HAIR_DROME
ID HAIR_DROME Reviewed; 337 AA.
AC P14003; A4V1N7; Q95NH3; Q95NU9; Q9VSN8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Protein hairy {ECO:0000303|PubMed:2479541};
GN Name=h {ECO:0000303|PubMed:2479541, ECO:0000312|FlyBase:FBgn0001168};
GN ORFNames=CG6494 {ECO:0000312|FlyBase:FBgn0001168};
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 VARIANT SER-292.
RC STRAIN=Oregon-R;
RX PubMed=2479541; DOI=10.1002/j.1460-2075.1989.tb08461.x;
RA Rushlow C.A., Hogan A., Pierchin S.M., Howe K.M., Lardelli M.,
RA Ish-Horowicz D.;
RT "The Drosophila hairy protein acts in both segmentation and bristle
RT patterning and shows homology to N-myc.";
RL EMBO J. 8:3095-3103(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-21.
RC STRAIN=R3-105, R3-107, R3-19, R3-2, R3-24, R3-48, R3-53, R3-6, R3-74, and
RC R3-95;
RX PubMed=12242230; DOI=10.1093/genetics/162.1.155;
RA Robin C., Lyman R.F., Long A.D., Langley C.H., Mackay T.F.C.;
RT "hairy. A quantitative trait locus for Drosophila sensory bristle number.";
RL Genetics 162:155-164(2002).
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=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 [6]
RP DOMAIN WRPW MOTIF.
RX PubMed=8001118; DOI=10.1016/0092-8674(94)90070-1;
RA Paroush Z., Finley R.L. Jr., Kidd T., Wainwright S.M., Ingham P.W.,
RA Brent R., Ish-Horowicz D.;
RT "Groucho is required for Drosophila neurogenesis, segmentation, and sex
RT determination and interacts directly with hairy-related bHLH proteins.";
RL Cell 79:805-815(1994).
RN [7]
RP FUNCTION, INTERACTION WITH GRO, AND DOMAIN WRPW MOTIF.
RX PubMed=8649374; DOI=10.1128/mcb.16.6.2670;
RA Fisher A.L., Ohsako S., Caudy M.;
RT "The WRPW motif of the hairy-related basic helix-loop-helix repressor
RT proteins acts as a 4-amino-acid transcription repression and protein-
RT protein interaction domain.";
RL Mol. Cell. Biol. 16:2670-2677(1996).
RN [8]
RP DNA-BINDING, INTERACTION WITH TOPORS, AND UBIQUITINATION.
RX PubMed=14871887; DOI=10.1074/jbc.m310097200;
RA Secombe J., Parkhurst S.M.;
RT "Drosophila Topors is a RING finger-containing protein that functions as a
RT ubiquitin-protein isopeptide ligase for the hairy basic helix-loop-helix
RT repressor protein.";
RL J. Biol. Chem. 279:17126-17133(2004).
CC -!- FUNCTION: Pair-rule protein that regulates embryonic segmentation and
CC adult bristle patterning. Transcriptional repressor of genes that
CC require a bHLH protein for their transcription (e.g. ftz).
CC {ECO:0000269|PubMed:8649374}.
CC -!- SUBUNIT: Transcription repression requires formation of a complex with
CC a corepressor protein (Groucho). Interacts with gro (via WPRW motif)
CC and Topors. {ECO:0000269|PubMed:14871887, ECO:0000269|PubMed:8649374}.
CC -!- INTERACTION:
CC P14003; O46036: CtBP; NbExp=4; IntAct=EBI-123011, EBI-159330;
CC P14003; Q9VNJ0: dgrn; NbExp=5; IntAct=EBI-123011, EBI-186615;
CC P14003; P16371: gro; NbExp=6; IntAct=EBI-123011, EBI-153866;
CC P14003; P16371-2: gro; NbExp=2; IntAct=EBI-123011, EBI-15661898;
CC P14003; Q9V8P9: Topors; NbExp=4; IntAct=EBI-123011, EBI-147805;
CC P14003; P83949: Ubx; NbExp=3; IntAct=EBI-123011, EBI-202590;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00380,
CC ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- DOMAIN: Has a particular type of basic domain (presence of a helix-
CC interrupting proline) that binds to the N-box (CACNAG), rather than the
CC canonical E-box (CANNTG). {ECO:0000250|UniProtKB:Q26263}.
CC -!- DOMAIN: The C-terminal WRPW motif is a transcriptional repression
CC domain necessary for the interaction with Groucho, a transcriptional
CC corepressor recruited to specific target DNA by Hairy-related proteins.
CC {ECO:0000269|PubMed:8001118, ECO:0000269|PubMed:8649374}.
CC -!- PTM: Ubiquitinated by Topors. {ECO:0000269|PubMed:14871887}.
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DR EMBL; X15904; CAA34018.1; -; Genomic_DNA.
DR EMBL; X15905; CAA34019.1; -; mRNA.
DR EMBL; AY055833; AAL17767.1; -; Genomic_DNA.
