BRAT_DROME
ID BRAT_DROME Reviewed; 1037 AA.
AC Q8MQJ9; A4V0U9; Q0E8P2; Q2XXZ6; Q8MR02; Q9U633; Q9U634; Q9U635; Q9U636;
AC Q9Y1W4;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Brain tumor protein;
GN Name=brat; ORFNames=CG10719;
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], TISSUE SPECIFICITY, AND MUTANTS
RP BRATTS1 AND BRATFS3.
RX PubMed=10949924; DOI=10.1038/sj.onc.1203706;
RA Arama E., Dickman D., Kimchie Z., Shearn A., Lev Z.;
RT "Mutations in the beta-propeller domain of the Drosophila brain tumor
RT (brat) protein induce neoplasm in the larval brain.";
RL Oncogene 19:3706-3716(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lukacsovich T.;
RT "Putative Drosophila transcription factor.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo, Larva, and Pupae;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-1031.
RC STRAIN=Ral1;
RX PubMed=16120803; DOI=10.1093/molbev/msi246;
RA Comeron J.M., Guthrie T.B.;
RT "Intragenic Hill-Robertson interference influences selection intensity on
RT synonymous mutations in Drosophila.";
RL Mol. Biol. Evol. 22:2519-2530(2005).
RN [7]
RP FUNCTION, INTERACTION WITH PUM AND NOS, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=11274060; DOI=10.1101/gad.870801;
RA Sonoda J., Wharton R.P.;
RT "Drosophila Brain tumor is a translational repressor.";
RL Genes Dev. 15:762-773(2001).
RN [8]
RP FUNCTION.
RX PubMed=11807032; DOI=10.1242/dev.129.2.399;
RA Frank D.J., Edgar B.A., Roth M.B.;
RT "The Drosophila melanogaster gene brain tumor negatively regulates cell
RT growth and ribosomal RNA synthesis.";
RL Development 129:399-407(2002).
RN [9]
RP FUNCTION, INTERACTION WITH MIRA, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16564014; DOI=10.1016/j.cell.2006.01.038;
RA Betschinger J., Mechtler K., Knoblich J.A.;
RT "Asymmetric segregation of the tumor suppressor brat regulates self-renewal
RT in Drosophila neural stem cells.";
RL Cell 124:1241-1253(2006).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18342578; DOI=10.1016/j.devcel.2008.03.004;
RA Bowman S.K., Rolland V., Betschinger J., Kinsey K.A., Emery G.,
RA Knoblich J.A.;
RT "The tumor suppressors Brat and Numb regulate transit-amplifying neuroblast
RT lineages in Drosophila.";
RL Dev. Cell 14:535-546(2008).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22143802; DOI=10.1073/pnas.1118595109;
RA Zhu S., Barshow S., Wildonger J., Jan L.Y., Jan Y.N.;
RT "Ets transcription factor Pointed promotes the generation of intermediate
RT neural progenitors in Drosophila larval brains.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20615-20620(2011).
RN [12]
RP FUNCTION.
RX PubMed=24550111; DOI=10.1242/dev.106534;
RA Janssens D.H., Komori H., Grbac D., Chen K., Koe C.T., Wang H., Lee C.Y.;
RT "Earmuff restricts progenitor cell potential by attenuating the competence
RT to respond to self-renewal factors.";
RL Development 141:1036-1046(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 757-1037, FUNCTION, AND
RP MUTAGENESIS OF TYR-829; ARG-847; TYR-859; ARG-875; GLU-970 AND ASP-1012.
RX PubMed=14561773; DOI=10.1101/gad.1119403;
RA Edwards T.A., Wilkinson B.D., Wharton R.P., Aggarwal A.K.;
RT "Model of the brain tumor-Pumilio translation repressor complex.";
RL Genes Dev. 17:2508-2513(2003).
