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GUS_DROME
ID   GUS_DROME               Reviewed;         279 AA.
AC   A1Z6E0; A1Z6D7; A1Z6D9; A1Z6E2; F2FB59; Q7JUY1;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Protein gustavus {ECO:0000312|EMBL:AAM68373.2};
GN   Name=gus; ORFNames=CG2944;
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] {ECO:0000312|EMBL:AAM68373.2}
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   [2] {ECO:0000312|EMBL:AAM68373.2}
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   [3] {ECO:0000312|EMBL:AAM50263.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC   TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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   [4] {ECO:0000312|EMBL:ADZ74173.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:ADZ74173.1}; TISSUE=Embryo;
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH VAS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=12479811; DOI=10.1016/s1534-5807(02)00361-1;
RA   Styhler S., Nakamura A., Lasko P.;
RT   "VASA localization requires the SPRY-domain and SOCS-box containing
RT   protein, GUSTAVUS.";
RL   Dev. Cell 3:865-876(2002).
RN   [6] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH VAS AND CUL-5, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   TRP-219.
RX   PubMed=20123973; DOI=10.1128/mcb.01100-09;
RA   Kugler J.M., Woo J.S., Oh B.H., Lasko P.;
RT   "Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3
RT   ligase specificity receptors.";
RL   Mol. Cell. Biol. 30:1769-1782(2010).
RN   [7] {ECO:0000305, ECO:0000312|PDB:2FNJ}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 27-251 IN COMPLEX WITH MOUSE
RP   ELONGIN-B AND ELONGIN-C, INTERACTION WITH VAS, AND MUTAGENESIS OF TYR-131;
RP   GLY-147; ARG-148; GLU-187; ARG-204 AND TRP-219.
RX   PubMed=16498413; DOI=10.1038/sj.emboj.7600994;
RA   Woo J.S., Imm J.H., Min C.K., Kim K.J., Cha S.S., Oh B.H.;
RT   "Structural and functional insights into the B30.2/SPRY domain.";
RL   EMBO J. 25:1353-1363(2006).
RN   [8] {ECO:0000305, ECO:0000312|PDB:2IHS}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 27-232 IN COMPLEX WITH VAS
RP   FRAGMENT, AND MUTAGENESIS OF TRP-219.
RX   PubMed=17189197; DOI=10.1016/j.molcel.2006.11.009;
RA   Woo J.S., Suh H.Y., Park S.Y., Oh B.H.;
RT   "Structural basis for protein recognition by B30.2/SPRY domains.";
RL   Mol. Cell 24:967-976(2006).
CC   -!- FUNCTION: Involved in the localization of vas to the posterior pole of
CC       the oocyte. Required maternally in the germ line for efficient
CC       primordial germ cell formation. {ECO:0000269|PubMed:12479811,
CC       ECO:0000269|PubMed:20123973}.
CC   -!- SUBUNIT: Interacts (via B30.2/SPRY domain) with vas; this interaction
CC       may be necessary for the transport of vas to the posterior pole of the
CC       oocyte. Interacts with Cul-5. May associate with the Elongin BC complex
CC       composed of Elongin-B and Elongin-C. {ECO:0000269|PubMed:12479811,
CC       ECO:0000269|PubMed:16498413, ECO:0000269|PubMed:17189197,
CC       ECO:0000269|PubMed:20123973}.
CC   -!- INTERACTION:
CC       A1Z6E0; O96757: stumps; NbExp=3; IntAct=EBI-75338, EBI-74922;
CC       A1Z6E0; P09052: vas; NbExp=5; IntAct=EBI-75338, EBI-134067;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12479811,
CC       ECO:0000269|PubMed:20123973}. Nucleus {ECO:0000269|PubMed:12479811,
CC       ECO:0000269|PubMed:20123973}. Note=Component of the cytoplasmic
CC       ribonucleoprotein (RNP) bodies which concentrate at the perinuclear
CC       region of the nurse cell and in punctate aggregates throughout the
CC       cytoplasm. Some cortical enrichment of these aggregates is also
CC       observed. At stage 7, accumulates in the anterior cytoplasm of the
CC       oocyte, whereas during stage 10 accumulates at the posterior pole. This
CC       posterior distribution is not maintained in later developmental stages.
CC       {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}.
