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LOZEN_DROME
ID   LOZEN_DROME             Reviewed;         826 AA.
AC   Q9W349; Q24183; Q9NHX9;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Protein lozenge;
GN   Name=lz; ORFNames=CG1689;
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], AND FUNCTION.
RX   PubMed=8675007; DOI=10.1101/gad.10.10.1194;
RA   Daga A., Karlovich C.A., Dumstrei K., Banerjee U.;
RT   "Patterning of cells in the Drosophila eye by Lozenge, which shares
RT   homologous domains with AML1.";
RL   Genes Dev. 10:1194-1205(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12111211; DOI=10.1007/s00427-002-0241-4;
RA   Behan K.J., Nichols C.D., Cheung T.L., Farlow A., Hogan B.M., Batterham P.,
RA   Pollock J.A.;
RT   "Yan regulates Lozenge during Drosophila eye development.";
RL   Dev. Genes Evol. 212:267-276(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   FUNCTION.
RX   PubMed=10707973; DOI=10.1016/s0896-6273(00)80872-7;
RA   Goulding S.E., zur Lage P., Jarman A.P.;
RT   "Amos, a proneural gene for Drosophila olfactory sense organs that is
RT   regulated by lozenge.";
RL   Neuron 25:69-78(2000).
RN   [6]
RP   FUNCTION.
RX   PubMed=15879554; DOI=10.1101/gad.1298105;
RA   Wildonger J., Sosinsky A., Honig B., Mann R.S.;
RT   "Lozenge directly activates argos and klumpfuss to regulate programmed cell
RT   death.";
RL   Genes Dev. 19:1034-1039(2005).
CC   -!- FUNCTION: Involved in prepatterning photoreceptor precursors in the
CC       developing eye; in the larval eye disk it defines a subset of cells as
CC       an equipotential group that is competent to respond to the sevenless
CC       developmental signal and another subset that confer proper
CC       photoreceptor identity by positively regulating the homeo box gene Bar.
CC       Involved in the aop/pnt dynamic in a Ras-dependent manner to regulate
CC       pros expression. Promotes apoptosis in the pupal eye by directly
CC       activating aos and klu. Also modulates hid- and rpr-mediated cell
CC       death. Regulates amos function in olfactory sensilla development.
CC       {ECO:0000269|PubMed:10707973, ECO:0000269|PubMed:12111211,
CC       ECO:0000269|PubMed:15879554, ECO:0000269|PubMed:8675007}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00399}.
CC   -!- TISSUE SPECIFICITY: Expressed in the pupal eye during programmed cell
CC       death. {ECO:0000269|PubMed:12111211}.
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DR   EMBL; U47849; AAC47196.2; -; mRNA.
DR   EMBL; AF217651; AAF35308.1; -; Genomic_DNA.
DR   EMBL; AE014298; AAF46486.2; -; Genomic_DNA.
DR   RefSeq; NP_511099.2; NM_078544.3.
DR   AlphaFoldDB; Q9W349; -.
DR   SMR; Q9W349; -.
DR   BioGRID; 58331; 22.
DR   ELM; Q9W349; -.
DR   STRING; 7227.FBpp0071255; -.
DR   PaxDb; Q9W349; -.
DR   EnsemblMetazoa; FBtr0071320; FBpp0071255; FBgn0002576.
DR   GeneID; 31883; -.
DR   KEGG; dme:Dmel_CG1689; -.
DR   UCSC; CG1689-RA; d. melanogaster.
DR   CTD; 17106; -.
DR   FlyBase; FBgn0002576; lz.
DR   VEuPathDB; VectorBase:FBgn0002576; -.
DR   eggNOG; KOG3982; Eukaryota.
DR   GeneTree; ENSGT00940000159255; -.
DR   HOGENOM; CLU_016277_0_0_1; -.
DR   InParanoid; Q9W349; -.
DR   OMA; YNNAAAW; -.
DR   OrthoDB; 1130963at2759; -.
DR   PhylomeDB; Q9W349; -.
DR   Reactome; R-DME-549127; Organic cation transport.
DR   Reactome; R-DME-8878166; Transcriptional regulation by RUNX2.
DR   Reactome; R-DME-8931987; RUNX1 regulates estrogen receptor mediated transcription.
DR   Reactome; R-DME-8934593; Regulation of RUNX1 Expression and Activity.
DR   Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-DME-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR   Reactome; R-DME-8939245; RUNX1 regulates transcription of genes involved in BCR signaling.
DR   Reactome; R-DME-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
DR   Reactome; R-DME-8939247; RUNX1 regulates transcription of genes involved in interleukin signaling.
DR   Reactome; R-DME-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-DME-8940973; RUNX2 regulates osteoblast differentiation.
DR   Reactome; R-DME-8941326; RUNX2 regulates bone development.
DR   Reactome; R-DME-8941855; RUNX3 regulates CDKN1A transcription.
DR   Reactome; R-DME-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-DME-8951430; RUNX3 regulates WNT signaling.
