NOTCH_DROME
ID NOTCH_DROME Reviewed; 2703 AA.
AC P07207; O97458; P04154; Q9W4T8;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 3.
DT 03-AUG-2022, entry version 255.
DE RecName: Full=Neurogenic locus Notch protein;
DE Contains:
DE RecName: Full=Processed neurogenic locus Notch protein;
DE Flags: Precursor;
GN Name=N; ORFNames=CG3936;
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 FUNCTION.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=3935325; DOI=10.1016/0092-8674(85)90229-6;
RA Wharton K.A., Johansen K.M., Xu T., Artavanis-Tsakonas S.;
RT "Nucleotide sequence from the neurogenic locus notch implies a gene product
RT that shares homology with proteins containing EGF-like repeats.";
RL Cell 43:567-581(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S, and Oregon-R; TISSUE=Embryo;
RX PubMed=3097517; DOI=10.1128/mcb.6.9.3094-3108.1986;
RA Kidd S., Kelley M.R., Young M.W.;
RT "Sequence of the notch locus of Drosophila melanogaster: relationship of
RT the encoded protein to mammalian clotting and growth factors.";
RL Mol. Cell. Biol. 6:3094-3108(1986).
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 GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RX PubMed=3037327; DOI=10.1128/mcb.7.4.1545-1548.1987;
RA Kelley M.R., Kidd S., Berg R.L., Young M.W.;
RT "Restriction of P-element insertions at the Notch locus of Drosophila
RT melanogaster.";
RL Mol. Cell. Biol. 7:1545-1548(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2505-2611.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=2981631; DOI=10.1016/0092-8674(85)90308-3;
RA Wharton K.A., Yedvobnick B., Finnerty V.G., Artavanis-Tsakonas S.;
RT "opa: a novel family of transcribed repeats shared by the Notch locus and
RT other developmentally regulated loci in D. melanogaster.";
RL Cell 40:55-62(1985).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2505-2604.
RX PubMed=2780284; DOI=10.1093/nar/17.16.6463;
RA Tautz D.;
RT "Hypervariability of simple sequences as a general source for polymorphic
RT DNA markers.";
RL Nucleic Acids Res. 17:6463-6471(1989).
RN [9]
RP INTERACTION WITH DX, AND MUTANT SU42C.
RX PubMed=8162848; DOI=10.1242/dev.120.3.473;
RA Diederich R.J., Matsuno K., Hing H., Artavanis-Tsakonas S.;
RT "Cytosolic interaction between deltex and Notch ankyrin repeats implicates
RT deltex in the Notch signaling pathway.";
RL Development 120:473-481(1994).
RN [10]
RP FUNCTION, AND INTERACTION WITH DX.
RX PubMed=7671825; DOI=10.1242/dev.121.8.2633;
RA Matsuno K., Diederich R.J., Go M.J., Blaumueller C.M.,
RA Artavanis-Tsakonas S.;
RT "Deltex acts as a positive regulator of Notch signaling through
RT interactions with the Notch ankyrin repeats.";
RL Development 121:2633-2644(1995).
RN [11]
RP S3 CLEAVAGE BY PSN.
RX PubMed=10206646; DOI=10.1038/19091;
RA Struhl G., Greenwald I.;
RT "Presenilin is required for activity and nuclear access of Notch in
RT Drosophila.";
RL Nature 398:522-525(1999).
RN [12]
RP S3 CLEAVAGE BY PSN.
RX PubMed=10206647; DOI=10.1038/19096;
RA Ye Y., Lukinova N., Fortini M.E.;
RT "Neurogenic phenotypes and altered Notch processing in Drosophila
RT Presenilin mutants.";
RL Nature 398:525-529(1999).
RN [13]
RP FUNCTION, INTERACTION WITH DL, AND GLYCOSYLATION.
RX PubMed=10935637; DOI=10.1038/35019075;
RA Bruckner K., Perez L., Clausen H., Cohen S.;
RT "Glycosyltransferase activity of Fringe modulates Notch-Delta
RT interactions.";
RL Nature 406:411-415(2000).
RN [14]
RP FUNCTION, AND MUTANT MCD5.
RX PubMed=11719214; DOI=10.1016/s0960-9822(01)00562-0;
RA Ramain P., Khechumian K., Seugnet L., Arbogast N., Ackermann C.,
RA Heitzler P.;
RT "Novel Notch alleles reveal a Deltex-dependent pathway repressing neural
RT fate.";
RL Curr. Biol. 11:1729-1738(2001).
RN [15]
RP S2 CLEAVAGE BY KUZ.
RX PubMed=11799064; DOI=10.1101/gad.942302;
RA Lieber T., Kidd S., Young M.W.;
RT "Kuzbanian-mediated cleavage of Drosophila Notch.";
RL Genes Dev. 16:209-221(2002).
RN [16]
RP FUNCTION, AND REVIEW.
RX PubMed=12369105; DOI=10.1034/j.1601-5223.2002.1360201.x;
RA Portin P.;
RT "General outlines of the molecular genetics of the Notch signalling pathway
RT in Drosophila melanogaster: a review.";
RL Hereditas 136:89-96(2002).
