SUH_DROME
ID SUH_DROME Reviewed; 594 AA.
AC P28159; Q3S1M8; Q9TVK8; Q9TVY7; Q9TW34; Q9U8F9; Q9V446;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Suppressor of hairless protein;
DE AltName: Full=J kappa-recombination signal-binding protein;
DE AltName: Full=RBP-J kappa;
GN Name=Su(H); Synonyms=dRBP-JK; ORFNames=CG3497;
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 [GENOMIC DNA / MRNA], AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=1744127; DOI=10.1016/s0021-9258(18)54501-4;
RA Furukawa T., Kawaichi M., Matsunami N., Ryo H., Nishida Y., Honjo T.;
RT "The Drosophila RBP-J kappa gene encodes the binding protein for the
RT immunoglobulin J kappa recombination signal sequence.";
RL J. Biol. Chem. 266:23334-23340(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC TISSUE=Imaginal disk;
RX PubMed=1617730; DOI=10.1016/0092-8674(92)90641-o;
RA Schweisguth F., Posakony J.W.;
RT "Suppressor of Hairless, the Drosophila homolog of the mouse recombination
RT signal-binding protein gene, controls sensory organ cell fates.";
RL Cell 69:1199-1212(1992).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-128.
RC STRAIN=LAMTO 101, LAMTO 106, LAMTO 111, LAMTO 12, LAMTO 120, LAMTO 124,
RC LAMTO 13, LAMTO 134, LAMTO 19, LAMTO 21, LAMTO 27, LAMTO 28, LAMTO 3,
RC LAMTO 31, LAMTO 33, LAMTO 35, LAMTO 37, LAMTO 4, LAMTO 5, and LAMTP 18;
RX PubMed=10388820; DOI=10.1093/genetics/152.3.1017;
RA Depaulis F., Brazier L., Veuille M.;
RT "Selective sweep at the Drosophila melanogaster Suppressor of Hairless
RT locus and its association with the In(2L)t inversion polymorphism.";
RL Genetics 152:1017-1024(1999).
RN [8]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=1617729; DOI=10.1016/0092-8674(92)90640-x;
RA Furukawa T., Maruyama S., Kawaichi M., Honjo T.;
RT "The Drosophila homolog of the immunoglobulin recombination signal-binding
RT protein regulates peripheral nervous system development.";
RL Cell 69:1191-1197(1992).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF TYR-315.
RX PubMed=7813798; DOI=10.1006/dbio.1994.1359;
RA Schweisguth F., Nero P., Posakony J.W.;
RT "The sequence similarity of the Drosophila suppressor of hairless protein
RT to the integrase domain has no functional significance in vivo.";
RL Dev. Biol. 166:812-814(1994).
RN [10]
RP INTERACTION WITH HAIRLESS.
RX PubMed=7958912; DOI=10.1101/gad.8.20.2491;
RA Brou C., Logeat F., Lecourtois M., Vandekerckhove J., Kourilsky P.,
RA Schweisguth F., Israel A.;
RT "Inhibition of the DNA-binding activity of Drosophila suppressor of
RT hairless and of its human homolog, KBF2/RBP-J kappa, by direct protein-
RT protein interaction with Drosophila hairless.";
RL Genes Dev. 8:2491-2503(1994).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8674407; DOI=10.1242/dev.122.6.1673;
RA Gho M., Lecourtois M., Geraud G., Posakony J.W., Schweisguth F.;
RT "Subcellular localization of Suppressor of Hairless in Drosophila sense
RT organ cells during Notch signalling.";
RL Development 122:1673-1682(1996).
RN [12]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=10673509;
RA Morel V., Schweisguth F.;
RT "Repression by suppressor of hairless and activation by Notch are required
RT to define a single row of single-minded expressing cells in the Drosophila
RT embryo.";
RL Genes Dev. 14:377-388(2000).
RN [13]
RP FUNCTION.
RX PubMed=12642500; DOI=10.1242/dev.00426;
RA Koelzer S., Klein T.;
RT "A Notch-independent function of Suppressor of Hairless during the
RT development of the bristle sensory organ precursor cell of Drosophila.";
RL Development 130:1973-1988(2003).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21262215; DOI=10.1016/j.ydbio.2011.01.019;
RA San-Juan B.P., Baonza A.;
RT "The bHLH factor deadpan is a direct target of Notch signaling and
RT regulates neuroblast self-renewal in Drosophila.";
RL Dev. Biol. 352:70-82(2011).
RN [15]
RP INTERACTION WITH INSV.
