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Database: UniProt
Entry: P07207
LinkDB: P07207
Original site: P07207 
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   13-FEB-2019, entry version 235.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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
RT   product that shares homology with proteins containing EGF-like
RT   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;
RA   Kidd S., Kelley M.R., Young M.W.;
RT   "Sequence of the notch locus of Drosophila melanogaster: relationship
RT   of 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E.,
RA   Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D.,
RA   Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S.,
RA   Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B.,
RA   Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F.,
RA   Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A.,
RA   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;
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
RT   and 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
RT   polymorphic DNA markers.";
RL   Nucleic Acids Res. 17:6463-6471(1989).
RN   [9]
RP   INTERACTION WITH DX, AND MUTANT SU42C.
RX   PubMed=8162848;
RA   Diederich R.J., Matsuno K., Hing H., Artavanis-Tsakonas S.;
RT   "Cytosolic interaction between deltex and Notch ankyrin repeats
RT   implicates deltex in the Notch signaling pathway.";
RL   Development 120:473-481(1994).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH DX.
RX   PubMed=7671825;
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
RT   neural 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
RT   pathway 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
RT   and 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.,
RA   Matsuno K., Hayashi S.;
RT   "Drosophila Nedd4 regulates endocytosis of notch and suppresses its
RT   ligand-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
RT   Nedd4 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
RT   neuroblast lineages in Drosophila.";
RL   Dev. Cell 14:535-546(2008).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2447, AND IDENTIFICATION
RP   BY 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
RT   specification of Drosophila larval neural stem cells independently of
RT   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;
RP   SER-494; SER-502; THR-519; SER-532; SER-570; THR-595; SER-608;
RP   SER-645; SER-683; THR-691; SER-721; SER-759; SER-797; THR-805;
RP   THR-822; THR-843; SER-922; SER-952; THR-960; SER-990; THR-998;
RP   SER-1036; SER-1066; THR-1074; THR-1112; SER-1189; THR-1197; THR-1235;
RP   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
RT   expression 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
RT   Drosophila 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
RP   REPEATS, AND 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
CC       many developmental processes (PubMed:3935325). Functions as a
CC       receptor for membrane-bound ligands Delta and Serrate to regulate
CC       cell-fate determination (PubMed:10935637, PubMed:15620650,
CC       PubMed:12909620, PubMed:18243100). Upon ligand activation, and
CC       releasing from the cell membrane, the Notch intracellular domain
CC       (NICD) forms a transcriptional activator complex with Su(H)
CC       (Suppressor of hairless) and activates genes of the E(spl) complex
CC       (PubMed:7671825). Regulates oogenesis, the differentiation of the
CC       ectoderm and the development of the central and peripheral nervous
CC       system, eye, wing disk, muscles and segmental appendages such as
CC       antennae and legs, through lateral inhibition or induction
CC       (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
CC       dpn expression through the activation of the transcriptional
CC       regulator Su(H) (PubMed:27151950, PubMed:28899667,
CC       PubMed:20152183, PubMed:18342578, PubMed:23056424,
CC       PubMed:21262215). {ECO:0000269|PubMed:10935637,
CC       ECO:0000269|PubMed:11719214, ECO:0000269|PubMed:12369105,
CC       ECO:0000269|PubMed:12909620, ECO:0000269|PubMed:15620650,
CC       ECO:0000269|PubMed:18243100, ECO:0000269|PubMed:18342578,
CC       ECO:0000269|PubMed:20152183, ECO:0000269|PubMed:21262215,
CC       ECO:0000269|PubMed:23056424, ECO:0000269|PubMed:27151950,
CC       ECO:0000269|PubMed:28899667, ECO:0000269|PubMed:7671825,
CC       ECO:0000303|PubMed:3935325}.
CC   -!- SUBUNIT: Homomer. Interacts with Su(H) when activated. Interacts
CC       with Dx via its ANK repeats. Interacts with Dl via the EGF repeats
CC       and the Dl EGF repeats. Interacts with Nedd4 and Su(dx). Interacts
CC       with O-fut1; the interaction glycosylates N and transports N to
CC       early endosomes. Interacts with Akap200; the interaction
CC       stabilizes N/Notch protein levels by preventing Cbl-mediated
CC       ubiquitination and subsequent lysosomal degration of N/Notch
CC       (PubMed:29309414). {ECO:0000269|PubMed:10935637,
CC       ECO:0000269|PubMed:14573873, ECO:0000269|PubMed:15620649,
CC       ECO:0000269|PubMed:15620650, ECO:0000269|PubMed:17329366,
CC       ECO:0000269|PubMed:29309414, ECO:0000269|PubMed:7671825,
CC       ECO:0000269|PubMed:8162848}.