CC   -!- TISSUE SPECIFICITY: Expressed in ovaries, primarily in nurse cells and
CC       oocytes (at protein level). {ECO:0000269|PubMed:12479811,
CC       ECO:0000269|PubMed:20123973}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during oogenesis, in early embryos (0 to
CC       4 hours) and in fertile adult females (at protein level).
CC       {ECO:0000269|PubMed:12479811, ECO:0000269|PubMed:20123973}.
CC   -!- DISRUPTION PHENOTYPE: Homozygous females produce defective eggs, which
CC       desiccate and collapse soon after egg laying, or embryos, which hatch
CC       very rarely. Mutants exhibit wing morphology defects, including
CC       blistering, formation of ectopic vein material, and loss of material at
CC       the margin. {ECO:0000269|PubMed:20123973}.
CC   -!- SIMILARITY: Belongs to the SPSB family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM50263.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ACU12389.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ACX32987.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ADZ74173.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=ADZ74173.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE013599; AAF57346.2; -; Genomic_DNA.
DR   EMBL; AE013599; AAF57347.3; -; Genomic_DNA.
DR   EMBL; AE013599; AAG22337.2; -; Genomic_DNA.
DR   EMBL; AE013599; AAM68372.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAM68373.2; -; Genomic_DNA.
DR   EMBL; AE013599; AAM68374.2; -; Genomic_DNA.
DR   EMBL; AY119609; AAM50263.1; ALT_INIT; mRNA.
DR   EMBL; BT089043; ACU12389.1; ALT_INIT; mRNA.
DR   EMBL; BT099916; ACX32987.1; ALT_INIT; mRNA.
DR   EMBL; BT126146; ADZ74173.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001246140.1; NM_001259211.2.
DR   RefSeq; NP_610158.3; NM_136314.4.
DR   RefSeq; NP_724398.2; NM_165418.3.
DR   RefSeq; NP_724399.2; NM_165419.3.
DR   RefSeq; NP_724400.2; NM_165420.3.
DR   RefSeq; NP_724401.2; NM_165421.3.
DR   RefSeq; NP_724402.2; NM_165422.3.
DR   PDB; 2FNJ; X-ray; 1.80 A; A=27-251.
DR   PDB; 2IHS; X-ray; 2.20 A; A/B=27-232.
DR   PDBsum; 2FNJ; -.
DR   PDBsum; 2IHS; -.
DR   AlphaFoldDB; A1Z6E0; -.
DR   SMR; A1Z6E0; -.
DR   BioGRID; 61396; 50.
DR   IntAct; A1Z6E0; 35.
DR   MINT; A1Z6E0; -.
DR   STRING; 7227.FBpp0301582; -.
DR   PaxDb; A1Z6E0; -.
DR   DNASU; 35478; -.
DR   EnsemblMetazoa; FBtr0309846; FBpp0301580; FBgn0026238.
DR   EnsemblMetazoa; FBtr0309847; FBpp0301581; FBgn0026238.
DR   EnsemblMetazoa; FBtr0309848; FBpp0301582; FBgn0026238.
DR   EnsemblMetazoa; FBtr0309849; FBpp0301583; FBgn0026238.
DR   EnsemblMetazoa; FBtr0309850; FBpp0301584; FBgn0026238.
DR   EnsemblMetazoa; FBtr0309851; FBpp0301585; FBgn0026238.
DR   EnsemblMetazoa; FBtr0309852; FBpp0301586; FBgn0026238.
DR   GeneID; 35478; -.
DR   KEGG; dme:Dmel_CG2944; -.
DR   UCSC; CG2944-RA; d. melanogaster.
DR   UCSC; CG2944-RB; d. melanogaster.
DR   UCSC; CG2944-RD; d. melanogaster.
DR   UCSC; CG2944-RE; d. melanogaster.
DR   UCSC; CG2944-RF; d. melanogaster.
DR   CTD; 35478; -.
DR   FlyBase; FBgn0026238; gus.
DR   VEuPathDB; VectorBase:FBgn0026238; -.
DR   eggNOG; KOG3953; Eukaryota.
DR   GeneTree; ENSGT01030000234629; -.
DR   HOGENOM; CLU_046756_0_1_1; -.
DR   InParanoid; A1Z6E0; -.
DR   OMA; SWNADDR; -.
DR   OrthoDB; 938259at2759; -.
DR   PhylomeDB; A1Z6E0; -.
DR   Reactome; R-DME-8951664; Neddylation.
DR   Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; A1Z6E0; -.
DR   BioGRID-ORCS; 35478; 0 hits in 3 CRISPR screens.
