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BCD_DROME
ID   BCD_DROME               Reviewed;         494 AA.
AC   P09081; Q5BI92; Q86BA9; Q86BP2; Q8INR7; Q8ST46; Q8STB1; Q8T9S9; Q8T9T0;
AC   Q8T9T1; Q95TN3; Q9UAM0; Q9VI47;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 3.
DT   03-AUG-2022, entry version 212.
DE   RecName: Full=Homeotic protein bicoid;
DE   AltName: Full=PRD-4;
GN   Name=bcd; ORFNames=CG1034;
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 [GENOMIC DNA / MRNA] (ISOFORMS A; D AND G).
RC   STRAIN=Oregon-R; TISSUE=Embryo;
RX   PubMed=2901954; DOI=10.1002/j.1460-2075.1988.tb03004.x;
RA   Berleth T., Burri M., Thoma G., Bopp D., Richstein S., Frigerio G.,
RA   Noll M., Nuesslein-Volhard C.;
RT   "The role of localization of bicoid RNA in organizing the anterior pattern
RT   of the Drosophila embryo.";
RL   EMBO J. 7:1749-1756(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM D), AND VARIANTS.
RC   STRAIN=Z116, Z131, Z145, Z157, Z159, Z184, Z186, Z191, Z194, Z196, Z197,
RC   Z209, Z210, Z212, Z216, Z229, Z266, Z346, Z362, Z377, Z384, Z398, Z82, Z84,
RC   and Z95;
RX   PubMed=12082119; DOI=10.1093/oxfordjournals.molbev.a004179;
RA   Baines J.F., Chen Y., Das A., Stephan W.;
RT   "DNA sequence variation at a duplicated gene: excess of replacement
RT   polymorphism and extensive haplotype structure in the Drosophila
RT   melanogaster bicoid region.";
RL   Mol. Biol. Evol. 19:989-998(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RA   Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A.,
RA   Palazzolo M.J.;
RT   "Complete sequence of the Antennapedia complex of Drosophila.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM G).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 12-47 AND 86-156 (ISOFORMS
RP   D/G).
RX   PubMed=2877746; DOI=10.1016/0092-8674(86)90516-7;
RA   Frigerio G., Burri M., Bopp D., Baumgartner S., Noll M.;
RT   "Structure of the segmentation gene paired and the Drosophila PRD gene set
RT   as part of a gene network.";
RL   Cell 47:735-746(1986).
RN   [9]
RP   POSSIBLE RNA-BINDING DOMAIN.
RX   PubMed=2752425; DOI=10.1016/0092-8674(89)90834-9;
RA   Rebagliati M.;
RT   "An RNA recognition motif in the bicoid protein.";
RL   Cell 58:231-232(1989).
RN   [10]
RP   INTERACTION WITH BIN3.
RX   PubMed=10717484; DOI=10.1016/s0378-1119(00)00048-2;
RA   Zhu W., Hanes S.D.;
RT   "Identification of Drosophila bicoid-interacting proteins using a custom
RT   two-hybrid selection.";
RL   Gene 245:329-339(2000).
RN   [11]
RP   INTERACTION WITH BIN1.
RX   PubMed=11455422; DOI=10.1007/s004270100135;
RA   Zhu W., Foehr M., Jaynes J.B., Hanes S.D.;
RT   "Drosophila SAP18, a member of the Sin3/Rpd3 histone deacetylase complex,
RT   interacts with Bicoid and inhibits its activity.";
RL   Dev. Genes Evol. 211:109-117(2001).
CC   -!- FUNCTION: Segment polarity protein that provides positional cues for
CC       the development of head and thoracic segments. Regulates the expression
CC       of zygotic genes, possibly through its homeodomain, and inhibits the
CC       activity of other maternal gene products. May also bind RNA. Interacts
CC       with Bin1 to repress transcription of bicoid target genes in the
CC       anterior tip of the embryo; a process known as retraction.
CC   -!- SUBUNIT: Interacts with Bin1; in vitro and yeast cells. Interacts with
CC       bin3. {ECO:0000269|PubMed:10717484, ECO:0000269|PubMed:11455422}.
CC   -!- INTERACTION:
CC       P09081; Q9VEX9: Bin1; NbExp=2; IntAct=EBI-196628, EBI-129424;
CC       P09081; Q7K480: bin3; NbExp=4; IntAct=EBI-196628, EBI-180984;
CC       P09081; O97102: smt3; NbExp=3; IntAct=EBI-196628, EBI-114439;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=G;
CC         IsoId=P09081-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=P09081-3; Sequence=VSP_002235;
CC       Name=D;
CC         IsoId=P09081-2; Sequence=VSP_002234;
CC       Name=E;
CC         IsoId=P09081-4; Sequence=VSP_027203;
CC       Name=F;
CC         IsoId=P09081-5; Sequence=VSP_027203, VSP_002234;
CC   -!- TISSUE SPECIFICITY: Maternal expression is an anterior cap concentrated
CC       in the cortical cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC   -!- SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X07870; CAA30720.1; -; Genomic_DNA.