RN [17]
RP FUNCTION, GLYCOSYLATION, AND LIGAND-BINDING.
RX PubMed=12909620; DOI=10.1074/jbc.m308687200;
RA Okajima T., Xu A., Irvine K.D.;
RT "Modulation of notch-ligand binding by protein O-fucosyltransferase 1 and
RT fringe.";
RL J. Biol. Chem. 278:42340-42345(2003).
RN [18]
RP INTERACTION WITH NEDD4, UBIQUITINATION, AND MUTAGENESIS OF TYR-2328.
RX PubMed=15620649; DOI=10.1016/j.cub.2004.12.028;
RA Sakata T., Sakaguchi H., Tsuda L., Higashitani A., Aigaki T., Matsuno K.,
RA Hayashi S.;
RT "Drosophila Nedd4 regulates endocytosis of notch and suppresses its ligand-
RT independent activation.";
RL Curr. Biol. 14:2228-2236(2004).
RN [19]
RP FUNCTION, AND INTERACTION WITH SU(DX).
RX PubMed=15620650; DOI=10.1016/j.cub.2004.11.030;
RA Wilkin M.B., Carbery A.-M., Fostier M., Aslam H., Mazaleyrat S.L.,
RA Higgs J., Myat A., Evans D.A.P., Cornell M., Baron M.;
RT "Regulation of notch endosomal sorting and signaling by Drosophila Nedd4
RT family proteins.";
RL Curr. Biol. 14:2237-2244(2004).
RN [20]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH O-FUT1.
RX PubMed=17329366; DOI=10.1242/dev.02811;
RA Sasamura T., Ishikawa H.O., Sasaki N., Higashi S., Kanai M., Nakao S.,
RA Ayukawa T., Aigaki T., Noda K., Miyoshi E., Taniguchi N., Matsuno K.;
RT "The O-fucosyltransferase O-fut1 is an extracellular component that is
RT essential for the constitutive endocytic trafficking of Notch in
RT Drosophila.";
RL Development 134:1347-1356(2007).
RN [21]
RP FUNCTION, AND GLYCOSYLATION.
RX PubMed=18243100; DOI=10.1016/j.cell.2007.12.016;
RA Acar M., Jafar-Nejad H., Takeuchi H., Rajan A., Ibrani D., Rana N.A.,
RA Pan H., Haltiwanger R.S., Bellen H.J.;
RT "Rumi is a CAP10 domain glycosyltransferase that modifies Notch and is
RT required for Notch signaling.";
RL Cell 132:247-258(2008).
RN [22]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18342578; DOI=10.1016/j.devcel.2008.03.004;
RA Bowman S.K., Rolland V., Betschinger J., Kinsey K.A., Emery G.,
RA Knoblich J.A.;
RT "The tumor suppressors Brat and Numb regulate transit-amplifying neuroblast
RT lineages in Drosophila.";
RL Dev. Cell 14:535-546(2008).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2447, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [24]
RP FUNCTION.
RX PubMed=20152183; DOI=10.1016/j.devcel.2009.12.007;
RA Weng M., Golden K.L., Lee C.Y.;
RT "dFezf/Earmuff maintains the restricted developmental potential of
RT intermediate neural progenitors in Drosophila.";
RL Dev. Cell 18:126-135(2010).
RN [25]
RP FUNCTION.
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 [26]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23056424; DOI=10.1371/journal.pone.0046724;
RA Zhu S., Wildonger J., Barshow S., Younger S., Huang Y., Lee T.;
RT "The bHLH repressor Deadpan regulates the self-renewal and specification of
RT Drosophila larval neural stem cells independently of Notch.";
RL PLoS ONE 7:E46724-E46724(2012).
RN [27]
RP GLYCOSYLATION AT THR-72; THR-110; THR-153; SER-183; THR-191; THR-210;
RP SER-223; THR-231; THR-307; THR-348; THR-386; SER-427; THR-481; SER-494;
RP SER-502; THR-519; SER-532; SER-570; THR-595; SER-608; SER-645; SER-683;
RP THR-691; SER-721; SER-759; SER-797; THR-805; THR-822; THR-843; SER-922;
RP SER-952; THR-960; SER-990; THR-998; SER-1036; SER-1066; THR-1074; THR-1112;
RP SER-1189; THR-1197; THR-1235; SER-1273; SER-1303 AND SER-1381.
RX PubMed=27268051; DOI=10.1074/jbc.m116.732537;
RA Harvey B.M., Rana N.A., Moss H., Leonardi J., Jafar-Nejad H.,
RA Haltiwanger R.S.;
RT "Mapping sites of O-glycosylation and fringe elongation on Drosophila
RT Notch.";
RL J. Biol. Chem. 291:16348-16360(2016).
RN [28]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27151950; DOI=10.1242/dev.136184;
RA Li X., Xie Y., Zhu S.;
RT "Notch maintains Drosophila type II neuroblasts by suppressing expression
RT of the Fez transcription factor Earmuff.";
RL Development 143:2511-2521(2016).
RN [29]
RP FUNCTION.
RX PubMed=28899667; DOI=10.1016/j.ydbio.2017.09.011;
RA Li X., Chen R., Zhu S.;
RT "bHLH-O proteins balance the self-renewal and differentiation of Drosophila
RT neural stem cells by regulating Earmuff expression.";
RL Dev. Biol. 431:239-251(2017).
