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ANTP_DROME
ID   ANTP_DROME              Reviewed;         378 AA.
AC   P02833; Q95SZ6;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 213.
DE   RecName: Full=Homeotic protein antennapedia;
GN   Name=Antp; ORFNames=CG1028;
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] (ISOFORM 1).
RX   PubMed=10408949; DOI=10.1002/j.1460-2075.1986.tb04275.x;
RA   Schneuwly S., Kuroiwa A., Baumgartner P., Gehring W.J.;
RT   "Structural organization and sequence of the homeotic gene Antennapedia of
RT   Drosophila melanogaster.";
RL   EMBO J. 5:733-739(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=Oregon-R; TISSUE=Embryo, Larva, and Pupae;
RX   PubMed=2879222; DOI=10.1128/mcb.6.12.4667-4675.1986;
RA   Stroeher V.L., Jorgensen E.M., Garber R.L.;
RT   "Multiple transcripts from the Antennapedia gene of Drosophila
RT   melanogaster.";
RL   Mol. Cell. Biol. 6:4667-4675(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=2879223; DOI=10.1128/mcb.6.12.4676-4689.1986;
RA   Laughon A., Boulet A.M., Bermingham J.R. Jr., Laymon R.A., Scott M.P.;
RT   "Structure of transcripts from the homeotic Antennapedia gene of Drosophila
RT   melanogaster: two promoters control the major protein-coding region.";
RL   Mol. Cell. Biol. 6:4676-4689(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
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   [5]
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   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 296-364.
RX   PubMed=6330741; DOI=10.1073/pnas.81.13.4115;
RA   Scott M.P., Weiner A.J.;
RT   "Structural relationships among genes that control development: sequence
RT   homology between the Antennapedia, Ultrabithorax, and fushi tarazu loci of
RT   Drosophila.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:4115-4119(1984).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 296-378.
RX   PubMed=6327065; DOI=10.1016/0092-8674(84)90370-2;
RA   McGinnis W., Garber R.L., Wirz J., Kuroiwa A., Gehring W.J.;
RT   "A homologous protein-coding sequence in Drosophila homeotic genes and its
RT   conservation in other metazoans.";
RL   Cell 37:403-408(1984).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 297-357.
RX   PubMed=2416463; DOI=10.1016/0092-8674(85)90013-3;
RA   Regulski M., Harding K., Kostriken R., Karch F., Levine M., McGinnis W.;
RT   "Homeo box genes of the Antennapedia and bithorax complexes of
RT   Drosophila.";
RL   Cell 43:71-80(1985).
RN   [11]
RP   MUTANT ANALYSIS.
RX   PubMed=3821869; DOI=10.1038/325816a0;
RA   Schneuwly S., Klemenz R., Gehring W.J.;
RT   "Redesigning the body plan of Drosophila by ectopic expression of the
RT   homoeotic gene Antennapedia.";
RL   Nature 325:816-818(1987).
RN   [12]
RP   STRUCTURE BY NMR OF HOMEOBOX.
RX   PubMed=2164583; DOI=10.1016/0022-2836(90)90155-f;
RA   Billeter M., Qian Y.-Q., Otting G., Mueller M., Gehring W.J., Wuethrich K.;
RT   "Determination of the three-dimensional structure of the Antennapedia
RT   homeodomain from Drosophila in solution by 1H nuclear magnetic resonance
RT   spectroscopy.";
RL   J. Mol. Biol. 214:183-197(1990).
RN   [13]
RP   STRUCTURE BY NMR OF HOMEOBOX.
RX   PubMed=7903397; DOI=10.1006/jmbi.1993.1660;
RA   Qian Y.-Q., Otting G., Billeter M., Mueller M., Gehring W.J., Wuethrich K.;
RT   "Nuclear magnetic resonance spectroscopy of a DNA complex with the
RT   uniformly 13C-labeled Antennapedia homeodomain and structure determination
RT   of the DNA-bound homeodomain.";
RL   J. Mol. Biol. 234:1070-1083(1993).
RN   [14]
RP   STRUCTURE BY NMR OF HOMEOBOX.
RX   PubMed=7903398; DOI=10.1006/jmbi.1993.1661;
RA   Billeter M., Qian Y.-Q., Otting G., Mueller M., Gehring W.J., Wuethrich K.;
RT   "Determination of the nuclear magnetic resonance solution structure of an
RT   Antennapedia homeodomain-DNA complex.";
RL   J. Mol. Biol. 234:1084-1093(1993).
RN   [15]
RP   STRUCTURE BY NMR OF 279-363.