CC   -!- INTERACTION:
CC       Q24279:cno; NbExp=3; IntAct=EBI-103438, EBI-868783;
CC       P10041:Dl; NbExp=2; IntAct=EBI-103438, EBI-115346;
CC       Q23985:dx; NbExp=4; IntAct=EBI-103438, EBI-190618;
CC       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
CC       the cell membrane and enters into the nucleus in conjunction with
CC       Su(H).
CC   -!- DOMAIN: Crystal structure of the ANK repeat domain shows that
CC       there are 7 repeats and the stabilizing C-terminal repeat enhances
CC       the protein stability by extending the ankyrin domain.
CC       {ECO:0000269|PubMed:14573873}.
CC   -!- PTM: Upon binding its ligands such as Delta or Serrate, it is
CC       cleaved (S2 cleavage) in its extracellular domain, close to the
CC       transmembrane domain. S2 cleavage is probably mediated by Kuz. It
CC       is then cleaved (S3 cleavage) downstream of its transmembrane
CC       domain, releasing it from the cell membrane. S3 cleavage requires
CC       Psn.
CC   -!- PTM: O-glycosylated (PubMed:27268051). Three forms of O-
CC       glycosylation (O-fucosylation, O-glucosylation and O-
CC       GlcNAcylation) are detected (PubMed:27268051). O-fucosylated by O-
CC       fut1 and fng in the EGF repeat domain inhibits both
CC       Serrate/Ser- and Delta/Dl-binding (PubMed:12909620,
CC       PubMed:10935637). O-glucosylation by rumi in the endoplasmic
CC       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
CC       by 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
CC       type II neuroblasts (NBs) and their premature loss
CC       (PubMed:18342578, PubMed:23056424, PubMed:27151950). Simultaneous
CC       RNAi-mediated knockdown of pnt partially restores normal
CC       neuroblast numbers and inhibits ectopic erm expression
CC       (PubMed:27151950). {ECO:0000269|PubMed:18342578,
CC       ECO:0000269|PubMed:23056424, ECO:0000269|PubMed:27151950}.
CC   -!- SIMILARITY: Belongs to the NOTCH family. {ECO:0000305}.
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   PDBsum; 1OT8; -.
DR   PDBsum; 2JMF; -.
DR   ProteinModelPortal; P07207; -.
DR   SMR; P07207; -.
DR   BioGrid; 57823; 304.
DR   DIP; DIP-5N; -.
DR   IntAct; P07207; 231.
DR   MINT; P07207; -.
DR   STRING; 7227.FBpp0070483; -.
DR   iPTMnet; P07207; -.
DR   PaxDb; P07207; -.
DR   PRIDE; P07207; -.
DR   EnsemblMetazoa; FBtr0070507; FBpp0070483; FBgn0004647.
DR   EnsemblMetazoa; FBtr0304659; FBpp0293201; FBgn0004647.
DR   GeneID; 31293; -.
DR   KEGG; dme:Dmel_CG3936; -.
DR   CTD; 109544; -.
DR   FlyBase; FBgn0004647; N.
DR   eggNOG; ENOG410IR7G; Eukaryota.
DR   eggNOG; COG0666; LUCA.
DR   GeneTree; ENSGT00940000167944; -.
DR   InParanoid; P07207; -.
DR   KO; K02599; -.
DR   OMA; GRDCESK; -.
DR   OrthoDB; 7525at2759; -.
DR   PhylomeDB; P07207; -.
DR   Reactome; R-DME-1912420; Pre-NOTCH Processing in Golgi.
DR   Reactome; R-DME-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   Reactome; R-DME-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
DR   Reactome; R-DME-8941856; RUNX3 regulates NOTCH signaling.
DR   Reactome; R-DME-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR   Reactome; R-DME-9013700; NOTCH4 Activation and Transmission of Signal to the Nucleus.
DR   Reactome; R-DME-9017802; Noncanonical activation of NOTCH3.
DR   Reactome; R-DME-9604323; Negative regulation of NOTCH4 signaling.
DR   SignaLink; P07207; -.
DR   ChiTaRS; N; fly.
DR   EvolutionaryTrace; P07207; -.
DR   GenomeRNAi; 31293; -.
DR   PRO; PR:P07207; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0004647; Expressed in 30 organ(s), highest expression level in embryo.
DR   ExpressionAtlas; P07207; differential.
DR   Genevisible; P07207; DM.
