BRC4_DROME
ID BRC4_DROME Reviewed; 880 AA.
AC Q24206; O46064; Q9W575;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Broad-complex core protein isoform 6;
GN Name=br; Synonyms=Br-C; ORFNames=CG11491;
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], DEVELOPMENTAL STAGE, AND CHARACTERIZATION OF
RP ISOFORMS.
RC TISSUE=Imaginal disk, and Larva;
RX PubMed=8660872; DOI=10.1006/dbio.1996.0140;
RA Bayer C.A., Holley B., Fristrom J.W.;
RT "A switch in broad-complex zinc-finger isoform expression is regulated
RT posttranscriptionally during the metamorphosis of Drosophila imaginal
RT discs.";
RL Dev. Biol. 177:1-14(1996).
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.
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 GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC STRAIN=Berkeley; TISSUE=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 CHARACTERIZATION OF ISOFORMS, AND MUTAGENESIS.
RX PubMed=9242423; DOI=10.1006/dbio.1997.8620;
RA Bayer C.A., von Kalm L., Fristrom J.W.;
RT "Relationships between protein isoforms and genetic functions demonstrate
RT functional redundancy at the Broad-Complex during Drosophila
RT metamorphosis.";
RL Dev. Biol. 187:267-282(1997).
CC -!- FUNCTION: Broad-complex proteins are required for puffing and
CC transcription of salivary gland late genes during metamorphosis.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=6; Synonyms=BRCORE-Z4;
CC IsoId=Q24206-1; Sequence=Displayed;
CC Name=1; Synonyms=BRCORE-TNT1-Q1-Z1;
CC IsoId=Q01295-1; Sequence=External;
CC Name=2; Synonyms=BRCORE-Q1-Z1;
CC IsoId=Q01295-2; Sequence=External;
CC Name=3; Synonyms=BRCORE-Q2-Z1;
CC IsoId=Q01295-3; Sequence=External;
CC Name=4; Synonyms=BRCORE-Z2;
CC IsoId=Q01295-4; Sequence=External;
CC Name=5; Synonyms=BRCORE-NS-Z3;
CC IsoId=Q01295-5; Sequence=External;
CC -!- DEVELOPMENTAL STAGE: Accumulates to a high level at the beginning of
CC the ecdysone response, during the metamorphosis of imaginal disks in
CC puff stage 1, and abruptly disappears after several hours.
CC {ECO:0000269|PubMed:8660872}.
CC -!- INDUCTION: Induced as a primary response to 20-hydroxyecdysone in third
CC instar larval imaginal disks.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB09760.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U51585; AAB09760.1; ALT_FRAME; mRNA.
DR EMBL; AE014298; AAF45647.1; -; Genomic_DNA.
DR EMBL; AL009146; CAA15627.1; -; Genomic_DNA.
DR EMBL; AY069756; AAL39901.1; -; mRNA.
DR RefSeq; NP_001138144.1; NM_001144672.3. [Q24206-1]
DR RefSeq; NP_001259134.1; NM_001272205.1. [Q24206-1]
DR RefSeq; NP_726751.2; NM_166895.2. [Q24206-1]
DR RefSeq; NP_726752.1; NM_166896.3. [Q24206-1]
DR RefSeq; NP_726753.1; NM_166897.2. [Q24206-1]
DR AlphaFoldDB; Q24206; -.
DR SMR; Q24206; -.
DR BioGRID; 69091; 41.
DR DIP; DIP-18557N; -.
DR IntAct; Q24206; 1.
DR STRING; 7227.FBpp0289656; -.
DR PaxDb; Q24206; -.
DR PRIDE; Q24206; -.
DR DNASU; 44505; -.
DR EnsemblMetazoa; FBtr0070261; FBpp0070251; FBgn0283451. [Q24206-1]
DR EnsemblMetazoa; FBtr0070263; FBpp0070253; FBgn0283451. [Q24206-1]
DR EnsemblMetazoa; FBtr0300427; FBpp0289656; FBgn0283451. [Q24206-1]
DR EnsemblMetazoa; FBtr0300428; FBpp0289657; FBgn0283451. [Q24206-1]
DR EnsemblMetazoa; FBtr0332293; FBpp0304572; FBgn0283451. [Q24206-1]
DR GeneID; 44505; -.