CC -!- FUNCTION: A NHL-domain family protein that functions a translational
CC repressor to inhibit cell proliferation (PubMed:11274060). Plays a
CC central role in translation repression of hb mRNA by being recruited by
CC nos and pum to the Nanos Response Element (NRE), a 16 bp sequence in
CC the hb mRNA 3'-UTR (PubMed:11274060). Probably recruited by other
CC proteins to repress translation of other mRNAs in other tissues
CC (PubMed:11274060). Involved in the regulation of ribosomal RNA
CC synthesis and cell growth (PubMed:11807032). Participates in abdominal
CC segmentation and imaginal disk development (PubMed:11274060). During
CC neuroblast division, segregates asymmetrically and inhibits self-
CC renewal of one of the two daughter cells (PubMed:16564014). Together
CC with the asymmetrically segregating transcription factor prospero
CC ensures that the daughter cell will stop growing, exit the cell cycle,
CC and differentiate into neurons possibly by modulating the function of
CC dm in ganglion mother cells (GMC) (PubMed:11807032, PubMed:16564014).
CC Restricts developmental potential of type II intermediary neuronal
CC progenitor (INP) cells playing a role in proliferation and maturation
CC of the neuroblasts (PubMed:24550111, PubMed:14561773, PubMed:22143802,
CC PubMed:18342578). {ECO:0000269|PubMed:11274060,
CC ECO:0000269|PubMed:11807032, ECO:0000269|PubMed:14561773,
CC ECO:0000269|PubMed:16564014, ECO:0000269|PubMed:18342578,
CC ECO:0000269|PubMed:22143802, ECO:0000269|PubMed:24550111}.
CC -!- SUBUNIT: Interacts with nos and pum (PubMed:11274060). Acts via the
CC formation of a quaternary complex composed of pum, nos, brat and the
CC 3'-UTR mRNA of hb (PubMed:11274060). Not recruited by nos and pum to
CC cyclin B 3'-UTR mRNA (PubMed:11274060). Might interact with mira; the
CC interaction seems to be important for brat localization during mitosis
CC (PubMed:16564014). {ECO:0000269|PubMed:11274060,
CC ECO:0000269|PubMed:16564014}.
CC -!- INTERACTION:
CC Q8MQJ9; Q27IR0: AGO1; NbExp=4; IntAct=EBI-414123, EBI-15707124;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11274060,
CC ECO:0000269|PubMed:16564014}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:16564014, ECO:0000269|PubMed:18342578}. Note=In
CC embryonic and larval neuroblasts, colocalizes with mira throughout
CC mitosis using it as an adapter to segregate into one of the two
CC daughter cells during asymmetric cell division. Accumulates at the
CC apical cell cortex in prophase, forms a basal crescent in metaphase,
CC and segregates into the ganglion mother cell (GMC). It is cortical in
CC telophase but becomes cytoplasmic in interphase after mira is degraded.
CC {ECO:0000269|PubMed:16564014, ECO:0000269|PubMed:18342578}.
CC -!- TISSUE SPECIFICITY: Expressed during embryogenesis, mainly in nervous
CC tissues. Expressed in the embryonic central and peripheral nervous
CC systems including the embryonic brain. In third instar larva it is
CC expressed in the larval central nervous system including the brain and
CC the ventral ganglion, in two glands (the ring gland and the salivary
CC gland, and in parts of the foregut) the gastric caeca and the
CC proventriculus. {ECO:0000269|PubMed:10949924}.
CC -!- DOMAIN: The NHL repeats form six-bladed beta-propeller that mediate the
CC interaction with the pumilio repeats of pum, and are essential for
CC translational effector function. {ECO:0000269|PubMed:11274060}.
CC -!- DISRUPTION PHENOTYPE: In larval brain, results in deregulated cell
CC cycle and defective differentiation of immature intermediate neuroblast
CC progenitors ultimately leading to overgrowth and proliferation
CC (PubMed:16564014, PubMed:18342578). RNAi-mediated knockdown in the
CC larval brain results in overproliferation of type II neuroblast cells
CC on the dorsal side of the larval brains but had no effect in the type I
CC neuroblast lineage in the ventral nerve cord (PubMed:22143802,
CC PubMed:18342578). {ECO:0000269|PubMed:16564014,
CC ECO:0000269|PubMed:18342578, ECO:0000269|PubMed:22143802}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM76183.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF119332; AAF03086.1; -; mRNA.