DR   GO; GO:0005912; C:adherens junction; IDA:FlyBase.
DR   GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR   GO; GO:1990433; C:CSL-Notch-Mastermind transcription factor complex; IPI:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030139; C:endocytic vesicle; IDA: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: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:0035003; C:subapical complex; IDA:FlyBase.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:FlyBase.
DR   GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; TAS: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:0007155; P:cell adhesion; TAS:FlyBase.
DR   GO; GO:0043697; P:cell dedifferentiation; IGI:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IMP:FlyBase.
DR   GO; GO:0001708; P:cell fate specification; TAS: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:0042676; P:compound eye cone cell fate commitment; TAS: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:0007451; P:dorsal/ventral lineage restriction, imaginal disc; TAS:FlyBase.
DR   GO; GO:0007450; P:dorsal/ventral pattern formation, imaginal disc; TAS:FlyBase.
DR   GO; GO:0007398; P:ectoderm development; TAS:FlyBase.
DR   GO; GO:0035165; P:embryonic crystal cell differentiation; TAS: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:0042067; P:establishment of ommatidial planar polarity; TAS: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:0030708; P:germarium-derived female germ-line cyst encapsulation; TAS: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:0007446; P:imaginal disc growth; TAS:FlyBase.
DR   GO; GO:0007447; P:imaginal disc pattern formation; TAS:FlyBase.
DR   GO; GO:0016348; P:imaginal disc-derived leg joint 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:0016333; P:morphogenesis of follicular epithelium; NAS:FlyBase.
DR   GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR   GO; GO:0007521; P:muscle cell fate determination; IMP: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:0046329; P:negative regulation of JNK cascade; NAS:FlyBase.
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:0000122; P:negative regulation of transcription by RNA polymerase II; TAS: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:0007405; P:neuroblast proliferation; IMP:UniProtKB.
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:0007314; P:oocyte anterior/posterior axis specification; TAS: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; IMP:UniProtKB.
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:0007464; P:R3/R4 cell fate commitment; NAS:FlyBase.
DR   GO; GO:0045466; P:R7 cell differentiation; IMP:FlyBase.
DR   GO; GO:0045463; P:R8 cell development; TAS:FlyBase.
DR   GO; GO:0007460; P:R8 cell fate commitment; TAS: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:0042689; P:regulation of crystal cell differentiation; TAS: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:0007519; P:skeletal muscle tissue development; IMP:FlyBase.
DR   GO; GO:0048863; P:stem cell differentiation; IMP:FlyBase.
DR   GO; GO:0007419; P:ventral cord development; NAS: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   GO; GO:0007473; P:wing disc proximal/distal pattern formation; TAS:FlyBase.
DR   CDD; cd00204; ANK; 2.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR024600; DUF3454_notch.
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; 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; PF11936; DUF3454; 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; Complete proteome;
KW   Developmental protein; Differentiation; Disulfide bond;
KW   EGF-like domain; Endosome; Glycoprotein; Membrane; Neurogenesis;
KW   Notch signaling pathway; Nucleus; Oogenesis; Phosphoprotein;
KW   Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW   Transcription; Transcription regulation; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     52       {ECO:0000255}.
FT   CHAIN        53   2703       Neurogenic locus Notch protein.
FT                                /FTId=PRO_0000007673.
FT   CHAIN         ?   2703       Processed neurogenic locus Notch protein.
FT                                /FTId=PRO_0000296234.
FT   TOPO_DOM     53   1745       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1746   1766       Helical. {ECO:0000255}.
FT   TOPO_DOM   1767   2703       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       58     95       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       96    136       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      139    176       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      177    215       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      217    253       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      255    291       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      293    329       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      331    370       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      372    408       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      409    447       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      449    486       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      488    524       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      526    562       EGF-like 13; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      564    600       EGF-like 14; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      602    637       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      639    675       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      677    713       EGF-like 17; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      715    751       EGF-like 18; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      753    789       EGF-like 19; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      791    827       EGF-like 20; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      829    865       EGF-like 21; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      867    905       EGF-like 22. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      907    944       EGF-like 23; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      946    982       EGF-like 24; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      984   1020       EGF-like 25. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1022   1058       EGF-like 26; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1060   1096       EGF-like 27. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1098   1134       EGF-like 28. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1136   1181       EGF-like 29. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1183   1219       EGF-like 30; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1221   1257       EGF-like 31; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1259   1295       EGF-like 32; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1297   1335       EGF-like 33. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1337   1373       EGF-like 34. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1375   1412       EGF-like 35. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1415   1451       EGF-like 36. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1482   1521       LNR 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   REPEAT     1522   1557       LNR 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   REPEAT     1559   1599       LNR 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00525}.