DR   EMBL; X14458; CAA32627.1; -; mRNA.
DR   EMBL; X14459; CAB37631.1; -; mRNA.
DR   EMBL; X14460; CAA32629.1; -; mRNA.
DR   EMBL; AF466621; AAL77008.1; -; Genomic_DNA.
DR   EMBL; AF466622; AAL77009.1; -; Genomic_DNA.
DR   EMBL; AF466623; AAL77010.1; -; Genomic_DNA.
DR   EMBL; AF466624; AAL77011.1; -; Genomic_DNA.
DR   EMBL; AF466625; AAL77012.1; -; Genomic_DNA.
DR   EMBL; AF466626; AAL77013.1; -; Genomic_DNA.
DR   EMBL; AF466627; AAL77014.1; -; Genomic_DNA.
DR   EMBL; AF466628; AAL77015.1; -; Genomic_DNA.
DR   EMBL; AF466629; AAL77016.1; -; Genomic_DNA.
DR   EMBL; AF466630; AAL77017.1; -; Genomic_DNA.
DR   EMBL; AF466631; AAL77018.1; -; Genomic_DNA.
DR   EMBL; AF466632; AAL77019.1; -; Genomic_DNA.
DR   EMBL; AF466633; AAL77020.1; -; Genomic_DNA.
DR   EMBL; AF466634; AAL77021.1; -; Genomic_DNA.
DR   EMBL; AF466635; AAL77022.1; -; Genomic_DNA.
DR   EMBL; AF466636; AAL77023.1; -; Genomic_DNA.
DR   EMBL; AF466637; AAL77024.1; -; Genomic_DNA.
DR   EMBL; AF466638; AAL77025.1; -; Genomic_DNA.
DR   EMBL; AF466639; AAL77026.1; -; Genomic_DNA.
DR   EMBL; AF466640; AAL77027.1; -; Genomic_DNA.
DR   EMBL; AF466641; AAL77028.1; -; Genomic_DNA.
DR   EMBL; AF466642; AAL77029.1; -; Genomic_DNA.
DR   EMBL; AF466643; AAL77030.1; -; Genomic_DNA.
DR   EMBL; AF466644; AAL77031.1; -; Genomic_DNA.
DR   EMBL; AF466645; AAL77032.1; -; Genomic_DNA.
DR   EMBL; AE001572; AAD19798.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF54085.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13368.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13369.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13371.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAO41514.1; -; Genomic_DNA.
DR   EMBL; AY058658; AAL13887.1; -; mRNA.
DR   EMBL; BT021332; AAX33480.1; -; mRNA.
DR   EMBL; M14549; AAA28385.1; -; Genomic_DNA.
DR   EMBL; K03517; AAA28391.1; -; mRNA.
DR   PIR; S00835; WJFFBC.
DR   RefSeq; NP_476825.1; NM_057477.5. [P09081-3]
DR   RefSeq; NP_731111.1; NM_169157.3. [P09081-2]
DR   RefSeq; NP_731113.2; NM_169159.4. [P09081-4]
DR   RefSeq; NP_788587.1; NM_176410.3. [P09081-1]
DR   RefSeq; NP_788588.1; NM_176411.3. [P09081-5]
DR   PDB; 1ZQ3; NMR; -; P=97-163.
DR   PDBsum; 1ZQ3; -.
DR   AlphaFoldDB; P09081; -.
DR   BMRB; P09081; -.
DR   SMR; P09081; -.
DR   BioGRID; 66028; 92.
DR   IntAct; P09081; 47.
DR   MINT; P09081; -.
DR   STRING; 7227.FBpp0081168; -.
DR   PaxDb; P09081; -.
DR   DNASU; 40830; -.
DR   EnsemblMetazoa; FBtr0081664; FBpp0081164; FBgn0000166. [P09081-3]
DR   EnsemblMetazoa; FBtr0081665; FBpp0081165; FBgn0000166. [P09081-2]
DR   EnsemblMetazoa; FBtr0081666; FBpp0081166; FBgn0000166. [P09081-4]
DR   EnsemblMetazoa; FBtr0081667; FBpp0081167; FBgn0000166. [P09081-5]
DR   EnsemblMetazoa; FBtr0081668; FBpp0081168; FBgn0000166. [P09081-1]
DR   GeneID; 40830; -.
DR   KEGG; dme:Dmel_CG1034; -.
DR   CTD; 40830; -.
