位置:首页 > 蛋白库 > ESCA_DROME
ESCA_DROME
ID   ESCA_DROME              Reviewed;         470 AA.
AC   P25932; Q8SYF2; Q9V3E1;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=Protein escargot;
DE   AltName: Full=Protein fleabag;
GN   Name=esg; Synonyms=flg; ORFNames=CG3758;
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], AND TISSUE SPECIFICITY.
RC   STRAIN=Oregon-R;
RX   PubMed=1571289; DOI=10.1016/0925-4773(92)90063-p;
RA   Whiteley M.H., Noguchi P.D., Sensabaugh S.M., Odenwald W., Kassis J.A.;
RT   "The Drosophila gene escargot encodes a zinc finger motif found in snail-
RT   related genes.";
RL   Mech. Dev. 36:117-127(1992).
RN   [2]
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   [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   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=8375329; DOI=10.1242/dev.118.1.105;
RA   Hayashi S., Hirose S., Metcalfe T., Shirras A.D.;
RT   "Control of imaginal cell development by the escargot gene of Drosophila.";
RL   Development 118:105-115(1993).
RN   [7]
RP   FUNCTION, DNA-BINDING SPECIFICITY, AND MUTAGENESIS OF GLY-387.
RX   PubMed=7958894; DOI=10.1101/gad.8.19.2270;
RA   Fuse N., Hirose S., Hayashi S.;
RT   "Diploidy of Drosophila imaginal cells is maintained by a transcriptional
RT   repressor encoded by escargot.";
RL   Genes Dev. 8:2270-2281(1994).
RN   [8]
RP   FUNCTION, DNA-BINDING SPECIFICITY, AND TISSUE SPECIFICITY.
RX   PubMed=8620833; DOI=10.1242/dev.122.4.1059;
RA   Fuse N., Hirose S., Hayashi S.;
RT   "Determination of wing cell fate by the escargot and snail genes in
RT   Drosophila.";
RL   Development 122:1059-1067(1996).
RN   [9]
RP   FUNCTION.
RX   PubMed=9012491; DOI=10.1242/dev.122.12.3697;
RA   Tanaka-Matakatsu M., Uemura T., Oda H., Takeichi M., Hayashi S.;
RT   "Cadherin-mediated cell adhesion and cell motility in Drosophila trachea
RT   regulated by the transcription factor Escargot.";
RL   Development 122:3697-3705(1996).
RN   [10]
RP   FUNCTION.
RX   PubMed=10562554; DOI=10.1093/emboj/18.22.6426;
RA   Ashraf S.I., Hu X., Roote J., Ip Y.T.;
RT   "The mesoderm determinant snail collaborates with related zinc-finger
RT   proteins to control Drosophila neurogenesis.";
RL   EMBO J. 18:6426-6438(1999).
RN   [11]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11902678;
RA   Streit A., Bernasconi L., Sergeev P., Cruz A., Steinmann-Zwicky M.;
RT   "mgm 1, the earliest sex-specific germline marker in Drosophila, reflects
RT   expression of the gene esg in male stem cells.";
RL   Int. J. Dev. Biol. 46:159-166(2002).
CC   -!- FUNCTION: Transcription factor that can both stimulate and repress
CC       transcription. Binds to the consensus DNA sequence 5'-A/GCAGGTG-3'.
CC       Regulates cell motility and adhesion during tracheal morphogenesis by
CC       stimulating transcription of the DE-cadherin gene shg at branch tips,
CC       thereby promoting tracheal tube fusion. Maintains diploidy in imaginal
CC       cells by inhibiting the transcription of genes required for
CC       endoreplication. Required for development of the genital disk and acts
CC       as an intrinsic determinant of wing cell fate. The somatic protein is
CC       required for maintenance of male germ cells. Acts with other members of
CC       the snail protein family to control embryonic central nervous system
CC       development. {ECO:0000269|PubMed:10562554, ECO:0000269|PubMed:11902678,
CC       ECO:0000269|PubMed:7958894, ECO:0000269|PubMed:8375329,
CC       ECO:0000269|PubMed:8620833, ECO:0000269|PubMed:9012491}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expression is complex and dynamic. In early
CC       embryogenesis, expression begins on the dorsal side of the embryo.
CC       Expressed in a pattern of longitudinal stripes early in germband
CC       elongation. Later in embryogenesis, expression is in cells that
CC       correspond to the wing, haltere, leg and genital imaginal disks and the
CC       abdominal histoblasts. In the embryonic leg disk, expression is
CC       restricted to imaginal cells. Also expressed in the central nervous
CC       system (CNS), tracheae and head of stage 14 embryos. CNS and tracheal
CC       expression decays during later stages, though head expression persists
CC       until late in embryogenesis. In third instar larvae, expression is seen
CC       in the brain and in regions of many imaginal tissues including the eye-
CC       antennal, wing, leg and haltere disks. Expressed in embryonic, larval
CC       and adult male germline stem cells and in the somatic cells of the
CC       embryonic gonads. {ECO:0000269|PubMed:11902678,
CC       ECO:0000269|PubMed:1571289, ECO:0000269|PubMed:8375329,
CC       ECO:0000269|PubMed:8620833}.