RX   PubMed=1359544; DOI=10.1073/pnas.89.22.10738;
RA   Qian Y.-Q., Otting G., Furukubo-Tokunaga K., Affolter M., Gehring W.J.,
RA   Wuethrich K.;
RT   "NMR structure determination reveals that the homeodomain is connected
RT   through a flexible linker to the main body in the Drosophila Antennapedia
RT   protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10738-10742(1992).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 297-356.
RX   PubMed=9699632; DOI=10.1038/1382;
RA   Fraenkel E., Pabo C.O.;
RT   "Comparison of X-ray and NMR structures for the Antennapedia homeodomain-
RT   DNA complex.";
RL   Nat. Struct. Biol. 5:692-697(1998).
CC   -!- FUNCTION: Sequence-specific transcription factor which is part of a
CC       developmental regulatory system that regulates segmental identity in
CC       the mesothorax. Provides cells with specific positional identities on
CC       the anterior-posterior axis.
CC   -!- INTERACTION:
CC       P02833-1; O18381: ey; NbExp=4; IntAct=EBI-15726199, EBI-232318;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=A, B, I, J;
CC         IsoId=P02833-1; Sequence=Displayed;
CC       Name=2; Synonyms=H;
CC         IsoId=P02833-2; Sequence=VSP_008097, VSP_008098;
CC   -!- MISCELLANEOUS: Loss of Antp results in altered development of the
CC       embryonic thoracic segments. Overexpression can cause antennae to be
CC       transformed into legs.
CC   -!- SIMILARITY: Belongs to the Antp homeobox family. {ECO:0000305}.
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DR   EMBL; X03790; CAA27417.1; -; Genomic_DNA.
DR   EMBL; X03791; CAA27417.1; JOINED; Genomic_DNA.
DR   EMBL; M20704; AAA70214.1; -; mRNA.
DR   EMBL; M20705; AAA70216.1; -; mRNA.
DR   EMBL; AE001572; AAD19793.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAG22205.3; -; Genomic_DNA.
DR   EMBL; AE014297; AAS65111.1; -; Genomic_DNA.
DR   EMBL; AY060407; AAL25446.1; -; mRNA.
DR   EMBL; M14496; AAA28376.1; -; Genomic_DNA.
DR   EMBL; K01948; AAA28373.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M12009; AAA79241.1; -; mRNA.
DR   PIR; A23450; A25399.
DR   RefSeq; NP_996167.1; NM_206445.1. [P02833-1]
DR   RefSeq; NP_996168.1; NM_206446.1. [P02833-1]
DR   RefSeq; NP_996170.1; NM_206448.1. [P02833-1]
DR   RefSeq; NP_996175.1; NM_206453.1. [P02833-1]
DR   RefSeq; NP_996176.1; NM_206454.1. [P02833-2]
DR   PDB; 1AHD; NMR; -; P=297-363.
DR   PDB; 1HOM; NMR; -; A=297-363.
DR   PDB; 1KZ0; NMR; -; A=339-354.
DR   PDB; 1KZ5; NMR; -; A=339-354.
DR   PDB; 1OMQ; NMR; -; A=339-354.
DR   PDB; 1SAN; NMR; -; A=303-363.
DR   PDB; 2HOA; NMR; -; A=297-363.
DR   PDB; 2ND6; NMR; -; A=338-354.
DR   PDB; 2ND7; NMR; -; A=338-354.
DR   PDB; 2ND8; NMR; -; A=338-354.
DR   PDB; 4XIC; X-ray; 2.69 A; A/D=297-356.
DR   PDB; 4XID; X-ray; 2.70 A; A/D=297-356.
DR   PDB; 5JLW; X-ray; 2.09 A; A/D=297-356.
DR   PDB; 5JLX; X-ray; 2.75 A; A/D=297-356.
DR   PDB; 9ANT; X-ray; 2.40 A; A/B=296-356.
DR   PDBsum; 1AHD; -.
DR   PDBsum; 1HOM; -.
DR   PDBsum; 1KZ0; -.
DR   PDBsum; 1KZ5; -.
DR   PDBsum; 1OMQ; -.
DR   PDBsum; 1SAN; -.
DR   PDBsum; 2HOA; -.
DR   PDBsum; 2ND6; -.
DR   PDBsum; 2ND7; -.
DR   PDBsum; 2ND8; -.
DR   PDBsum; 4XIC; -.
DR   PDBsum; 4XID; -.
DR   PDBsum; 5JLW; -.
DR   PDBsum; 5JLX; -.
DR   PDBsum; 9ANT; -.
DR   AlphaFoldDB; P02833; -.
DR   BMRB; P02833; -.
DR   SMR; P02833; -.
DR   BioGRID; 66033; 182.
DR   DIP; DIP-51405N; -.
