSNSAANT PNAAAPPPPQ PQPTLVSHSG GFVVLDQTTG AAMNASPPSL YGGGGGPNAG
     ISGGAGASGA AGSNGGHQPG GGGGARSHIP TAQLHHSAAA AAAAAAGSQQ ATAAVLSGVA
     AAAALGGYNP NGASGVYFKY GQTYFAHPSV ALPNSRRSPS NDIRPQMAQV AGMYPTMMIQ
     ARHPSRHPNP NYKGSRPR
 
 
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