DR   Reactome; R-DME-8951671; RUNX3 regulates YAP1-mediated transcription.
DR   Reactome; R-DME-8951936; RUNX3 regulates p14-ARF.
DR   Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR   SignaLink; Q9W349; -.
DR   BioGRID-ORCS; 31883; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 31883; -.
DR   PRO; PR:Q9W349; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0002576; Expressed in crystal cell primordium (Drosophila) and 12 other tissues.
DR   ExpressionAtlas; Q9W349; baseline and differential.
DR   Genevisible; Q9W349; DM.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:FlyBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR   GO; GO:0007469; P:antennal development; TAS:FlyBase.
DR   GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
DR   GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR   GO; GO:0042688; P:crystal cell differentiation; IMP:FlyBase.
DR   GO; GO:0035165; P:embryonic crystal cell differentiation; IMP:FlyBase.
DR   GO; GO:0035163; P:embryonic hemocyte differentiation; IMP:FlyBase.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:FlyBase.
DR   GO; GO:0048592; P:eye morphogenesis; IMP:FlyBase.
DR   GO; GO:0007486; P:imaginal disc-derived female genitalia development; IMP:FlyBase.
DR   GO; GO:0035168; P:larval lymph gland hemocyte differentiation; TAS:FlyBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:FlyBase.
DR   GO; GO:0046672; P:positive regulation of compound eye retinal cell programmed cell death; IMP:UniProtKB.
DR   GO; GO:0042691; P:positive regulation of crystal cell differentiation; IMP:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0045467; P:R7 cell development; IMP:FlyBase.
DR   GO; GO:0035314; P:scab formation; IMP:FlyBase.
DR   GO; GO:0016360; P:sensory organ precursor cell fate determination; TAS:FlyBase.
DR   GO; GO:0035211; P:spermathecum morphogenesis; TAS:FlyBase.
DR   GO; GO:0042060; P:wound healing; IMP:FlyBase.
DR   Gene3D; 2.60.40.720; -; 1.
DR   InterPro; IPR000040; AML1_Runt.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR   InterPro; IPR013524; Runt_dom.
DR   PANTHER; PTHR11950; PTHR11950; 1.
DR   Pfam; PF00853; Runt; 1.
DR   PRINTS; PR00967; ONCOGENEAML1.
DR   SUPFAM; SSF49417; SSF49417; 1.
DR   PROSITE; PS51062; RUNT; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..826
FT                   /note="Protein lozenge"
FT                   /id="PRO_0000174666"
FT   DOMAIN          275..403
FT                   /note="Runt"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          774..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..142
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        8
FT                   /note="A -> V (in Ref. 1; AAC47196)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="S -> F (in Ref. 1; AAC47196)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        252
FT                   /note="N -> NNNN (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        341..342
FT                   /note="EL -> DV (in Ref. 1; AAC47196)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   826 AA;  84722 MW;  BCDF558F3E42B5CC CRC64;
     MHLHLLAAEK TPPSPSPNPT PTPSASPSGH TGAAGESQLD LASQTESQLQ LGLPLASGYG
     LGLGLGLGLG LGLGQELVAD HSTTVAPVSV AGPGRLGRSI NGSGGSHHHH HLHHHYSPYH
     HAHPYHPPHP HAPHHHHHHH PPYPYPPAGP HPPAMVTSSS TSPTGNGWSS STGDFKGITA
     VATATGGGVG GATQGATAST GATAAEVLAV SSSASVGSSS PTGGASNGTA HSGHSGHTGG
     HSSSTASNNN NNGASNSNSN NNNAVHQDLL WMERLVQKRQ QEHPGELVRT SNPYFLCSAL
     PAHWRSNKTL PMAFKVVALA EVGDGTYVTI RAGNDENCCA ELRNFTTQMK NDVAKFNDLR
     FVGRSGRGKS FTLTITVATS PPQVATYAKA IKVTVDGPRE PRSKTSPTGG PHYRALGLGQ
     RPYIDGFPST KALHELESLR RSAKVAAVTT AAAAAATAAS AANAVAAAAA AVAVTPTGGG
     GGVAAGGVAG GAGAGLVQQL SSNYSSPNST INSDCQVYKP NAPHIQAAEM MGAGEWTNGS
     SSSAAAYYHS HAHHPHAHHA HAHLQHQMAL PPPPPPPAAA PVSVGVGGNG ATMGMGMGVG
     VGMGMNHYGG GYDSANSLEA GQYAAHLPAV LPEMHGHGFA TDPYQTAGYG GGNTGGGSAS
     KSELDYGGSY NQAWSNGYQN YQYGSCLATA QYGPQAAPPP QPPPPPPVVL CPQLYSTVNQ
     NQIHLHLHSS EKLEQYLGTA TSADHLTIGS LTGSSRSSIE IGQDQYHQQV HHAQQQQQQQ
     QQQQQVHHPQ QQQVESAGEV GGSGAGGVES AREEDVGDLS QVWRPY
 
 
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