NC2B_DROME
ID NC2B_DROME Reviewed; 183 AA.
AC Q9VJQ5; Q2XYD4; Q9NKA2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein Dr1;
DE AltName: Full=Down-regulator of transcription 1;
DE AltName: Full=Negative cofactor 2-beta;
DE Short=NC2-beta;
DE AltName: Full=dNC2;
GN Name=NC2beta; Synonyms=Dr1; ORFNames=CG4185;
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], PROTEIN SEQUENCE OF 72-84 AND 114-133,
RP FUNCTION, INTERACTION WITH NC2-ALPHA, AND SUBCELLULAR LOCATION.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=11062130; DOI=10.1126/science.290.5493.982;
RA Willy P.J., Kobayashi R., Kadonaga J.T.;
RT "A basal transcription factor that activates or represses transcription.";
RL Science 290:982-985(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10471707; DOI=10.1093/genetics/153.1.179;
RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T.,
RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A.,
RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.,
RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K.,
RA Celniker S.E., Rubin G.M.;
RT "An exploration of the sequence of a 2.9-Mb region of the genome of
RT Drosophila melanogaster: the Adh region.";
RL Genetics 153:179-219(1999).
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=Head;
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 9-177.
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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, IDENTIFICATION IN
RP THE ATAC COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=18327268; DOI=10.1038/nsmb.1397;
RA Suganuma T., Gutierrez J.L., Li B., Florens L., Swanson S.K.,
RA Washburn M.P., Abmayr S.M., Workman J.L.;
RT "ATAC is a double histone acetyltransferase complex that stimulates
RT nucleosome sliding.";
RL Nat. Struct. Mol. Biol. 15:364-372(2008).
CC -!- FUNCTION: Bifunctional basic transcription factor. Activates
CC transcription of DPE (Downstream Promoter Element) containing promoters
CC while repressing transcription of promoters which contain TATA elements
CC (PubMed:11062130). Together with Chrac-14, promotes nucleosome sliding
CC of ATP-dependent nucelosome remodeling complexes (PubMed:18327268).
CC {ECO:0000269|PubMed:11062130, ECO:0000269|PubMed:18327268}.
CC -!- SUBUNIT: Component of the Ada2a-containing (ATAC) complex composed of
CC at least Ada2a, Atac1, Hcf, Ada3, Gcn5, Mocs2B, Charac-14, Atac3,
CC Atac2, NC2beta and wds (PubMed:18327268). Homodimer (PubMed:18327268).
CC Interacts with NC2-alpha/Drap1 to form the dNC2 complex
CC (PubMed:11062130). {ECO:0000269|PubMed:11062130,
CC ECO:0000269|PubMed:18327268}.
CC -!- INTERACTION:
CC Q9VJQ5; Q9GSP1: NC2alpha; NbExp=4; IntAct=EBI-176193, EBI-22062696;
CC Q9VJQ5; P49906: Taf11; NbExp=3; IntAct=EBI-176193, EBI-187533;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11062130,
CC ECO:0000269|PubMed:18327268}.
CC -!- SIMILARITY: Belongs to the NC2 beta/DR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28265.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AF302257; AAG15388.1; -; mRNA.
DR EMBL; AE014134; AAF53428.1; -; Genomic_DNA.
DR EMBL; AY060717; AAL28265.2; ALT_SEQ; mRNA.
DR EMBL; DQ138728; ABA86334.1; -; Genomic_DNA.
DR RefSeq; NP_609736.1; NM_135892.4.
DR AlphaFoldDB; Q9VJQ5; -.
DR SMR; Q9VJQ5; -.
DR BioGRID; 60894; 25.
DR IntAct; Q9VJQ5; 14.
DR STRING; 7227.FBpp0080256; -.
DR PaxDb; Q9VJQ5; -.
DR PRIDE; Q9VJQ5; -.
DR DNASU; 34875; -.
DR EnsemblMetazoa; FBtr0080695; FBpp0080256; FBgn0028926.
DR GeneID; 34875; -.
DR KEGG; dme:Dmel_CG4185; -.
DR UCSC; CG4185-RA; d. melanogaster.
DR CTD; 34875; -.
DR FlyBase; FBgn0028926; NC2beta.
DR VEuPathDB; VectorBase:FBgn0028926; -.
DR eggNOG; KOG0871; Eukaryota.
DR GeneTree; ENSGT00550000075010; -.
DR HOGENOM; CLU_066247_11_1_1; -.
DR InParanoid; Q9VJQ5; -.
DR OMA; KTIAPDH; -.
DR OrthoDB; 1465912at2759; -.
DR PhylomeDB; Q9VJQ5; -.
DR SignaLink; Q9VJQ5; -.
DR BioGRID-ORCS; 34875; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34875; -.
DR PRO; PR:Q9VJQ5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0028926; Expressed in oviduct (Drosophila) and 33 other tissues.
DR Genevisible; Q9VJQ5; DM.
DR GO; GO:0140672; C:ATAC complex; IDA:FlyBase.
DR GO; GO:0017054; C:negative cofactor 2 complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0140223; F:general transcription initiation factor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR GO; GO:0016573; P:histone acetylation; IDA:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR042225; Ncb2.
DR PANTHER; PTHR46138; PTHR46138; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Activator; Direct protein sequencing; DNA-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..183
FT /note="Protein Dr1"
FT /id="PRO_0000096752"
FT DOMAIN 19..82
FT /note="Histone-fold"
FT /evidence="ECO:0000255"
FT REGION 92..183
FT /note="Repression of TATA-containing promoters"
FT REGION 155..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 183 AA; 20914 MW; BE7B25679CE02F7C CRC64;
MSNPQEELLP PSAEDDELTL PRASINKIIK ELVPTVRVAN ESRELILNCC SEFIHLISSE
ANEVCNMRNK KTINAEHVLE ALERLGFHDY KQEAEAVLHD CKEVAAKRRR QSTRLENLGI
PEEELLRQQQ ELFAKAREEQ AREEQQQWMS MQAAAMVQRP PLADGSVASK PSEDDDDDDD
DDY