DR EMBL; AF195870; AAF13926.1; -; Genomic_DNA.
DR EMBL; AF195871; AAF13927.1; -; Genomic_DNA.
DR EMBL; AF195872; AAF13928.1; -; Genomic_DNA.
DR EMBL; AF195873; AAF13929.1; -; Genomic_DNA.
DR EMBL; AB022432; BAA82071.1; -; mRNA.
DR EMBL; AE014134; AAN11027.1; -; Genomic_DNA.
DR EMBL; AE014134; AAS64719.1; -; Genomic_DNA.
DR EMBL; AY122207; AAM52719.1; -; mRNA.
DR EMBL; AY129441; AAM76183.1; ALT_INIT; mRNA.
DR EMBL; DQ138866; ABA86472.1; -; Genomic_DNA.
DR RefSeq; NP_001286083.1; NM_001299154.1.
DR RefSeq; NP_476945.1; NM_057597.4.
DR RefSeq; NP_599129.1; NM_134302.2.
DR RefSeq; NP_995726.1; NM_206004.2.
DR PDB; 1Q7F; X-ray; 1.95 A; A/B=756-1037.
DR PDB; 4ZLR; X-ray; 2.30 A; A/B=756-1037.
DR PDB; 5EX7; X-ray; 2.60 A; A=758-1037.
DR PDB; 6J9R; X-ray; 2.50 A; A/B=376-511.
DR PDBsum; 1Q7F; -.
DR PDBsum; 4ZLR; -.
DR PDBsum; 5EX7; -.
DR PDBsum; 6J9R; -.
DR AlphaFoldDB; Q8MQJ9; -.
DR SASBDB; Q8MQJ9; -.
DR SMR; Q8MQJ9; -.
DR BioGRID; 61181; 57.
DR DIP; DIP-37857N; -.
DR IntAct; Q8MQJ9; 4.
DR MINT; Q8MQJ9; -.
DR STRING; 7227.FBpp0293081; -.
DR PaxDb; Q8MQJ9; -.
DR DNASU; 35197; -.
DR EnsemblMetazoa; FBtr0081158; FBpp0080702; FBgn0010300.
DR EnsemblMetazoa; FBtr0081159; FBpp0080703; FBgn0010300.
DR EnsemblMetazoa; FBtr0081160; FBpp0089239; FBgn0010300.
DR EnsemblMetazoa; FBtr0344846; FBpp0311161; FBgn0010300.
DR GeneID; 35197; -.
DR KEGG; dme:Dmel_CG10719; -.
DR UCSC; CG10719-RC; d. melanogaster.
DR CTD; 35197; -.
DR FlyBase; FBgn0010300; brat.
DR VEuPathDB; VectorBase:FBgn0010300; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000170685; -.
DR HOGENOM; CLU_007697_0_0_1; -.
DR InParanoid; Q8MQJ9; -.
DR OMA; IYRYVQV; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q8MQJ9; -.
DR SignaLink; Q8MQJ9; -.
DR BioGRID-ORCS; 35197; 0 hits in 3 CRISPR screens.
DR ChiTaRS; brat; fly.
DR EvolutionaryTrace; Q8MQJ9; -.
DR GenomeRNAi; 35197; -.
DR PRO; PR:Q8MQJ9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0010300; Expressed in cleaving embryo and 67 other tissues.
DR ExpressionAtlas; Q8MQJ9; baseline and differential.
DR Genevisible; Q8MQJ9; DM.
DR GO; GO:0045179; C:apical cortex; IDA:FlyBase.
DR GO; GO:0045180; C:basal cortex; IDA:FlyBase.
DR GO; GO:0099738; C:cell cortex region; IMP:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IMP:FlyBase.