RN [30]
RP INTERACTION WITH AKAP200, AND UBIQUITINATION.
RX PubMed=29309414; DOI=10.1371/journal.pgen.1007153;
RA Bala Tannan N., Collu G., Humphries A.C., Serysheva E., Weber U.,
RA Mlodzik M.;
RT "AKAP200 promotes Notch stability by protecting it from Cbl/lysosome-
RT mediated degradation in Drosophila melanogaster.";
RL PLoS Genet. 14:E1007153-E1007153(2018).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1901-2139, DOMAIN ANK REPEATS, AND
RP SUBUNIT.
RX PubMed=14573873; DOI=10.1110/ps.03279003;
RA Zweifel M.E., Leahy D.J., Hughson F.M., Barrick D.;
RT "Structure and stability of the ankyrin domain of the Drosophila Notch
RT receptor.";
RL Protein Sci. 12:2622-2632(2003).
CC -!- FUNCTION: Essential signaling protein which has a major role in many
CC developmental processes (PubMed:3935325). Functions as a receptor for
CC membrane-bound ligands Delta and Serrate to regulate cell-fate
CC determination (PubMed:10935637, PubMed:15620650, PubMed:12909620,
CC PubMed:18243100). Upon ligand activation, and releasing from the cell
CC membrane, the Notch intracellular domain (NICD) forms a transcriptional
CC activator complex with Su(H) (Suppressor of hairless) and activates
CC genes of the E(spl) complex (PubMed:7671825). Regulates oogenesis, the
CC differentiation of the ectoderm and the development of the central and
CC peripheral nervous system, eye, wing disk, muscles and segmental
CC appendages such as antennae and legs, through lateral inhibition or
CC induction (PubMed:11719214, PubMed:12369105, PubMed:3935325). Regulates
CC neuroblast self-renewal, identity and proliferation through the
CC regulation of bHLH-O proteins; in larval brains, involved in the
CC maintenance of type II neuroblast self-renewal and identity by
CC suppressing erm expression together with pnt; might also regulate dpn
CC expression through the activation of the transcriptional regulator
CC Su(H) (PubMed:27151950, PubMed:28899667, PubMed:20152183,
CC PubMed:18342578, PubMed:23056424, PubMed:21262215).
CC {ECO:0000269|PubMed:10935637, ECO:0000269|PubMed:11719214,
CC ECO:0000269|PubMed:12369105, ECO:0000269|PubMed:12909620,
CC ECO:0000269|PubMed:15620650, ECO:0000269|PubMed:18243100,
CC ECO:0000269|PubMed:18342578, ECO:0000269|PubMed:20152183,
CC ECO:0000269|PubMed:21262215, ECO:0000269|PubMed:23056424,
CC ECO:0000269|PubMed:27151950, ECO:0000269|PubMed:28899667,
CC ECO:0000269|PubMed:7671825, ECO:0000303|PubMed:3935325}.
CC -!- SUBUNIT: Homomer. Interacts with Su(H) when activated. Interacts with
CC Dx via its ANK repeats. Interacts with Dl via the EGF repeats and the
CC Dl EGF repeats. Interacts with Nedd4 and Su(dx). Interacts with O-fut1;
CC the interaction glycosylates N and transports N to early endosomes.
CC Interacts with Akap200; the interaction stabilizes N/Notch protein
CC levels by preventing Cbl-mediated ubiquitination and subsequent
CC lysosomal degradation of N/Notch (PubMed:29309414).
CC {ECO:0000269|PubMed:10935637, ECO:0000269|PubMed:14573873,
CC ECO:0000269|PubMed:15620649, ECO:0000269|PubMed:15620650,
CC ECO:0000269|PubMed:17329366, ECO:0000269|PubMed:29309414,
CC ECO:0000269|PubMed:7671825, ECO:0000269|PubMed:8162848}.
CC -!- INTERACTION:
CC P07207; Q24279: cno; NbExp=3; IntAct=EBI-103438, EBI-868783;
CC P07207; P10041: Dl; NbExp=2; IntAct=EBI-103438, EBI-115346;
CC P07207; Q23985: dx; NbExp=4; IntAct=EBI-103438, EBI-190618;
CC P07207; P28159: Su(H); NbExp=7; IntAct=EBI-103438, EBI-92180;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17329366};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:17329366}.
CC Endosome {ECO:0000269|PubMed:17329366}. Note=Transported to early
CC endosomes by O-fut1 (PubMed:17329366).
CC -!- SUBCELLULAR LOCATION: [Processed neurogenic locus Notch protein]:
CC Nucleus. Note=Upon activation and S3 cleavage, it is released from the
CC cell membrane and enters into the nucleus in conjunction with Su(H).
CC -!- DOMAIN: Crystal structure of the ANK repeat domain shows that there are
CC 7 repeats and the stabilizing C-terminal repeat enhances the protein
CC stability by extending the ankyrin domain.
CC {ECO:0000269|PubMed:14573873}.