RX PubMed=21765394; DOI=10.1038/emboj.2011.218;
RA Duan H., Dai Q., Kavaler J., Bejarano F., Medranda G., Negre N., Lai E.C.;
RT "Insensitive is a corepressor for Suppressor of Hairless and regulates
RT Notch signalling during neural development.";
RL EMBO J. 30:3120-3133(2011).
CC -!- FUNCTION: Transcriptional regulator that plays a central role in Notch
CC signaling, a signaling pathway involved in cell-cell communication that
CC regulates a broad spectrum of cell-fate determinations
CC (PubMed:21262215, PubMed:1617729, PubMed:8674407, PubMed:10673509).
CC Binds directly the 5'-GTGRGAR-3' DNA consensus sequence, which is
CC present in the regulatory region of several genes (PubMed:10673509).
CC Acts as a transcriptional repressor when it is not associated with
CC Notch proteins (PubMed:10673509). When associated with some Notch
CC protein, it acts as a transcriptional activator that activates
CC transcription of Notch target genes (PubMed:10673509). Required for
CC transcription of Sim (PubMed:10673509). Specifically binds to the
CC immunoglobulin kappa-type J segment recombination signal sequence
CC (PubMed:1744127, PubMed:1617730, PubMed:1617729). Required for
CC neurogenesis in imaginal disks (PubMed:1617730, PubMed:7813798). In the
CC larval brain, might play a role as a transducer of Notch signaling
CC during type II neuroblast development (PubMed:21262215). Also functions
CC independently of the Notch pathway, in the development of the bristle
CC sensory organ precursor cell (PubMed:12642500).
CC {ECO:0000269|PubMed:10673509, ECO:0000269|PubMed:12642500,
CC ECO:0000269|PubMed:1617729, ECO:0000269|PubMed:1617730,
CC ECO:0000269|PubMed:1744127, ECO:0000269|PubMed:21262215,
CC ECO:0000269|PubMed:7813798, ECO:0000269|PubMed:8674407}.
CC -!- SUBUNIT: Interacts with activated cleaved Notch. Interacts with
CC Hairless, this interaction preventing its DNA-binding activity.
CC Interacts with insv (via BEN domain). {ECO:0000269|PubMed:21765394,
CC ECO:0000269|PubMed:7958912}.
CC -!- INTERACTION:
CC P28159; Q8SYK5: insv; NbExp=4; IntAct=EBI-92180, EBI-192407;
CC P28159; P07207: N; NbExp=7; IntAct=EBI-92180, EBI-103438;
CC P28159; Q01705: Notch1; Xeno; NbExp=3; IntAct=EBI-92180, EBI-1392707;
CC P28159; P20226: TBP; Xeno; NbExp=2; IntAct=EBI-92180, EBI-355371;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8674407}. Cytoplasm
CC {ECO:0000269|PubMed:8674407}. Note=In imaginal disk, at the onset of
CC differentiation of socket cell, it is also present in the cytoplasm.
CC {ECO:0000269|PubMed:8674407}.
CC -!- DEVELOPMENTAL STAGE: Expressed in early syncytial embryo
CC (PubMed:1617730, PubMed:1617729). During cellularization, transient
CC accumulation in a striped pattern (PubMed:1617730, PubMed:1617729).
CC From late stage 11 onward, expressed gradually in a small number of
CC segmentally reiterated cells of the peripheral nervous system (PNS)
CC (PubMed:1617730, PubMed:1617729). This expression is specific to the
CC external sensory organs (PubMed:1617730). In the thoracic and abdominal
CC segments, expressed in the trichogen and tormogen cells, two outer
CC accessory cells present in all larval external sensory organs
CC (PubMed:1617730). During the late third larval instar, expressed in
CC many larval and imaginal tissues (PubMed:1617730). Broadly distributed
CC in the disks, but most abundant in the posterior region of the wing
CC pouch (PubMed:1617730). In the leg disk, predominant in a zone largely
CC overlapping the posterior region (PubMed:1617730). In the eye-antenna
CC disk, low level in both the retinal field posterior to the
CC morphogenetic furrow and the central antenna region, while higher
CC levels appears on the margins of the disk and in the vicinity of the
CC morphogenetic furrow (PubMed:1617730). In pupae, expressed in many
CC tissues at this stage, including developing muscle and epidermis
CC (PubMed:1617730). In both microchaetes and macrochaetes of 24 hr pupae,
CC expressed on the notum and the head (PubMed:1617730). Expressed in the
CC tormogen cell and in specific bristle cells (PubMed:1617730).
CC {ECO:0000269|PubMed:1617729, ECO:0000269|PubMed:1617730}.
