位置:首页 > 蛋白库 > EMC_DROME
EMC_DROME
ID   EMC_DROME               Reviewed;         199 AA.
AC   P18491; Q9W0N0;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 194.
DE   RecName: Full=Protein extra-macrochaetae;
GN   Name=emc; ORFNames=CG1007;
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].
RX   PubMed=1690605; DOI=10.1016/0092-8674(90)90213-x;
RA   Garrell J., Modolell J.;
RT   "The Drosophila extramacrochaetae locus, an antagonist of proneural genes
RT   that, like these genes, encodes a helix-loop-helix protein.";
RL   Cell 61:39-48(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1690604; DOI=10.1016/0092-8674(90)90212-w;
RA   Ellis H.M., Spann D.R., Posakony J.W.;
RT   "Extramacrochaetae, a negative regulator of sensory organ development in
RT   Drosophila, defines a new class of helix-loop-helix proteins.";
RL   Cell 61:27-38(1990).
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).
CC   -!- FUNCTION: Participates in sensory organ patterning by antagonizing the
CC       neurogenic activity of the Achaete-scute complex (AS-C). It lacks a
CC       basic DNA-binding domain but is able to form heterodimers with other
CC       HLH proteins, thereby inhibiting DNA binding. May sequester proneural
CC       proteins in complexes inefficient for DNA interaction. EMC also affects
CC       vein differentiation. Inhibits the activity of AS-C proteins by forming
CC       an non-DNA binding heterodimer.
CC   -!- SUBUNIT: Heterodimer with other HLH proteins.
CC   -!- INTERACTION:
CC       P18491; P10084: sc; NbExp=4; IntAct=EBI-105737, EBI-174136;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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; M31900; AAA28510.1; -; Genomic_DNA.
DR   EMBL; M31901; AAA28510.1; JOINED; Genomic_DNA.
DR   EMBL; M31902; AAA28509.1; -; mRNA.
DR   EMBL; M32637; AAA28511.1; -; Genomic_DNA.
DR   EMBL; M32636; AAA28511.1; JOINED; Genomic_DNA.
DR   EMBL; AE014296; AAF47413.2; -; Genomic_DNA.
DR   EMBL; AY069405; AAL39550.1; -; mRNA.
DR   PIR; A34688; A34688.
DR   PIR; A34689; A34689.
DR   RefSeq; NP_523876.2; NM_079152.4.
DR   AlphaFoldDB; P18491; -.
DR   SMR; P18491; -.
DR   BioGRID; 63646; 30.
DR   DIP; DIP-73N; -.
DR   IntAct; P18491; 17.
DR   STRING; 7227.FBpp0072477; -.
DR   PaxDb; P18491; -.
DR   EnsemblMetazoa; FBtr0072578; FBpp0072477; FBgn0000575.
DR   GeneID; 38091; -.
DR   KEGG; dme:Dmel_CG1007; -.
DR   CTD; 38091; -.
DR   FlyBase; FBgn0000575; emc.
DR   VEuPathDB; VectorBase:FBgn0000575; -.
DR   eggNOG; ENOG502RZP5; Eukaryota.
DR   GeneTree; ENSGT00940000169907; -.
DR   HOGENOM; CLU_115564_0_0_1; -.
DR   InParanoid; P18491; -.
DR   OMA; GRIQRHP; -.
DR   OrthoDB; 1624054at2759; -.
DR   PhylomeDB; P18491; -.
DR   Reactome; R-DME-2559585; Oncogene Induced Senescence.
DR   SignaLink; P18491; -.
DR   BioGRID-ORCS; 38091; 1 hit in 3 CRISPR screens.
DR   GenomeRNAi; 38091; -.
DR   PRO; PR:P18491; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0000575; Expressed in wing disc and 82 other tissues.
DR   Genevisible; P18491; DM.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:FlyBase.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0008407; P:chaeta morphogenesis; TAS:FlyBase.
DR   GO; GO:0030381; P:chorion-containing eggshell pattern formation; IMP:FlyBase.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:FlyBase.
DR   GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR   GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR   GO; GO:0008258; P:head involution; IMP:FlyBase.
DR   GO; GO:0061525; P:hindgut development; IMP:FlyBase.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR   GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR   GO; GO:0007494; P:midgut development; IMP:FlyBase.
DR   GO; GO:0043392; P:negative regulation of DNA binding; IDA:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
DR   GO; GO:0046552; P:photoreceptor cell fate commitment; IMP:FlyBase.
DR   GO; GO:0007458; P:progression of morphogenetic furrow involved in compound eye morphogenesis; IMP:FlyBase.
DR   GO; GO:0048056; P:R3/R4 cell differentiation; IMP:FlyBase.
DR   GO; GO:0045466; P:R7 cell differentiation; IMP:FlyBase.
DR   GO; GO:0007530; P:sex determination; IGI:FlyBase.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR026052; DNA-bd_prot-inh.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR11723; PTHR11723; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..199
FT                   /note="Protein extra-macrochaetae"
FT                   /id="PRO_0000127169"
FT   DOMAIN          23..75
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          127..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        123
FT                   /note="I -> V (in Ref. 1; AAA28510/AAA28509)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   199 AA;  21978 MW;  08C1683352B26F0E CRC64;
     MKSLTAVCQT GASGMPALNA SGRIQRHPTH RGDGENAEMK MYLSKLKDLV PFMPKNRKLT
     KLEIIQHVID YICDLQTELE THPEMGNFDA AAALTAVNGL HEDEDSDMED ADAEAEAEVD
     PDILAQRLNA EQPAKVSSPA ARLPLTDRQT PNTLVAPAHP QQHQQQQQLQ LQQQQLQSQQ
     QLSNSLATPQ NAEKDSRQS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024