CC -!- PTM: Upon binding its ligands such as Delta or Serrate, it is cleaved
CC (S2 cleavage) in its extracellular domain, close to the transmembrane
CC domain. S2 cleavage is probably mediated by Kuz. It is then cleaved (S3
CC cleavage) downstream of its transmembrane domain, releasing it from the
CC cell membrane. S3 cleavage requires Psn.
CC -!- PTM: O-glycosylated (PubMed:27268051). Three forms of O-glycosylation
CC (O-fucosylation, O-glucosylation and O-GlcNAcylation) are detected
CC (PubMed:27268051). O-fucosylated by O-fut1 and fng in the EGF repeat
CC domain inhibits both Serrate/Ser- and Delta/Dl-binding
CC (PubMed:12909620, PubMed:10935637). O-glucosylation by rumi in the
CC endoplasmic reticulum is necessary for correct folding and signaling
CC (PubMed:18243100). {ECO:0000269|PubMed:10935637,
CC ECO:0000269|PubMed:12909620, ECO:0000269|PubMed:18243100,
CC ECO:0000269|PubMed:27268051}.
CC -!- PTM: Ubiquitinated by Nedd4; which promotes ligand-independent
CC endocytosis and proteasomal degradation. May also be ubiquitinated by
CC Su(dx) and Cbl. {ECO:0000269|PubMed:15620649,
CC ECO:0000269|PubMed:29309414}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the larval brain
CC neuroblasts abolishes the expression of pnt, induces the ectopic
CC expression of erm, results in the ectopic expression of Ase in type II
CC neuroblasts (NBs) and their premature loss (PubMed:18342578,
CC PubMed:23056424, PubMed:27151950). Simultaneous RNAi-mediated knockdown
CC of pnt partially restores normal neuroblast numbers and inhibits
CC ectopic erm expression (PubMed:27151950). {ECO:0000269|PubMed:18342578,
CC ECO:0000269|PubMed:23056424, ECO:0000269|PubMed:27151950}.
CC -!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
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DR EMBL; M16152; AAB59220.1; -; Genomic_DNA.
DR EMBL; M16153; AAB59220.1; JOINED; Genomic_DNA.
DR EMBL; M16149; AAB59220.1; JOINED; Genomic_DNA.
DR EMBL; M16150; AAB59220.1; JOINED; Genomic_DNA.
DR EMBL; M16151; AAB59220.1; JOINED; Genomic_DNA.
DR EMBL; K03508; AAA28725.1; -; Genomic_DNA.
DR EMBL; M13689; AAA28725.1; JOINED; Genomic_DNA.
DR EMBL; K03507; AAA28725.1; JOINED; Genomic_DNA.
DR EMBL; AE014298; AAF45848.2; -; Genomic_DNA.
DR EMBL; AL035436; CAB37610.1; -; Genomic_DNA.
DR EMBL; AL035395; CAB37610.1; JOINED; Genomic_DNA.
DR EMBL; M16025; AAA28726.1; -; Genomic_DNA.
DR EMBL; M12175; AAA74496.1; -; Genomic_DNA.
DR PIR; A24420; A24420.
DR RefSeq; NP_001245510.1; NM_001258581.2.
DR RefSeq; NP_476859.2; NM_057511.4.
DR PDB; 1OT8; X-ray; 2.00 A; A/B/C=1902-2139.
DR PDB; 2JMF; NMR; -; B=2318-2333.
DR PDB; 7ALJ; X-ray; 1.52 A; A=449-564.
DR PDBsum; 1OT8; -.
DR PDBsum; 2JMF; -.
DR PDBsum; 7ALJ; -.
DR SMR; P07207; -.
DR BioGRID; 57823; 309.
DR DIP; DIP-5N; -.
DR IntAct; P07207; 229.
DR MINT; P07207; -.
DR STRING; 7227.FBpp0070483; -.
DR GlyGen; P07207; 55 sites.
DR iPTMnet; P07207; -.
DR PaxDb; P07207; -.
DR DNASU; 31293; -.
DR EnsemblMetazoa; FBtr0070507; FBpp0070483; FBgn0004647.
DR EnsemblMetazoa; FBtr0304659; FBpp0293201; FBgn0004647.
DR GeneID; 31293; -.
DR KEGG; dme:Dmel_CG3936; -.
DR CTD; 31293; -.
DR FlyBase; FBgn0004647; N.
DR VEuPathDB; VectorBase:FBgn0004647; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00980000198606; -.
DR HOGENOM; CLU_000576_0_1_1; -.
DR InParanoid; P07207; -.
DR OMA; IAGYSCE; -.
DR OrthoDB; 7525at2759; -.
DR PhylomeDB; P07207; -.
DR Reactome; R-DME-1474228; Degradation of the extracellular matrix.
DR Reactome; R-DME-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-DME-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-DME-2022857; Keratan sulfate degradation.
DR Reactome; R-DME-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-DME-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-DME-2024101; CS/DS degradation.
DR Reactome; R-DME-3000178; ECM proteoglycans.
DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR SignaLink; P07207; -.
DR BioGRID-ORCS; 31293; 0 hits in 3 CRISPR screens.
DR ChiTaRS; N; fly.
DR EvolutionaryTrace; P07207; -.
DR GenomeRNAi; 31293; -.
