CTBP_DROME
ID CTBP_DROME Reviewed; 476 AA.
AC O46036; O61283; Q59DX5; Q95SQ8; Q9VG02;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=C-terminal-binding protein;
DE Short=CtBP protein;
DE AltName: Full=dCtBP;
GN Name=CtBP; ORFNames=CG7583;
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] (ISOFORM A), FUNCTION, INTERACTION WITH H AND
RP HLHM-DELTA, DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
RC TISSUE=Embryo;
RX PubMed=9524128; DOI=10.1093/emboj/17.7.2067;
RA Poortinga G., Watanabe M., Parkhurst S.M.;
RT "Drosophila CtBP: a Hairy-interacting protein required for embryonic
RT segmentation and hairy-mediated transcriptional repression.";
RL EMBO J. 17:2067-2078(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
RX PubMed=9525852; DOI=10.1126/science.280.5360.101;
RA Nibu Y., Zhang H., Levine M.;
RT "Interaction of short-range repressors with Drosophila CtBP in the
RT embryo.";
RL Science 280:101-104(1998).
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] (ISOFORM A), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 319-476 (ISOFORM E).
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 SEQUENCE REVISION.
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Corepressor targeting diverse transcription regulators.
CC Hairy-interacting protein required for embryonic segmentation and
CC hairy-mediated transcriptional repression. {ECO:0000269|PubMed:9524128,
CC ECO:0000269|PubMed:9525852}.
CC -!- SUBUNIT: Homodimer. Interacts with hairy (h), knirps (kni), snail
CC (sna), and Enhancer of split m-delta (HLHm-delta). Complex may be
CC involved in transcriptional repression. Interacts also with adenovirus
CC E1A protein. {ECO:0000269|PubMed:9524128}.
CC -!- INTERACTION:
CC O46036; Q9XTN4: brk; NbExp=3; IntAct=EBI-159330, EBI-159245;
CC O46036; O46036: CtBP; NbExp=3; IntAct=EBI-159330, EBI-159330;
CC O46036; P14003: h; NbExp=4; IntAct=EBI-159330, EBI-123011;
CC O46036; P10734: kni; NbExp=5; IntAct=EBI-159330, EBI-170297;
CC O46036; P08044: sna; NbExp=4; IntAct=EBI-159330, EBI-152305;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A number of isoforms are produced.;
CC Name=E;
CC IsoId=O46036-1; Sequence=Displayed;
CC Name=A; Synonyms=B;
CC IsoId=O46036-2; Sequence=VSP_011813, VSP_011814;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Zygotic
CC expression is highest in pupae. {ECO:0000269|PubMed:9524128}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AJ224690; CAA12074.1; -; mRNA.
DR EMBL; AB011840; BAA25287.1; -; mRNA.
DR EMBL; AE014297; AAF54891.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52947.1; -; Genomic_DNA.
DR EMBL; AY060646; AAL28194.2; -; mRNA.
DR EMBL; AY069170; AAL39315.1; -; mRNA.
DR RefSeq; NP_001014617.1; NM_001014617.2. [O46036-1]
DR RefSeq; NP_001262520.1; NM_001275591.1.
DR RefSeq; NP_524336.2; NM_079612.3. [O46036-2]
DR RefSeq; NP_731762.1; NM_169490.2. [O46036-2]
DR RefSeq; NP_731763.1; NM_169491.2. [O46036-2]
DR RefSeq; NP_731764.1; NM_169492.2. [O46036-2]
DR AlphaFoldDB; O46036; -.
DR SMR; O46036; -.
DR BioGRID; 66690; 96.
DR DIP; DIP-17268N; -.
DR IntAct; O46036; 35.
DR MINT; O46036; -.
DR STRING; 7227.FBpp0099514; -.
DR PaxDb; O46036; -.
DR PRIDE; O46036; -.
DR DNASU; 41602; -.
DR EnsemblMetazoa; FBtr0082699; FBpp0082167; FBgn0020496. [O46036-2]
DR EnsemblMetazoa; FBtr0082700; FBpp0082168; FBgn0020496. [O46036-2]
DR EnsemblMetazoa; FBtr0082701; FBpp0082169; FBgn0020496. [O46036-2]
DR EnsemblMetazoa; FBtr0082702; FBpp0082170; FBgn0020496. [O46036-2]
DR EnsemblMetazoa; FBtr0100161; FBpp0099514; FBgn0020496. [O46036-1]
DR GeneID; 41602; -.
DR KEGG; dme:Dmel_CG7583; -.
DR CTD; 41602; -.
DR FlyBase; FBgn0020496; CtBP.
DR VEuPathDB; VectorBase:FBgn0020496; -.
DR eggNOG; KOG0067; Eukaryota.
DR GeneTree; ENSGT00940000171573; -.
DR InParanoid; O46036; -.
DR PhylomeDB; O46036; -.
DR Reactome; R-DME-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-DME-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DME-4641265; Repression of WNT target genes.
DR SignaLink; O46036; -.
DR BioGRID-ORCS; 41602; 1 hit in 3 CRISPR screens.
DR ChiTaRS; CtBP; fly.
DR GenomeRNAi; 41602; -.
DR PRO; PR:O46036; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0020496; Expressed in imaginal disc and 30 other tissues.
DR ExpressionAtlas; O46036; baseline and differential.
DR Genevisible; O46036; DM.
DR GO; GO:0031010; C:ISWI-type complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:FlyBase.
DR GO; GO:0001221; F:transcription coregulator binding; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0016360; P:sensory organ precursor cell fate determination; IMP:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR CDD; cd05299; CtBP_dh; 1.
DR InterPro; IPR043322; CtBP.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Oxidoreductase; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..476
FT /note="C-terminal-binding protein"
FT /id="PRO_0000076048"
FT REGION 445..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /evidence="ECO:0000250"
FT ACT_SITE 295
FT /evidence="ECO:0000250"
FT ACT_SITE 315
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 180..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 237..243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 264..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 315..318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT VAR_SEQ 377..386
FT /note="ALHHRAHSTT -> KLQMISNQEK (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:9524128, ECO:0000303|PubMed:9525852"
FT /id="VSP_011813"
FT VAR_SEQ 387..476
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:9524128, ECO:0000303|PubMed:9525852"
FT /id="VSP_011814"
FT CONFLICT 299..301
FT /note="Missing (in Ref. 2; BAA25287)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="A -> S (in Ref. 1; CAA12074)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 50737 MW; DD5F85535BEB56C1 CRC64;
MDKNLMMPKR SRIDVKGNFA NGPLQARPLV ALLDGRDCSI EMPILKDVAT VAFCDAQSTS
EIHEKVLNEA VGALMWHTII LTKEDLEKFK ALRIIVRIGS GTDNIDVKAA GELGIAVCNV
PGYGVEEVAD TTMCLILNLY RRTYWLANMV REGKKFTGPE QVREAAHGCA RIRGDTLGLV
GLGRIGSAVA LRAKAFGFNV IFYDPYLPDG IDKSLGLTRV YTLQDLLFQS DCVSLHCTLN
EHNHHLINEF TIKQMRPGAF LVNTARGGLV DDETLALALK QGRIRAAALD VHENEPYNVF
QGALKDAPNL ICTPHAAFFS DASATELREM AATEIRRAIV GNIPDVLRNC VNKEYFMRTP
PAAAAGGVAA AVYPEGALHH RAHSTTPHDG PHSTTNLGST VGGGPTTVAQ AAAAAVAAAA
AAALLPSPVP SHLSPQVGGL PLGIVSSQSP LSAPDPNNHL SSSIKTEVKA ESTEAP