DR KEGG; dme:Dmel_CG11491; -.
DR CTD; 103946; -.
DR FlyBase; FBgn0283451; br.
DR VEuPathDB; VectorBase:FBgn0283451; -.
DR eggNOG; ENOG502QUP1; Eukaryota.
DR HOGENOM; CLU_011721_0_0_1; -.
DR InParanoid; Q24206; -.
DR SignaLink; Q24206; -.
DR BioGRID-ORCS; 44505; 1 hit in 1 CRISPR screen.
DR ChiTaRS; br; fly.
DR GenomeRNAi; 44505; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0283451; Expressed in wing disc and 23 other tissues.
DR ExpressionAtlas; Q24206; baseline and differential.
DR Genevisible; Q24206; DM.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0006914; P:autophagy; IMP:FlyBase.
DR GO; GO:0071390; P:cellular response to ecdysone; IDA:FlyBase.
DR GO; GO:0001752; P:compound eye photoreceptor fate commitment; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007562; P:eclosion; IEP:FlyBase.
DR GO; GO:0042332; P:gravitaxis; IMP:FlyBase.
DR GO; GO:0048808; P:male genitalia morphogenesis; IMP:FlyBase.
DR GO; GO:0055001; P:muscle cell development; IGI:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0007458; P:progression of morphogenetic furrow involved in compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0040034; P:regulation of development, heterochronic; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035075; P:response to ecdysone; IMP:FlyBase.
DR GO; GO:0009608; P:response to symbiont; IMP:FlyBase.
DR GO; GO:0035070; P:salivary gland histolysis; IMP:FlyBase.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..880
FT /note="Broad-complex core protein isoform 6"
FT /id="PRO_0000047070"
FT DOMAIN 32..97
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 710..733
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 740..763
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 135..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 436
FT /note="G -> D (in Ref. 1; AAB09760)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="A -> R (in Ref. 1; AAB09760)"
FT /evidence="ECO:0000305"
FT CONFLICT 661..662
FT /note="AV -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 722..723
FT /note="KL -> NV (in Ref. 1; AAB09760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 880 AA; 92305 MW; 500C0A4A38663AAF CRC64;
MDDTQHFCLR WNNYQSSITS AFENLRDDEA FVDVTLACEG RSIKAHRVVL SACSPYFREL
LKSTPCKHPV ILLQDVNFMD LHALVEFIYH GEVNVHQKSL QSFLKTAEVL RVSGLTQQQA
EDTHSHLAQI QNLANSGGRT PLNTHTQSLP HPHHGSLHDD GGSSTLFSRQ GAGSPPPTAV
PSLPSHINNQ LLKRMAMMHR SSAAAAAEET SHAFKRLRGS DNSLPLSGAV GSGSNNNSPD
LPPLHARSAS PQQTPADFST IKHHNNNNTP PLKEEKRNGP TGNGNSGNGN GNGNGASNGN
GISISDKLGS LTPSPLARAG ADDVKSEPMD MVCSNNNANA NDEHSNDSTG EHDANRSSSG
DGGKGSLSSG NDEEIGDGLA SHHAAPQFIM SPAENKMFHA AAFNFPNIDP SALLGLNTQL
QQSGDLAVSP QGGSTGSLLS GVIVPGGSGG TPSNSSSNNN NNNSNNQQQK VEQQSSPHQL
LQQQHHSTPH TNSPQLKQEQ PKSGGGSCKS SDLHIAAGSE RSLSRSSQGM PDAGGHSATP
SPTAAYHKRE RERERERERE RERERERSLD HERDLERPGG TGSPPPPPPS HHSHFGQHPL
SLLPSHHQLH ATHHELSAAA AHHAHAHAHA AHAHALARAG SPMEHHHLLH HRRASLSPSG
AVSSASGAGG RGGGAGGPGG PGGSLLSSVR AQDVAQANRL LLPLPLNACH RCDVCGKLLS
TKLTLKRHKE QQHLQPLNNA VCNLCHKVFR TLNSLNNHKS IYHRRQKNHH SYFHHGAGVS
QAGSPGSRLH QSLSSLSAAA AAANNSVNVG GGSVGGAGGN AVAAAAAAAA AAAELLLSPI
VGAAAVAGGT ASSTLQLAAA HQQQQQQSSP GIVKPCMDFL