DR PRO; PR:P07207; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004647; Expressed in wing disc and 30 other tissues.
DR ExpressionAtlas; P07207; baseline and differential.
DR Genevisible; P07207; DM.
DR GO; GO:0005912; C:adherens junction; IMP:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IMP:FlyBase.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:1990433; C:CSL-Notch-Mastermind transcription factor complex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IDA:FlyBase.
DR GO; GO:0030139; C:endocytic vesicle; IDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IMP:FlyBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:FlyBase.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005770; C:late endosome; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:FlyBase.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:FlyBase.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:FlyBase.
DR GO; GO:0050699; F:WW domain binding; IDA:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0008356; P:asymmetric cell division; TAS:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0043697; P:cell dedifferentiation; IGI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IMP:FlyBase.
DR GO; GO:0045165; P:cell fate commitment; IMP:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
DR GO; GO:0060289; P:compartment boundary maintenance; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0046667; P:compound eye retinal cell programmed cell death; TAS:FlyBase.
DR GO; GO:0042688; P:crystal cell differentiation; IMP:FlyBase.
DR GO; GO:0002213; P:defense response to insect; IDA:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; TAS:FlyBase.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:FlyBase.
DR GO; GO:0061331; P:epithelial cell proliferation involved in Malpighian tubule morphogenesis; IMP:FlyBase.
DR GO; GO:0035153; P:epithelial cell type specification, open tracheal system; IMP:FlyBase.
DR GO; GO:0035214; P:eye-antennal disc development; IMP:FlyBase.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0036099; P:female germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007440; P:foregut morphogenesis; IMP:FlyBase.
DR GO; GO:0060288; P:formation of a compartment boundary; IMP:FlyBase.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0010001; P:glial cell differentiation; IMP:FlyBase.
DR GO; GO:0007403; P:glial cell fate determination; IMP:FlyBase.
DR GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR GO; GO:0035172; P:hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0016348; P:imaginal disc-derived leg joint morphogenesis; IMP:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0036011; P:imaginal disc-derived leg segmentation; IMP:FlyBase.
DR GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase.
DR GO; GO:0035171; P:lamellocyte differentiation; IMP:FlyBase.
DR GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
DR GO; GO:0046331; P:lateral inhibition; TAS:FlyBase.
DR GO; GO:0007478; P:leg disc morphogenesis; TAS:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0048542; P:lymph gland development; IMP:FlyBase.
DR GO; GO:0061382; P:Malpighian tubule tip cell differentiation; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; IMP:FlyBase.
DR GO; GO:0060571; P:morphogenesis of an epithelial fold; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
DR GO; GO:0007521; P:muscle cell fate determination; IMP:FlyBase.
DR GO; GO:0048627; P:myoblast development; IEP:FlyBase.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; IMP:FlyBase.
DR GO; GO:0045316; P:negative regulation of compound eye photoreceptor development; IMP:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0035204; P:negative regulation of lamellocyte differentiation; IMP:FlyBase.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:FlyBase.
DR GO; GO:0050877; P:nervous system process; IMP:FlyBase.
DR GO; GO:0014019; P:neuroblast development; IMP:UniProtKB.
DR GO; GO:0007400; P:neuroblast fate determination; IDA:FlyBase.
DR GO; GO:0014018; P:neuroblast fate specification; IMP:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0048664; P:neuron fate determination; IMP:FlyBase.
DR GO; GO:0048665; P:neuron fate specification; IMP:FlyBase.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:FlyBase.
DR GO; GO:0030720; P:oocyte localization involved in germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0007297; P:ovarian follicle cell migration; IMP:FlyBase.
DR GO; GO:0030713; P:ovarian follicle cell stalk formation; IMP:FlyBase.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0042691; P:positive regulation of crystal cell differentiation; IMP:FlyBase.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:FlyBase.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0048052; P:R1/R6 cell differentiation; 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:0042686; P:regulation of cardioblast cell fate specification; IMP:FlyBase.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:FlyBase.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0006110; P:regulation of glycolytic process; IMP:FlyBase.
DR GO; GO:0040008; P:regulation of growth; IMP:FlyBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; TAS:FlyBase.
DR GO; GO:1902692; P:regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:FlyBase.
DR GO; GO:2000035; P:regulation of stem cell division; IMP:FlyBase.
DR GO; GO:0009608; P:response to symbiont; IMP:FlyBase.
DR GO; GO:0046666; P:retinal cell programmed cell death; TAS:FlyBase.
DR GO; GO:0016330; P:second mitotic wave involved in compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
DR GO; GO:0016360; P:sensory organ precursor cell fate determination; IMP:FlyBase.
DR GO; GO:0048863; P:stem cell differentiation; IMP:FlyBase.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0035222; P:wing disc pattern formation; IMP:FlyBase.
DR Gene3D; 1.25.40.20; -; 1.
DR IDEAL; IID50157; -.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR008297; Notch.
DR InterPro; IPR035993; Notch-like_dom_sf.
DR InterPro; IPR024600; Notch_C.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR010660; Notch_NOD_dom.
DR InterPro; IPR011656; Notch_NODP_dom.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00008; EGF; 24.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF06816; NOD; 1.