DR GO; GO:0045182; F:translation regulator activity; TAS:FlyBase.
DR GO; GO:0030371; F:translation repressor activity; IMP:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008356; P:asymmetric cell division; IMP:FlyBase.
DR GO; GO:0055060; P:asymmetric neuroblast division resulting in ganglion mother cell formation; IMP:FlyBase.
DR GO; GO:0007420; P:brain development; IMP:FlyBase.
DR GO; GO:0007402; P:ganglion mother cell fate determination; IMP:FlyBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IMP:FlyBase.
DR GO; GO:0014019; P:neuroblast development; IMP:UniProtKB.
DR GO; GO:0014016; P:neuroblast differentiation; IMP:FlyBase.
DR GO; GO:0007400; P:neuroblast fate determination; IMP:FlyBase.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; HMP:FlyBase.
DR GO; GO:1902692; P:regulation of neuroblast proliferation; IGI:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:FlyBase.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IMP:FlyBase.
DR GO; GO:0006417; P:regulation of translation; TAS:FlyBase.
DR GO; GO:0009303; P:rRNA transcription; IMP:UniProtKB.
DR GO; GO:0035282; P:segmentation; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR000315; Znf_B-box.
DR Pfam; PF01436; NHL; 4.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 2.
DR PROSITE; PS51125; NHL; 5.
DR PROSITE; PS50119; ZF_BBOX; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Reference proteome; Repeat;
KW Repressor; Translation regulation; Zinc; Zinc-finger.
FT CHAIN 1..1037
FT /note="Brain tumor protein"
FT /id="PRO_0000220368"
FT REPEAT 767..810
FT /note="NHL 1"
FT REPEAT 814..859
FT /note="NHL 2"
FT REPEAT 860..901
FT /note="NHL 3"
FT REPEAT 902..944
FT /note="NHL 4"
FT REPEAT 945..988
FT /note="NHL 5"
FT ZN_FING 174..222
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 323..366
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 29..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..598
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MUTAGEN 802
FT /note="H->L: In bratfs3; induces production of tumor-like
FT neoplasms in the larval brain. Disrupts interaction with
FT nos and pum."
FT MUTAGEN 829
FT /note="Y->A: Disrupts recruitment by pum."
FT /evidence="ECO:0000269|PubMed:14561773"
FT MUTAGEN 847
FT /note="R->A: Disrupts recruitment by pum."
FT /evidence="ECO:0000269|PubMed:14561773"
FT MUTAGEN 859
FT /note="Y->A: Does not affect recruitment by pum."
FT /evidence="ECO:0000269|PubMed:14561773"
FT MUTAGEN 860
FT /note="G->D: In bratts1; induces production of tumor-like
FT neoplasms in the larval brain. Disrupts interaction with
FT nos and pum."
FT MUTAGEN 875
FT /note="R->A: Disrupts recruitment by pum."
FT /evidence="ECO:0000269|PubMed:14561773"
FT MUTAGEN 970
FT /note="E->A: Does not affect recruitment by pum."
FT /evidence="ECO:0000269|PubMed:14561773"
FT MUTAGEN 1012
FT /note="D->A: Does not affect recruitment by pum."