CC   -!- SIMILARITY: Belongs to the snail C2H2-type zinc-finger protein family.
CC       {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; M83207; AAA28513.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAF53458.1; -; Genomic_DNA.
DR   EMBL; AY071590; AAL49212.1; -; mRNA.
DR   PIR; S33639; S33639.
DR   RefSeq; NP_476600.1; NM_057252.4.
DR   AlphaFoldDB; P25932; -.
DR   SMR; P25932; -.
DR   BioGRID; 60919; 56.
DR   IntAct; P25932; 23.
DR   STRING; 7227.FBpp0080293; -.
DR   PaxDb; P25932; -.
DR   EnsemblMetazoa; FBtr0080734; FBpp0080293; FBgn0001981.
DR   GeneID; 34903; -.
DR   KEGG; dme:Dmel_CG3758; -.
DR   CTD; 34903; -.
DR   FlyBase; FBgn0287768; esg.
DR   VEuPathDB; VectorBase:FBgn0001981; -.
DR   eggNOG; KOG2462; Eukaryota.
DR   GeneTree; ENSGT00940000166773; -.
DR   HOGENOM; CLU_030677_0_0_1; -.
DR   InParanoid; P25932; -.
DR   OMA; INVSDCC; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P25932; -.
DR   SignaLink; P25932; -.
DR   BioGRID-ORCS; 34903; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 34903; -.
DR   PRO; PR:P25932; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0001981; Expressed in wing disc and 14 other tissues.
DR   ExpressionAtlas; P25932; baseline and differential.
DR   Genevisible; P25932; DM.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR   GO; GO:0055059; P:asymmetric neuroblast division; IGI:FlyBase.
DR   GO; GO:0035147; P:branch fusion, open tracheal system; IMP:UniProtKB.
DR   GO; GO:0001709; P:cell fate determination; IMP:UniProtKB.
DR   GO; GO:0001708; P:cell fate specification; IMP:FlyBase.
DR   GO; GO:0007417; P:central nervous system development; IMP:UniProtKB.
DR   GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:UniProtKB.
DR   GO; GO:0035215; P:genital disc development; IMP:UniProtKB.
DR   GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:UniProtKB.
DR   GO; GO:0042332; P:gravitaxis; IMP:FlyBase.
DR   GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
DR   GO; GO:0007489; P:maintenance of imaginal histoblast diploidy; IMP:UniProtKB.
DR   GO; GO:0032876; P:negative regulation of DNA endoreduplication; IMP: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:0007424; P:open tracheal system development; IMP:FlyBase.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0048076; P:regulation of compound eye pigmentation; IMP:FlyBase.
DR   GO; GO:2000177; P:regulation of neural precursor cell proliferation; IMP:FlyBase.
DR   GO; GO:0035094; P:response to nicotine; IMP:FlyBase.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
DR   GO; GO:0035220; P:wing disc development; IMP:UniProtKB.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; SSF57667; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   1: Evidence at protein level;
KW   Activator; Developmental protein; Differentiation; DNA-binding;
KW   Metal-binding; Neurogenesis; Nucleus; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..470
FT                   /note="Protein escargot"
FT                   /id="PRO_0000047027"
FT   ZN_FING         309..331
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         344..366
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         370..392
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         398..420
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         426..449
FT                   /note="C2H2-type 5; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          271..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         387
FT                   /note="G->E: In esg[VS8]; 50-fold reduction of affinity for
FT                   DNA binding."
FT                   /evidence="ECO:0000269|PubMed:7958894"
FT   CONFLICT        149
FT                   /note="Q -> P (in Ref. 1; AAA28513)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="I -> M (in Ref. 1; AAA28513)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        459
FT                   /note="S -> G (in Ref. 5; AAL49212)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   470 AA;  51963 MW;  E038F4DE991B5547 CRC64;
     MHTVEDMLVE KNYSKCPLKK RPVNYQFEAP QNHSNTPNEP QDLCVKKMEI LEENPSEELI
     NVSDCCEDEG VDVDHTDDEH IEEEDEDVDV DVDSDPNQTQ AAALAAAAAV AAAAAASVVV
     PTPTYPKYPW NNFHMSPYTA EFYRTINQQG HQILPLRGDL IAPSSPSDSL GSLSPPPHHY
     LHGRASSVSP PMRSEIIHRP IGVRQHRFLP YPQMPGYPSL GGYTHTHHHH APISPAYSEN
     SYYSMRSMTP ESSCSSSLPE DLSLKHKNLN LNLNTSQPGE QAAAKTGDMS PETMPNASAK
     KDKNQPPRYQ CPDCQKSYST FSGLTKHQQF HCPAAEGNQV KKSFSCKDCD KTYVSLGALK
     MHIRTHTLPC KCNLCGKAFS RPWLLQGHIR THTGEKPFSC QHCHRAFADR SNLRAHLQTH
     SDIKKYSCTS CSKTFSRMSL LTKHSEGGCP GGSAGSSSSS ELNYAGYAEP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024