DR EMBL; AY055834; AAL17768.1; -; Genomic_DNA.
DR EMBL; AY055835; AAL17769.1; -; Genomic_DNA.
DR EMBL; AY055836; AAL17770.1; -; Genomic_DNA.
DR EMBL; AY055837; AAL17771.1; -; Genomic_DNA.
DR EMBL; AY055838; AAL17772.1; -; Genomic_DNA.
DR EMBL; AY055839; AAL17773.1; -; Genomic_DNA.
DR EMBL; AY055840; AAL17774.1; -; Genomic_DNA.
DR EMBL; AY055841; AAL17775.1; -; Genomic_DNA.
DR EMBL; AY055842; AAL17776.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50378.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52752.1; -; Genomic_DNA.
DR EMBL; AY119633; AAM50287.1; -; mRNA.
DR PIR; S06956; S06956.
DR RefSeq; NP_001014577.1; NM_001014577.2.
DR RefSeq; NP_523977.2; NM_079253.4.
DR AlphaFoldDB; P14003; -.
DR SMR; P14003; -.
DR BioGRID; 64402; 46.
DR DIP; DIP-637N; -.
DR ELM; P14003; -.
DR IntAct; P14003; 17.
DR MINT; P14003; -.
DR STRING; 7227.FBpp0099504; -.
DR PaxDb; P14003; -.
DR EnsemblMetazoa; FBtr0076569; FBpp0076296; FBgn0001168.
DR EnsemblMetazoa; FBtr0100153; FBpp0099504; FBgn0001168.
DR GeneID; 38995; -.
DR KEGG; dme:Dmel_CG6494; -.
DR UCSC; CG6494-RA; d. melanogaster.
DR CTD; 38995; -.
DR FlyBase; FBgn0001168; h.
DR VEuPathDB; VectorBase:FBgn0001168; -.
DR eggNOG; KOG4304; Eukaryota.
DR GeneTree; ENSGT00940000166705; -.
DR HOGENOM; CLU_068550_2_1_1; -.
DR InParanoid; P14003; -.
DR OMA; EQPWRPW; -.
DR OrthoDB; 1427802at2759; -.
DR PhylomeDB; P14003; -.
DR SignaLink; P14003; -.
DR ChiTaRS; h; fly.
DR GenomeRNAi; 38995; -.
DR PRO; PR:P14003; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0001168; Expressed in spermathecum and 52 other tissues.
DR Genevisible; P14003; DM.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0070888; F:E-box binding; IDA:FlyBase.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR GO; GO:0061024; P:membrane organization; TAS: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:0007399; P:nervous system development; TAS:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0007366; P:periodic partitioning by pair rule gene; TAS:FlyBase.
DR GO; GO:0035289; P:posterior head segmentation; TAS:FlyBase.
DR GO; GO:0031323; P:regulation of cellular metabolic process; IMP:FlyBase.
DR GO; GO:0050767; P:regulation of neurogenesis; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IMP:FlyBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
DR GO; GO:0035290; P:trunk segmentation; TAS:FlyBase.
DR GO; GO:0035239; P:tube morphogenesis; IMP:FlyBase.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR003650; Orange_dom.
DR Pfam; PF07527; Hairy_orange; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00511; ORANGE; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS51054; ORANGE; 1.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Nucleus; Pair-rule protein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..337
FT /note="Protein hairy"
FT /id="PRO_0000127181"
FT DOMAIN 31..88
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 107..136
FT /note="Orange"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00380"
FT REGION 29..48
FT /note="Interaction with Topors"
FT /evidence="ECO:0000269|PubMed:14871887"
FT REGION 146..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 334..337
FT /note="WRPW motif"
FT /evidence="ECO:0000269|PubMed:8001118,
FT ECO:0000269|PubMed:8649374"
FT COMPBIAS 146..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 21
FT /note="A -> S (in strain: R3-6, R3-105 and R3-107)"
FT /evidence="ECO:0000269|PubMed:12242230"
FT VARIANT 292
FT /note="P -> S"
FT /evidence="ECO:0000269|PubMed:2479541"
SQ SEQUENCE 337 AA; 37005 MW; 49BECAF7F2D69FC4 CRC64;
MVTGVTAANM TNVLGTAVVP AQLKETPLKS DRRSNKPIME KRRRARINNC LNELKTLILD
ATKKDPARHS KLEKADILEK TVKHLQELQR QQAAMQQAAD PKIVNKFKAG FADCVNEVSR
FPGIEPAQRR RLLQHLSNCI NGVKTELHQQ QRQQQQQSIH AQMLPSPPSS PEQDSQQGAA
APYLFGIQQT ASGYFLPNGM QVIPTKLPNG SIALVLPQSL PQQQQQQLLQ HQQQQQQLAV
AAAAAAAAAA QQQPMLVSMP QRTASTGSAS SHSSAGYESA PGSSSSCSYA PPSPANSSYE
PMDIKPSVIQ RVPMEQQPLS LVIKKQIKEE EQPWRPW