FT /evidence="ECO:0000269|PubMed:14561773"
FT CONFLICT 591
FT /note="H -> Y (in Ref. 6; ABA86472)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="G -> S (in Ref. 1; AAF13928/AAF13929)"
FT /evidence="ECO:0000305"
FT HELIX 383..402
FT /evidence="ECO:0007829|PDB:6J9R"
FT HELIX 405..479
FT /evidence="ECO:0007829|PDB:6J9R"
FT HELIX 485..503
FT /evidence="ECO:0007829|PDB:6J9R"
FT STRAND 762..764
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 766..770
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 773..776
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:5EX7"
FT STRAND 783..788
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 794..798
FT /evidence="ECO:0007829|PDB:1Q7F"
FT HELIX 799..801
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 803..807
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 813..817
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 820..823
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 827..835
FT /evidence="ECO:0007829|PDB:1Q7F"
FT TURN 837..839
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 842..846
FT /evidence="ECO:0007829|PDB:1Q7F"
FT HELIX 848..850
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 852..856
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 862..866
FT /evidence="ECO:0007829|PDB:1Q7F"
FT TURN 868..870
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 874..879
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 885..889
FT /evidence="ECO:0007829|PDB:1Q7F"
FT TURN 890..893
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 894..898
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 904..909
FT /evidence="ECO:0007829|PDB:1Q7F"
FT TURN 911..913
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 915..922
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 924..932
FT /evidence="ECO:0007829|PDB:1Q7F"
FT HELIX 933..935
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 937..942
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 947..952
FT /evidence="ECO:0007829|PDB:1Q7F"
FT TURN 954..956
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 959..965
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 971..975
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 977..979
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 981..985
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 991..999
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 1004..1010
FT /evidence="ECO:0007829|PDB:1Q7F"
FT TURN 1011..1013
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 1014..1019
FT /evidence="ECO:0007829|PDB:1Q7F"
FT TURN 1020..1022
FT /evidence="ECO:0007829|PDB:1Q7F"
FT STRAND 1023..1028
FT /evidence="ECO:0007829|PDB:1Q7F"
SQ SEQUENCE 1037 AA; 110366 MW; 6B829CD924139DDF CRC64;
MASSPTPSLD SMRGGANSIE SYEHAGYLSD SPLTLSGSSP PASDSAICSD EYTGGSSVKS
RSEVTVINGH HPISASVSSS SSASSSSCSS SSSSSSSSSS SSSSTSGLSG CGSTSSSVIS
ANNVASSNGP GVIGSNLQSS NNGGNSGISS LVVGAGKGSN SSSNSSSSNT SANGSPPRCT
ACKSKCSDAV AKCFECQSYL CANCVTAHEF MHCFNGHNVC LIKGFEASTT GTPLSVGSPS
NNPASNEFKY ASSLTMMLQQ QQQLDSQQQQ QQQQLLPAQP MSQLSKIVLA AAAQANSQEQ
QREDSIYGSL HPQQQQQQQQ QQQRQLFCPR HKQELLKFSC RTCCILVCKE CIVLEHSTGL
HELENVQSPG MTTSTGSTAN ESALQTLLAD MRGKIGEIVG IAGNSDQNLT KVKLQYQKAH
NELNETHQFF ASMLDERKTE LLKELETLYT AKVNSNNSWQ QRSRDLIDKG LATCEAVERS
PAPPSSLLTE ALLLRKSLEQ QLQTGIQEMQ LPFEIEFMSN YQSIQAGVRN TFGYIRANSS
DGGPTGMSLT SNGHGKQPPI ARPTQSASNS SASSAGSGHH GHHQQSHHHG HHNHHQTAHH
QQLQAQSSLH GLGLGLSGAS LLDSSSSAGG AVGAFSNGGL LLGGRDRNAL AVEQHFGELM
PKRGGGGYTG SNGSATSAVA HYNPYEKWSN GGSDNLFSSV TSGVSGSSAV ADAFASLSAV
GGSVVSGAGA GGSTVSSESL LDLTNKLLSA TIYPPKSQIK RQKMIYHCKF GEFGVMEGQF
TEPSGVAVNA QNDIIVADTN NHRIQIFDKE GRFKFQFGEC GKRDSQLLYP NRVAVVRNSG
DIIVTERSPT HQIQIYNQYG QFVRKFGATI LQHPRGVTVD NKGRIIVVEC KVMRVIIFDQ
NGNVLHKFGC SKHLEFPNGV VVNDKQEIFI SDNRAHCVKV FNYEGQYLRQ IGGEGITNYP
IGVGINSNGE ILIADNHNNF NLTIFTQDGQ LISALESKVK HAQCFDVALM DDGSVVLASK
DYRLYIYRYV QLAPVGM