DR   IntAct; P02833; 10.
DR   STRING; 7227.FBpp0081161; -.
DR   PaxDb; P02833; -.
DR   DNASU; 40835; -.
DR   EnsemblMetazoa; FBtr0081646; FBpp0081160; FBgn0260642. [P02833-2]
DR   EnsemblMetazoa; FBtr0081647; FBpp0081161; FBgn0260642. [P02833-1]
DR   EnsemblMetazoa; FBtr0081652; FBpp0081162; FBgn0260642. [P02833-1]
DR   EnsemblMetazoa; FBtr0081654; FBpp0089245; FBgn0260642. [P02833-1]
DR   EnsemblMetazoa; FBtr0081655; FBpp0089246; FBgn0260642. [P02833-1]
DR   GeneID; 40835; -.
DR   KEGG; dme:Dmel_CG1028; -.
DR   CTD; 40835; -.
DR   FlyBase; FBgn0260642; Antp.
DR   VEuPathDB; VectorBase:FBgn0260642; -.
DR   eggNOG; KOG0489; Eukaryota.
DR   InParanoid; P02833; -.
DR   PhylomeDB; P02833; -.
DR   SignaLink; P02833; -.
DR   BioGRID-ORCS; 40835; 0 hits in 3 CRISPR screens.
DR   EvolutionaryTrace; P02833; -.
DR   GenomeRNAi; 40835; -.
DR   PRO; PR:P02833; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0260642; Expressed in presumptive embryonic/larval central nervous system and 42 other tissues.
DR   ExpressionAtlas; P02833; baseline and differential.
DR   Genevisible; P02833; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IBA:GO_Central.
DR   GO; GO:0007507; P:heart development; IEP:FlyBase.
DR   GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
DR   GO; GO:0007494; P:midgut development; TAS:FlyBase.
DR   GO; GO:0042694; P:muscle cell fate specification; IMP:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0014019; P:neuroblast development; IMP:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR   GO; GO:0050767; P:regulation of neurogenesis; IMP:FlyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007383; P:specification of segmental identity, antennal segment; IMP:FlyBase.
DR   GO; GO:0007384; P:specification of segmental identity, thorax; IMP:UniProtKB.
DR   GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017995; Homeobox_antennapedia.
DR   InterPro; IPR001827; Homeobox_Antennapedia_CS.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR020479; Homeobox_metazoa.
DR   Pfam; PF00046; Homeodomain; 1.
DR   PRINTS; PR00025; ANTENNAPEDIA.
DR   PRINTS; PR00024; HOMEOBOX.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00032; ANTENNAPEDIA; 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; Repeat.
FT   CHAIN           1..378
FT                   /note="Homeotic protein antennapedia"
FT                   /id="PRO_0000200259"
FT   DNA_BIND        297..356
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          48..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           283..288
FT                   /note="Antp-type hexapeptide"
FT   COMPBIAS        71..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         296..297
FT                   /note="ER -> GK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_008097"
FT   VAR_SEQ         298..378
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12537569"
FT                   /id="VSP_008098"
FT   CONFLICT        300
FT                   /note="G -> E (in Ref. 10; AAA79241)"
FT                   /evidence="ECO:0000305"
FT   STRAND          299..301
FT                   /evidence="ECO:0007829|PDB:1HOM"
FT   HELIX           306..318
FT                   /evidence="ECO:0007829|PDB:5JLW"
FT   HELIX           324..334
FT                   /evidence="ECO:0007829|PDB:5JLW"
FT   HELIX           338..353
FT                   /evidence="ECO:0007829|PDB:5JLW"
SQ   SEQUENCE   378 AA;  42760 MW;  D653232A8622D055 CRC64;
     MTMSTNNCES MTSYFTNSYM GADMHHGHYP GNGVTDLDAQ QMHHYSQNAN HQGNMPYPRF
     PPYDRMPYYN GQGMDQQQQH QVYSRPDSPS SQVGGVMPQA QTNGQLGVPQ QQQQQQQQPS
     QNQQQQQAQQ APQQLQQQLP QVTQQVTHPQ QQQQQPVVYA SCKLQAAVGG LGMVPEGGSP
     PLVDQMSGHH MNAQMTLPHH MGHPQAQLGY TDVGVPDVTE VHQNHHNMGM YQQQSGVPPV
     GAPPQGMMHQ GQGPPQMHQG HPGQHTPPSQ NPNSQSSGMP SPLYPWMRSQ FGKCQERKRG
     RQTYTRYQTL ELEKEFHFNR YLTRRRRIEI AHALCLTERQ IKIWFQNRRM KWKKENKTKG
     EPGSGGEGDE ITPPNSPQ
 
 
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