DR Pfam; PF07684; NODP; 1.
DR Pfam; PF00066; Notch; 3.
DR PIRSF; PIRSF002279; Notch; 1.
DR PRINTS; PR01452; LNOTCHREPEAT.
DR SMART; SM00248; ANK; 7.
DR SMART; SM01334; DUF3454; 1.
DR SMART; SM00181; EGF; 36.
DR SMART; SM00179; EGF_CA; 33.
DR SMART; SM00004; NL; 3.
DR SMART; SM01338; NOD; 1.
DR SMART; SM01339; NODP; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57184; SSF57184; 5.
DR SUPFAM; SSF90193; SSF90193; 3.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS00010; ASX_HYDROXYL; 22.
DR PROSITE; PS00022; EGF_1; 34.
DR PROSITE; PS01186; EGF_2; 28.
DR PROSITE; PS50026; EGF_3; 36.
DR PROSITE; PS01187; EGF_CA; 21.
DR PROSITE; PS50258; LNR; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ANK repeat; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; EGF-like domain; Endosome; Glycoprotein;
KW Membrane; Neurogenesis; Notch signaling pathway; Nucleus; Oogenesis;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..52
FT /evidence="ECO:0000255"
FT CHAIN 53..2703
FT /note="Neurogenic locus Notch protein"
FT /id="PRO_0000007673"
FT CHAIN ?..2703
FT /note="Processed neurogenic locus Notch protein"
FT /id="PRO_0000296234"
FT TOPO_DOM 53..1745
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1746..1766
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1767..2703
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..95
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 96..136
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 139..176
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 177..215
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 217..253
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 255..291
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 293..329
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 331..370
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 372..408
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 409..447
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 449..486
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 488..524
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 526..562
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 564..600
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 602..637
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 639..675
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 677..713
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 715..751
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 753..789
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 791..827
FT /note="EGF-like 20; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 829..865
FT /note="EGF-like 21; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 867..905
FT /note="EGF-like 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 907..944
FT /note="EGF-like 23; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 946..982
FT /note="EGF-like 24; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 984..1020
FT /note="EGF-like 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1022..1058
FT /note="EGF-like 26; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1060..1096
FT /note="EGF-like 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1098..1134
FT /note="EGF-like 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1136..1181
FT /note="EGF-like 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1183..1219
FT /note="EGF-like 30; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1221..1257
FT /note="EGF-like 31; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1259..1295
FT /note="EGF-like 32; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1297..1335
FT /note="EGF-like 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1337..1373
FT /note="EGF-like 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1375..1412
FT /note="EGF-like 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1415..1451
FT /note="EGF-like 36"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 1482..1521
FT /note="LNR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT REPEAT 1522..1557
FT /note="LNR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT REPEAT 1559..1599
FT /note="LNR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT REPEAT 1901..1945
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 1950..1979
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 1983..2013
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 2017..2046
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 2050..2079
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 2083..2112
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 2116..2139
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REGION 1810..1850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2172..2257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2325..2328
FT /note="Interaction with Nedd4"
FT REGION 2399..2452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2488..2524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2579..2620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2632..2703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2172..2199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2224..2248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2402..2433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2588..2620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2632..2692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2447
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 72
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 110
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 153
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 183
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 191
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 210
FT /note="O-linked (GlcNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 223
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 231
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 307
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 427
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="O-linked (GlcNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 494
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 502
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 519
FT /note="O-linked (GlcNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 532
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 570
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 595
FT /note="O-linked (GlcNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 608
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 645
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 683
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 691
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 721
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 759
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 797
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 805
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 822
FT /note="O-linked (GlcNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 843
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 922
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 952
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 960
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 990
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 998
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 1036
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 1045
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1066
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 1074
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 1112
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 1157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1189
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 1197
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 1235
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 1242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1273
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 1303
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 1381
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:27268051"
FT CARBOHYD 1521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 67..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 85..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 100..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 105..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 126..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 143..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 148..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 166..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 181..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 186..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 205..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 221..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 226..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 243..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 259..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 264..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 281..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 297..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 302..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 319..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 335..349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 343..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 360..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 376..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 381..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 398..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 413..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 418..435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 437..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 453..465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 459..474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 476..485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 492..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 497..512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 514..523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 530..541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 535..550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 552..561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 568..579
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 573..588
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 590..599
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 606..616
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 611..625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 627..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 643..654
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 648..663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 665..674
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 681..692
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 686..701
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 703..712
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 719..730
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 724..739
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 741..750
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 757..768
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 762..777
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 779..788
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 795..806
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 800..815
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 817..826
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 833..844
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 838..853
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 855..864
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 871..882
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 876..893
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 895..904
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 911..923
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 917..932
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 934..943
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 950..961
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 955..970
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 972..981
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 988..999
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 993..1008
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1010..1019
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1026..1037
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1031..1046
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1048..1057
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1064..1075
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1069..1084
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1086..1095
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1102..1113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1107..1122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1124..1133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1155..1160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1171..1180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1187..1198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1192..1207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1209..1218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1225..1236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1230..1245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1247..1256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1263..1274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1268..1283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1285..1294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1301..1314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1306..1323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1325..1334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1341..1352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1346..1361
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1363..1372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1379..1389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1384..1400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1402..1411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1419..1430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1424..1439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1441..1450
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1482..1505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 1487..1500
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 1496..1512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 1522..1545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 1527..1540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 1536..1552
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 1559..1585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 1567..1580
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 1576..1592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT VARIANT 578
FT /note="I -> T"
FT VARIANT 2044
FT /note="I -> R"
FT VARIANT 2265
FT /note="A -> V"
FT VARIANT 2407
FT /note="H -> R"
FT VARIANT 2445
FT /note="R -> L"
FT VARIANT 2568
FT /note="Q -> QQQQQ"
FT MUTAGEN 739
FT /note="C->Y: In mcd5; induces loss of microchaetae sensory
FT precursors."
