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Database: UniProt
Entry: ELBA1_DROME
LinkDB: ELBA1_DROME
Original site: 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   24-JAN-2024, entry version 145.
DE   RecName: Full=Early boundary activity protein 1 {ECO:0000303|PubMed:23240086};
DE   AltName: Full=Blastoderm-specific gene 25A {ECO:0000303|PubMed:25561495};
GN   Name=Elba1 {ECO:0000303|PubMed:23240086, ECO:0000312|FlyBase:FBgn0000227};
GN   Synonyms=Bsg25A {ECO:0000303|PubMed:25561495};
GN   ORFNames=CG12205 {ECO:0000312|FlyBase:FBgn0000227};
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 Elba1, Elba2 and
CC       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   ComplexPortal; CPX-2439; ELBA boundary factor complex.
DR   IntAct; Q9VR17; 1.
DR   STRING; 7227.FBpp0077114; -.
DR   PaxDb; 7227-FBpp0077114; -.
DR   DNASU; 33669; -.
DR   EnsemblMetazoa; FBtr0077423; FBpp0077114; FBgn0000227.
DR   GeneID; 33669; -.
DR   KEGG; dme:Dmel_CG12205; -.
DR   UCSC; CG12205-RA; d. melanogaster.
DR   AGR; FB:FBgn0000227; -.
DR   CTD; 33669; -.
DR   FlyBase; FBgn0000227; Elba1.
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; 4265296at2759; -.
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 cell types or 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:0003714; F:transcription corepressor activity; IEA:InterPro.
DR   GO; GO:0001700; P:embryonic development via the syncytial blastoderm; IEP:FlyBase.
DR   GO; GO:0033696; P:heterochromatin boundary formation; IMP:FlyBase.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; IEA:InterPro.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:InterPro.
DR   Gene3D; 1.10.10.2590; BEN domain; 1.
DR   InterPro; IPR018379; BEN_domain.
DR   InterPro; IPR037496; BEND6-like.
DR   PANTHER; PTHR35346; BEN DOMAIN-CONTAINING PROTEIN 6; 1.
DR   PANTHER; PTHR35346:SF1; BEN DOMAIN-CONTAINING PROTEIN 6; 1.
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
//
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