DR   EvolutionaryTrace; A1Z6E0; -.
DR   GenomeRNAi; 35478; -.
DR   PRO; PR:A1Z6E0; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0026238; Expressed in cleaving embryo and 28 other tissues.
DR   ExpressionAtlas; A1Z6E0; baseline and differential.
DR   Genevisible; A1Z6E0; DM.
DR   GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR   GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0070449; C:elongin complex; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0045495; C:pole plasm; IDA:UniProtKB.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0035017; P:cuticle pattern formation; IMP:UniProtKB.
DR   GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR   GO; GO:0007281; P:germ cell development; IMP:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0007314; P:oocyte anterior/posterior axis specification; IMP:FlyBase.
DR   GO; GO:0007280; P:pole cell migration; IMP:UniProtKB.
DR   GO; GO:0007315; P:pole plasm assembly; IMP:UniProtKB.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR   GO; GO:0007472; P:wing disc morphogenesis; IMP:UniProtKB.
DR   Gene3D; 2.60.120.920; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001496; SOCS_box.
DR   InterPro; IPR036036; SOCS_box-like_dom_sf.
DR   InterPro; IPR003877; SPRY_dom.
DR   Pfam; PF07525; SOCS_box; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00969; SOCS_box; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF158235; SSF158235; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50225; SOCS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Developmental protein; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..279
FT                   /note="Protein gustavus"
FT                   /id="PRO_0000422158"
FT   DOMAIN          36..233
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   DOMAIN          234..279
FT                   /note="SOCS box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00194"
FT   REGION          236..279
FT                   /note="Involved in binding to the Elongin BC complex"
FT                   /evidence="ECO:0000269|PubMed:16498413"
FT   MUTAGEN         131
FT                   /note="Y->A: Does not affect binding to Elongin BC complex.
FT                   Abolishes interaction with vas."
FT                   /evidence="ECO:0000269|PubMed:16498413"
FT   MUTAGEN         147
FT                   /note="G->Y: Does not affect binding to Elongin BC complex.
FT                   Abolishes interaction with vas."
FT                   /evidence="ECO:0000269|PubMed:16498413"
FT   MUTAGEN         148
FT                   /note="R->W: Does not affect binding to Elongin BC complex.
FT                   Abolishes interaction with vas."
FT                   /evidence="ECO:0000269|PubMed:16498413"
FT   MUTAGEN         187
FT                   /note="E->A: Does not affect binding to Elongin BC complex
FT                   or vas."
FT                   /evidence="ECO:0000269|PubMed:16498413"
FT   MUTAGEN         204
FT                   /note="R->S: Does not affect binding to Elongin BC complex
FT                   or vas."
FT                   /evidence="ECO:0000269|PubMed:16498413"
FT   MUTAGEN         219
FT                   /note="W->L: Does not affect binding to Elongin BC complex.
FT                   Decreases interaction with vas."
FT                   /evidence="ECO:0000269|PubMed:16498413,
FT                   ECO:0000269|PubMed:17189197, ECO:0000269|PubMed:20123973"
FT   HELIX           37..44
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   HELIX           50..55
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          57..63
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          67..70
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          73..79
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          85..92
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          97..105
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   HELIX           108..110
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          126..131
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          141..145
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   TURN            146..149
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          150..154
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   TURN            155..157
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          161..164
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          177..184
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   TURN            185..188
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          189..194
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          197..203
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          211..217
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   STRAND          223..232
FT                   /evidence="ECO:0007829|PDB:2FNJ"
FT   HELIX           239..247
FT                   /evidence="ECO:0007829|PDB:2FNJ"
SQ   SEQUENCE   279 AA;  31713 MW;  DCA657FEEA83D785 CRC64;
     MGQKISGGVK TVSRNDSQST FKPIIPRELQ ADFVKPARID ILLDMPPASR DLQLKHSWNS
     EDRSLNIFVK EDDKLTFHRH PVAQSTDCIR GKVGLTKGLH IWEIYWPTRQ RGTHAVVGVC
     TADAPLHSVG YQSLVGSTEQ SWGWDLGRNK LYHDSKNCAG VTYPAILKND EAFLVPDKFL
     VALDMDEGTL SFIVDQQYLG IAFRGLRGKK LYPIVSAVWG HCEITMRYIG GLDPEPLPLM
     DLCRRTIRQK IGRTNLEEHI QQLQLPLSMK TYLLYKNRR
 
 
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