CC -!- DISRUPTION PHENOTYPE: Lethal during the first day of pupal development
CC (PubMed:1617730). At the larval stage, results in a 'neurogenic'
CC phenotype in imaginal disks, in which too many cells adopt the sensory
CC organ precursor cell fate (PubMed:1617730). RNAi-mediated knockdown in
CC type II neuroblasts, results in smaller cells (PubMed:1617730).
CC {ECO:0000269|PubMed:1617730, ECO:0000269|PubMed:21262215}.
CC -!- SIMILARITY: Belongs to the Su(H) family. {ECO:0000305}.
CC -!- CAUTION: Despite some similarity with the 'phage' integrase family,
CC PubMed:7958912 showed that it has no recombinase activity.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA06211.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA41282.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; S69213; AAA06211.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X58393; CAA41282.1; ALT_INIT; mRNA.
DR EMBL; M94383; AAA28919.1; -; mRNA.
DR EMBL; AE014134; AAF53434.1; -; Genomic_DNA.
DR EMBL; AY069091; AAL39236.1; -; mRNA.
DR EMBL; AF088255; AAD39698.1; -; Genomic_DNA.
DR EMBL; AF088256; AAD39699.1; -; Genomic_DNA.
DR EMBL; AF088257; AAD39700.1; -; Genomic_DNA.
DR EMBL; AF088258; AAD39701.1; -; Genomic_DNA.
DR EMBL; AF088259; AAD39702.1; -; Genomic_DNA.
DR EMBL; AF088260; AAD39703.1; -; Genomic_DNA.
DR EMBL; AF088261; AAD39704.1; -; Genomic_DNA.
DR EMBL; AF088262; AAD39705.1; -; Genomic_DNA.
DR EMBL; AF088263; AAD39706.1; -; Genomic_DNA.
DR EMBL; AF088264; AAD39707.1; -; Genomic_DNA.
DR EMBL; AF088265; AAD39708.1; -; Genomic_DNA.
DR EMBL; AF088266; AAD39709.1; -; Genomic_DNA.
DR EMBL; AF088267; AAD39710.1; -; Genomic_DNA.
DR EMBL; AF088268; AAD39711.1; -; Genomic_DNA.
DR EMBL; AF088269; AAD39712.1; -; Genomic_DNA.
DR EMBL; AF088270; AAD39713.1; -; Genomic_DNA.
DR EMBL; AF088271; AAD39714.1; -; Genomic_DNA.
DR EMBL; AF088272; AAD39715.1; -; Genomic_DNA.
DR EMBL; AF088273; AAD39716.1; -; Genomic_DNA.
DR EMBL; AF088274; AAD39717.1; -; Genomic_DNA.
DR PIR; A41585; A41585.
DR PIR; A42770; A42770.
DR RefSeq; NP_001285948.1; NM_001299019.1.
DR RefSeq; NP_476868.1; NM_057520.4.
DR PDB; 5E24; X-ray; 2.14 A; E/F=99-522.
DR PDBsum; 5E24; -.
DR AlphaFoldDB; P28159; -.
DR SMR; P28159; -.
DR BioGRID; 60899; 85.
DR DIP; DIP-177N; -.
DR IntAct; P28159; 23.
DR MINT; P28159; -.
DR STRING; 7227.FBpp0080261; -.
DR iPTMnet; P28159; -.
DR PaxDb; P28159; -.
DR EnsemblMetazoa; FBtr0080700; FBpp0080261; FBgn0004837.
DR EnsemblMetazoa; FBtr0346621; FBpp0312201; FBgn0004837.
DR GeneID; 34881; -.
DR KEGG; dme:Dmel_CG3497; -.
DR CTD; 34881; -.
DR FlyBase; FBgn0004837; Su(H).
DR VEuPathDB; VectorBase:FBgn0004837; -.
DR eggNOG; KOG3743; Eukaryota.
DR HOGENOM; CLU_022207_2_1_1; -.
DR InParanoid; P28159; -.
DR OMA; ISEVQWN; -.
DR OrthoDB; 444988at2759; -.
DR PhylomeDB; P28159; -.
DR Reactome; R-DME-350054; Notch-HLH transcription pathway.
DR SignaLink; P28159; -.
DR BioGRID-ORCS; 34881; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34881; -.
DR PRO; PR:P28159; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004837; Expressed in outer epithelium and 71 other tissues.
DR ExpressionAtlas; P28159; baseline and differential.
DR Genevisible; P28159; DM.
DR GO; GO:1990433; C:CSL-Notch-Mastermind transcription factor complex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IPI:FlyBase.
DR GO; GO:0017053; C:transcription repressor complex; IGI:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:FlyBase.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:FlyBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0008356; P:asymmetric cell division; TAS:FlyBase.