FT MUTAGEN 2060
FT /note="A->V: In su42c; deltex-like mutation that induces
FT outstreched wings and variability-fused ocelli."
FT MUTAGEN 2328
FT /note="Y->F: Abolishes interaction with Nedd4 and reduces
FT ubiquitination."
FT /evidence="ECO:0000269|PubMed:15620649"
FT CONFLICT 9
FT /note="R -> G (in Ref. 5; CAB37610)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="A -> G (in Ref. 5; CAB37610)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="M -> I (in Ref. 1; AAB59220)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="R -> H (in Ref. 2; AAA28725)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="T -> I (in Ref. 1; AAB59220)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="Q -> R (in Ref. 5; CAB37610)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="G -> A (in Ref. 1; AAB59220)"
FT /evidence="ECO:0000305"
FT CONFLICT 1561
FT /note="S -> T (in Ref. 1; AAB59220 and 2; AAA28725)"
FT /evidence="ECO:0000305"
FT CONFLICT 2257
FT /note="G -> S (in Ref. 2; AAA28725)"
FT /evidence="ECO:0000305"
FT CONFLICT 2577
FT /note="A -> E (in Ref. 7; AAA74496)"
FT /evidence="ECO:0000305"
FT STRAND 464..468
FT /evidence="ECO:0007829|PDB:7ALJ"
FT STRAND 471..475
FT /evidence="ECO:0007829|PDB:7ALJ"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:7ALJ"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:7ALJ"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:7ALJ"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:7ALJ"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:7ALJ"
FT HELIX 529..532
FT /evidence="ECO:0007829|PDB:7ALJ"
FT STRAND 540..544
FT /evidence="ECO:0007829|PDB:7ALJ"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:7ALJ"
FT HELIX 1930..1950
FT /evidence="ECO:0007829|PDB:1OT8"
FT HELIX 1954..1960
FT /evidence="ECO:0007829|PDB:1OT8"
FT HELIX 1964..1972
FT /evidence="ECO:0007829|PDB:1OT8"
FT HELIX 1987..1993
FT /evidence="ECO:0007829|PDB:1OT8"
FT HELIX 1997..2004
FT /evidence="ECO:0007829|PDB:1OT8"
FT HELIX 2021..2027
FT /evidence="ECO:0007829|PDB:1OT8"
FT HELIX 2033..2039
FT /evidence="ECO:0007829|PDB:1OT8"
FT HELIX 2054..2060
FT /evidence="ECO:0007829|PDB:1OT8"
FT HELIX 2064..2072
FT /evidence="ECO:0007829|PDB:1OT8"
FT HELIX 2087..2093
FT /evidence="ECO:0007829|PDB:1OT8"
FT HELIX 2097..2105
FT /evidence="ECO:0007829|PDB:1OT8"
FT HELIX 2120..2126
FT /evidence="ECO:0007829|PDB:1OT8"
FT HELIX 2130..2136
FT /evidence="ECO:0007829|PDB:1OT8"
SQ SEQUENCE 2703 AA; 288853 MW; 0EAE23F426FECD7B CRC64;
MQSQRSRRRS RAPNTWICFW INKMHAVASL PASLPLLLLT LAFANLPNTV RGTDTALVAA
SCTSVGCQNG GTCVTQLNGK TYCACDSHYV GDYCEHRNPC NSMRCQNGGT CQVTFRNGRP
GISCKCPLGF DESLCEIAVP NACDHVTCLN GGTCQLKTLE EYTCACANGY TGERCETKNL
CASSPCRNGA TCTALAGSSS FTCSCPPGFT GDTCSYDIEE CQSNPCKYGG TCVNTHGSYQ
