ELBA1_DROME
ID ELBA1_DROME Reviewed; 363 AA.
AC Q9VR17; O01400; Q8SXI9;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Early boundary activity protein 1;
DE AltName: Full=Blastoderm-specific gene 25A;
GN Name=Bsg25A; Synonyms=Elba1; ORFNames=CG12205;
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 [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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, DOMAIN BEN, AND DNA-BINDING.
RX PubMed=23240086; DOI=10.7554/elife.00171;
RA Aoki T., Sarkeshik A., Yates J., Schedl P.;
RT "Elba, a novel developmentally regulated chromatin boundary factor is a
RT hetero-tripartite DNA binding complex.";
RL Elife 1:E00171-E00171(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 250-358, FUNCTION, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, DNA-BINDING, AND DOMAIN BEN.
RX PubMed=25561495; DOI=10.1101/gad.252122.114;
RA Dai Q., Ren A., Westholm J.O., Duan H., Patel D.J., Lai E.C.;
RT "Common and distinct DNA-binding and regulatory activities of the BEN-solo
RT transcription factor family.";
RL Genes Dev. 29:48-62(2015).
CC -!- FUNCTION: The heterotrimeric Elba complex is required for chromatin
CC domain boundary function during early embryogenesis. It binds to a 8-bp
CC sequence 5'-CCAATAAG-3' in the Fab-7 insulator or boundary element in
CC the bithorax complex and contributes to its insulator or boundary
CC activity (PubMed:23240086). Elba1 may act as a transcriptional
CC repressor and binds the palindromic sequence 5'-CCAATTGG-3' to mediate
CC transcriptional repression (PubMed:25561495).
CC {ECO:0000269|PubMed:23240086, ECO:0000269|PubMed:25561495}.
CC -!- SUBUNIT: The heterotrimeric Elba complex consists of Bsg25A/Elba1,
CC Elba2 and Elba3. {ECO:0000269|PubMed:23240086}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23240086,
CC ECO:0000269|PubMed:25561495}.
CC -!- DEVELOPMENTAL STAGE: Expression is developmentally restricted, peaks at
CC the blastoderm stage (2-4 hours) and then disappears (at protein
CC level). {ECO:0000269|PubMed:23240086, ECO:0000269|PubMed:25561495}.
CC -!- DOMAIN: The BEN domain mediates DNA-binding.
CC {ECO:0000269|PubMed:23240086, ECO:0000269|PubMed:25561495}.
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DR EMBL; AE014134; AAF50991.2; -; Genomic_DNA.
DR EMBL; AY089611; AAL90349.1; -; mRNA.
DR RefSeq; NP_523472.2; NM_078748.3.
DR PDB; 4X0G; X-ray; 3.21 A; A/B/C/D=250-358.
DR PDBsum; 4X0G; -.
DR AlphaFoldDB; Q9VR17; -.
DR SMR; Q9VR17; -.
DR IntAct; Q9VR17; 1.
DR STRING; 7227.FBpp0077114; -.
DR PaxDb; Q9VR17; -.
DR DNASU; 33669; -.
DR EnsemblMetazoa; FBtr0077423; FBpp0077114; FBgn0000227.
DR GeneID; 33669; -.
DR KEGG; dme:Dmel_CG12205; -.
DR UCSC; CG12205-RA; d. melanogaster.
DR CTD; 33669; -.
DR FlyBase; FBgn0000227; Bsg25A.
DR VEuPathDB; VectorBase:FBgn0000227; -.
DR eggNOG; ENOG502TBXG; Eukaryota.
DR GeneTree; ENSGT00530000069528; -.
DR HOGENOM; CLU_750683_0_0_1; -.
DR InParanoid; Q9VR17; -.
DR OMA; EHNTSTP; -.
DR OrthoDB; 983061at2759; -.
DR PhylomeDB; Q9VR17; -.
DR BioGRID-ORCS; 33669; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33669; -.
DR PRO; PR:Q9VR17; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000227; Expressed in anlage in statu nascendi and 8 other tissues.
DR ExpressionAtlas; Q9VR17; baseline and differential.
DR Genevisible; Q9VR17; DM.
DR GO; GO:0005677; C:chromatin silencing complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043035; F:chromatin insulator sequence binding; IDA:FlyBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001700; P:embryonic development via the syncytial blastoderm; IEP:FlyBase.
DR GO; GO:0033696; P:heterochromatin boundary formation; IMP:FlyBase.
DR InterPro; IPR018379; BEN_domain.
DR Pfam; PF10523; BEN; 1.
DR SMART; SM01025; BEN; 1.
DR PROSITE; PS51457; BEN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..363
FT /note="Early boundary activity protein 1"
FT /id="PRO_0000434579"
FT DOMAIN 255..354
FT /note="BEN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00784"
FT REGION 155..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:4X0G"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:4X0G"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:4X0G"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:4X0G"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:4X0G"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:4X0G"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:4X0G"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:4X0G"
FT HELIX 318..330
FT /evidence="ECO:0007829|PDB:4X0G"
FT HELIX 336..356
FT /evidence="ECO:0007829|PDB:4X0G"
SQ SEQUENCE 363 AA; 41583 MW; D265C944DDD2CE74 CRC64;
MINRRQRLEF ALTLLPYDPE TVQLSETQKK VEAIIARLRT DDSFTEEESD DCKVRRIQDA
NEFADSAMRH IEMSDSGKLS TLETLTLAAE KLLRTQRSPD QDFDDMVQDV EYSQLMRNTI
QAVNEARLKL LQQWERSKRK ALDLLTIEIE KVQEMDQEPE HKQSHEQDQD QEQSSEPFNA
FRDGADEHNT STPKTNDEDL GLDDDDEDYV PGGEETMGNK RKRIKKPVTS TPNAKRRCPG
FEFDLDGESP MVTIGPNGTE VSRISLSAIN WDMTGPSITR KLLCEIFDRD TLAHHTLSGK
PSPAFRDCAR PSKQQLDPLK VADLVYLMTN SLDMTPREVR TAITTKCADE NKMLRSRMQR
KSK