DR GO; GO:0001709; P:cell fate determination; TAS:FlyBase.
DR GO; GO:0042688; P:crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0030097; P:hemopoiesis; TAS:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0042683; P:negative regulation of compound eye cone cell fate specification; TAS:FlyBase.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; TAS:FlyBase.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:FlyBase.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0016360; P:sensory organ precursor cell fate determination; IMP:UniProtKB.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IMP:FlyBase.
DR CDD; cd01176; IPT_RBP-Jkappa; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1450; -; 1.
DR InterPro; IPR015350; Beta-trefoil_DNA-bd_dom.
DR InterPro; IPR036358; BTD_sf.
DR InterPro; IPR040159; CLS_fam.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR015351; RBP-J/Cbf11/Cbf12_DNA-bd.
DR InterPro; IPR037095; RBP-J/Cbf11_DNA-bd_sf.
DR InterPro; IPR038007; RBP-Jkappa_IPT.
DR PANTHER; PTHR10665; PTHR10665; 1.
DR Pfam; PF09270; BTD; 1.
DR Pfam; PF09271; LAG1-DNAbind; 1.
DR Pfam; PF20144; TIG_SUH; 1.
DR SMART; SM01268; BTD; 1.
DR SMART; SM01267; LAG1_DNAbind; 1.
DR SUPFAM; SSF110217; SSF110217; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Developmental protein; DNA-binding;
KW Notch signaling pathway; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..594
FT /note="Suppressor of hairless protein"
FT /id="PRO_0000208572"
FT DOMAIN 429..519
FT /note="IPT/TIG"
FT REGION 20..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..141
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q06330"
FT REGION 239..244
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q06330"
FT REGION 266..271
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q06330"
FT REGION 542..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 80..82
FT /note="Missing (in strain: LAMTO 3, LAMTO 4, LAMTO 12,
FT LAMTO 18, LAMTO 19, LAMTO 21, LAMTO 31, LAMTO 35, LAMTO 101
FT and LAMTO 111)"
FT VARIANT 81..82
FT /note="Missing (in strain: LAMTO 13, LAMTO 37 and LAMTO
FT 134)"
FT VARIANT 82
FT /note="Missing (in strain: LAMTO 124)"
FT MUTAGEN 315
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:7813798"
FT CONFLICT 116..117
FT /note="ER -> DG (in Ref. 1; AAA06211/CAA41282)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="V -> A (in Ref. 1; AAA06211/CAA41282)"
FT /evidence="ECO:0000305"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 120..131
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:5E24"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:5E24"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:5E24"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 259..266
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:5E24"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 367..375
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 388..395
FT /evidence="ECO:0007829|PDB:5E24"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 402..416
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 444..450
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:5E24"
FT HELIX 483..488
FT /evidence="ECO:0007829|PDB:5E24"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 498..504
FT /evidence="ECO:0007829|PDB:5E24"
FT STRAND 507..520
FT /evidence="ECO:0007829|PDB:5E24"
SQ SEQUENCE 594 AA; 66924 MW; 145144F336CD8F4C CRC64;
MKSYSQFNLN AAAPPAIAYE TTVVNPNGSP LDPHQQQQQQ SQDMPHFGLP GPQPPSSQQQ
QQQLQVHHQQ QQQQQQQQQQ QQHQQQMQMS LLPGPYRPHI EEKKLTRDAM EKYMRERNDM
VIVILHAKVA QKSYGNEKRF FCPPPCIYLF GSGWRRRYEE MLQQGEGEQG AQLCAFIGIG
SSDQDMQQLD LNGKQYCAAK TLFISDSDKR KHFMLSVKMF YGNGHDIGVF NSKRIKVISK
PSKKKQSLKN ADLCIASGTN VALFNRLRSQ TVSTRYLHVE NGHFHASSTQ WGAFTIHLLD
DNESESEEFQ VRDGYIHYGA TVKLVCSVTG MALPRLIIRK VDKQMALLEA DDPVSQLHKC
AFYMKDTDRM YLCLSQEKII QFQATPCPKE PNKEMINDGA CWTIISTDKA EYQFYEGMGP
VASPVTPVPI VNSLNLNGGG DVAMLELSGD NFTPHLQVWF GDVEAETMYR CTETLLCVVP
EISQFRGEWL WVRQPTQVPI SLVRNDGIIY ATGLTFTYTP EPGPRPHCNT QAEDVMRARQ
NNNNNNITSI SNNNNSNNAG SPAAGGGLQQ QQQQHQALPS ISEVQWNSHG SGLS