CMCPTGYTGK DCDTKYKPCS PSPCQNGGIC RSNGLSYECK CPKGFEGKNC EQNYDDCLGH
LCQNGGTCID GISDYTCRCP PNFTGRFCQD DVDECAQRDH PVCQNGATCT NTHGSYSCIC
VNGWAGLDCS NNTDDCKQAA CFYGATCIDG VGSFYCQCTK GKTGLLCHLD DACTSNPCHA
DAICDTSPIN GSYACSCATG YKGVDCSEDI DECDQGSPCE HNGICVNTPG SYRCNCSQGF
TGPRCETNIN ECESHPCQNE GSCLDDPGTF RCVCMPGFTG TQCEIDIDEC QSNPCLNDGT
CHDKINGFKC SCALGFTGAR CQINIDDCQS QPCRNRGICH DSIAGYSCEC PPGYTGTSCE
ININDCDSNP CHRGKCIDDV NSFKCLCDPG YTGYICQKQI NECESNPCQF DGHCQDRVGS
YYCQCQAGTS GKNCEVNVNE CHSNPCNNGA TCIDGINSYK CQCVPGFTGQ HCEKNVDECI
SSPCANNGVC IDQVNGYKCE CPRGFYDAHC LSDVDECASN PCVNEGRCED GINEFICHCP
PGYTGKRCEL DIDECSSNPC QHGGTCYDKL NAFSCQCMPG YTGQKCETNI DDCVTNPCGN
GGTCIDKVNG YKCVCKVPFT GRDCESKMDP CASNRCKNEA KCTPSSNFLD FSCTCKLGYT
GRYCDEDIDE CSLSSPCRNG ASCLNVPGSY RCLCTKGYEG RDCAINTDDC ASFPCQNGGT
CLDGIGDYSC LCVDGFDGKH CETDINECLS QPCQNGATCS QYVNSYTCTC PLGFSGINCQ
TNDEDCTESS CLNGGSCIDG INGYNCSCLA GYSGANCQYK LNKCDSNPCL NGATCHEQNN
EYTCHCPSGF TGKQCSEYVD WCGQSPCENG ATCSQMKHQF SCKCSAGWTG KLCDVQTISC
QDAADRKGLS LRQLCNNGTC KDYGNSHVCY CSQGYAGSYC QKEIDECQSQ PCQNGGTCRD
LIGAYECQCR QGFQGQNCEL NIDDCAPNPC QNGGTCHDRV MNFSCSCPPG TMGIICEINK
DDCKPGACHN NGSCIDRVGG FECVCQPGFV GARCEGDINE CLSNPCSNAG TLDCVQLVNN
YHCNCRPGHM GRHCEHKVDF CAQSPCQNGG NCNIRQSGHH CICNNGFYGK NCELSGQDCD
SNPCRVGNCV VADEGFGYRC ECPRGTLGEH CEIDTLDECS PNPCAQGAAC EDLLGDYECL
CPSKWKGKRC DIYDANYPGW NGGSGSGNDR YAADLEQQRA MCDKRGCTEK QGNGICDSDC
NTYACNFDGN DCSLGINPWA NCTANECWNK FKNGKCNEEC NNAACHYDGH DCERKLKSCD
SLFDAYCQKH YGDGFCDYGC NNAECSWDGL DCENKTQSPV LAEGAMSVVM LMNVEAFREI
QAQFLRNMSH MLRTTVRLKK DALGHDIIIN WKDNVRVPEI EDTDFARKNK ILYTQQVHQT
GIQIYLEIDN RKCTECFTHA VEAAEFLAAT AAKHQLRNDF QIHSVRGIKN PGDEDNGEPP
ANVKYVITGI ILVIIALAFF GMVLSTQRKR AHGVTWFPEG FRAPAAVMSR RRRDPHGQEM
RNLNKQVAMQ SQGVGQPGAH WSDDESDMPL PKRQRSDPVS GVGLGNNGGY ASDHTMVSEY
EEADQRVWSQ AHLDVVDVRA IMTPPAHQDG GKHDVDARGP CGLTPLMIAA VRGGGLDTGE
DIENNEDSTA QVISDLLAQG AELNATMDKT GETSLHLAAR FARADAAKRL LDAGADANCQ
DNTGRTPLHA AVAADAMGVF QILLRNRATN LNARMHDGTT PLILAARLAI EGMVEDLITA
DADINAADNS GKTALHWAAA VNNTEAVNIL LMHHANRDAQ DDKDETPLFL AAREGSYEAC
KALLDNFANR EITDHMDRLP RDVASERLHH DIVRLLDEHV PRSPQMLSMT PQAMIGSPPP
GQQQPQLITQ PTVISAGNGG NNGNGNASGK QSNQTAKQKA AKKAKLIEGS PDNGLDATGS
LRRKASSKKT SAASKKAANL NGLNPGQLTG GVSGVPGVPP TNSAAQAAAA AAAAVAAMSH
ELEGSPVGVG MGGNLPSPYD TSSMYSNAMA APLANGNPNT GAKQPPSYED CIKNAQSMQS
LQGNGLDMIK LDNYAYSMGS PFQQELLNGQ GLGMNGNGQR NGVGPGVLPG GLCGMGGLSG
AGNGNSHEQG LSPPYSNQSP PHSVQSSLAL SPHAYLGSPS PAKSRPSLPT SPTHIQAMRH
ATQQKQFGGS NLNSLLGGAN GGGVVGGGGG GGGGVGQGPQ NSPVSLGIIS PTGSDMGIML
APPQSSKNSA IMQTISPQQQ QQQQQQQQQQ HQQQQQQQQQ QQQQQQQQLG GLEFGSAGLD
LNGFCGSPDS FHSGQMNPPS IQSSMSGSSP STNMLSPSSQ HNQQAFYQYL TPSSQHSGGH
TPQHLVQTLD SYPTPSPESP GHWSSSSPRS NSDWSEGVQS PAANNLYISG GHQANKGSEA
IYI