DR   FlyBase; FBgn0000166; bcd.
DR   VEuPathDB; VectorBase:FBgn0000166; -.
DR   eggNOG; KOG0489; Eukaryota.
DR   GeneTree; ENSGT00940000172642; -.
DR   InParanoid; P09081; -.
DR   OMA; FYHHTLP; -.
DR   PhylomeDB; P09081; -.
DR   SignaLink; P09081; -.
DR   BioGRID-ORCS; 40830; 0 hits in 1 CRISPR screen.
DR   EvolutionaryTrace; P09081; -.
DR   GenomeRNAi; 40830; -.
DR   PRO; PR:P09081; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0000166; Expressed in cleaving embryo and 10 other tissues.
DR   Genevisible; P09081; DM.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:FlyBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IMP:FlyBase.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0030371; F:translation repressor activity; IGI:FlyBase.
DR   GO; GO:0007355; P:anterior region determination; IMP:FlyBase.
DR   GO; GO:0009948; P:anterior/posterior axis specification; TAS:FlyBase.
DR   GO; GO:0008595; P:anterior/posterior axis specification, embryo; TAS:FlyBase.
DR   GO; GO:0008358; P:maternal determination of anterior/posterior axis, embryo; TAS:FlyBase.
DR   GO; GO:0017148; P:negative regulation of translation; IMP:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:FlyBase.
DR   GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
DR   GO; GO:0008293; P:torso signaling pathway; IMP:FlyBase.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   Pfam; PF00046; Homeodomain; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Developmental protein; DNA-binding;
KW   Homeobox; Nucleus; Reference proteome; RNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..494
FT                   /note="Homeotic protein bicoid"
FT                   /id="PRO_0000049014"
FT   DNA_BIND        97..156
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..440
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        16..38
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..76
FT                   /note="Missing (in isoform E and isoform F)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_027203"
FT   VAR_SEQ         56..400
FT                   /note="Missing (in isoform A)"
FT                   /evidence="ECO:0000303|PubMed:2901954"
FT                   /id="VSP_002235"
FT   VAR_SEQ         81..85
FT                   /note="Missing (in isoform D and isoform F)"
FT                   /evidence="ECO:0000303|PubMed:12537569,
FT                   ECO:0000303|PubMed:2901954"
FT                   /id="VSP_002234"
FT   VARIANT         284
FT                   /note="Q -> H (in strain: Z362)"
FT   VARIANT         317
FT                   /note="E -> K (in strain: Z229)"
FT   VARIANT         337
FT                   /note="A -> S (in strain: Z95, Z197 and Z229)"
FT   VARIANT         438
FT                   /note="A -> P (in strain: Z184, Z210 and Z216)"
FT   VARIANT         458
FT                   /note="V -> L (in strain: Z157)"
FT   VARIANT         460
FT                   /note="M -> L (in strain: Oregon-R, Z145, Z266, Z346 and
FT                   Z398)"
FT   CONFLICT        298
FT                   /note="F -> S (in Ref. 1; CAB37631)"
FT                   /evidence="ECO:0000305"
FT   HELIX           106..116
FT                   /evidence="ECO:0007829|PDB:1ZQ3"
FT   HELIX           124..134
FT                   /evidence="ECO:0007829|PDB:1ZQ3"
FT   HELIX           138..157
FT                   /evidence="ECO:0007829|PDB:1ZQ3"
SQ   SEQUENCE   494 AA;  54511 MW;  561D8509D5C11FD3 CRC64;
     MAQPPPDQNF YHHPLPHTHT HPHPHSHPHP HSHPHPHHQH PQLQLPPQFR NPFDLLFDER
     TGAINYNYIR PYLPNQMPKP DVFPSEELPD SLVMRRPRRT RTTFTSSQIA ELEQHFLQGR
     YLTAPRLADL SAKLALGTAQ VKIWFKNRRR RHKIQSDQHK DQSYEGMPLS PGMKQSDGDP
     PSLQTLSLGG GATPNALTPS PTPSTPTAHM TEHYSESFNA YYNYNGGHNH AQANRHMHMQ
     YPSGGGPGPG STNVNGGQFF QQQQVHNHQQ QLHHQGNHVP HQMQQQQQQA QQQQYHHFDF
     QQKQASACRV LVKDEPEADY NFNSSYYMRS GMSGATASAS AVARGAASPG SEVYEPLTPK
     NDESPSLCGI GIGGPCAIAV GETEAADDMD DGTSKKTTLQ ILEPLKGLDK SCDDGSSDDM
     STGIRALAGT GNRGAAFAKF GKPSPPQGPQ PPLGMGGVAM GESNQYQCTM DTIMQAYNPH
     RNAAGNSQFA YCFN
 
 
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