FT   REPEAT     1901   1945       ANK 1. {ECO:0000255}.
FT   REPEAT     1950   1979       ANK 2. {ECO:0000255}.
FT   REPEAT     1983   2013       ANK 3. {ECO:0000255}.
FT   REPEAT     2017   2046       ANK 4. {ECO:0000255}.
FT   REPEAT     2050   2079       ANK 5. {ECO:0000255}.
FT   REPEAT     2083   2112       ANK 6. {ECO:0000255}.
FT   REPEAT     2116   2139       ANK 7. {ECO:0000255}.
FT   REGION     2325   2328       Interaction with Nedd4.
FT   COMPBIAS   2264   2277       Ala-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00001}.
FT   COMPBIAS   2369   2498       Gly-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00008}.
FT   COMPBIAS   2533   2568       Gln-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00006}.
FT   COMPBIAS   2587   2675       Ser-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00016}.
FT   MOD_RES    2447   2447       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   CARBOHYD     72     72       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    110    110       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    153    153       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    183    183       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    191    191       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    210    210       O-linked (GlcNAc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    223    223       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    231    231       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    307    307       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    322    322       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    348    348       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    371    371       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    386    386       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    427    427       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    430    430       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    475    475       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    481    481       O-linked (GlcNAc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    494    494       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    502    502       O-linked (Fuc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    519    519       O-linked (GlcNAc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    532    532       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    570    570       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    595    595       O-linked (GlcNAc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    608    608       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    645    645       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    683    683       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    691    691       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    721    721       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    759    759       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    797    797       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    805    805       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    822    822       O-linked (GlcNAc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    843    843       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    922    922       O-linked (Fuc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    952    952       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    960    960       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    990    990       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD    998    998       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD   1036   1036       O-linked (Fuc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD   1045   1045       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1066   1066       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD   1074   1074       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD   1112   1112       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD   1157   1157       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1189   1189       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD   1197   1197       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD   1235   1235       O-linked (Fuc...) threonine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD   1242   1242       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1271   1271       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1273   1273       O-linked (Fuc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD   1303   1303       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD   1381   1381       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:27268051}.
FT   CARBOHYD   1521   1521       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1594   1594       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1627   1627       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     62     73       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     67     83       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     85     94       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    100    111       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    105    124       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    126    135       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    143    154       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    148    164       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    166    175       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    181    192       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    186    203       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    205    214       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    221    232       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    226    241       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    243    252       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    259    270       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    264    279       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    281    290       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    297    308       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    302    317       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    319    328       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    335    349       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    343    358       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    360    369       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    376    387       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    381    396       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    398    407       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    413    424       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    418    435       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    437    446       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    453    465       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    459    474       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    476    485       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    492    503       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    497    512       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    514    523       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    530    541       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    535    550       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    552    561       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    568    579       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    573    588       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    590    599       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    606    616       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    611    625       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    627    636       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    643    654       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    648    663       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    665    674       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    681    692       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    686    701       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    703    712       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    719    730       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    724    739       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    741    750       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    757    768       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    762    777       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    779    788       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    795    806       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    800    815       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    817    826       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    833    844       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    838    853       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    855    864       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    871    882       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    876    893       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    895    904       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    911    923       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    917    932       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    934    943       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    950    961       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    955    970       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    972    981       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    988    999       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    993   1008       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1010   1019       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1026   1037       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1031   1046       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1048   1057       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1064   1075       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1069   1084       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1086   1095       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1102   1113       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1107   1122       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1124   1133       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1155   1160       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1171   1180       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1187   1198       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1192   1207       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1209   1218       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1225   1236       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1230   1245       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1247   1256       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1263   1274       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1268   1283       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1285   1294       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1301   1314       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1306   1323       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1325   1334       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1341   1352       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1346   1361       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1363   1372       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1379   1389       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1384   1400       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1402   1411       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1419   1430       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1424   1439       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1441   1450       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1482   1505       {ECO:0000255|PROSITE-ProRule:PRU00525}.
FT   DISULFID   1487   1500       {ECO:0000255|PROSITE-ProRule:PRU00525}.
FT   DISULFID   1496   1512       {ECO:0000255|PROSITE-ProRule:PRU00525}.
FT   DISULFID   1522   1545       {ECO:0000255|PROSITE-ProRule:PRU00525}.
FT   DISULFID   1527   1540       {ECO:0000255|PROSITE-ProRule:PRU00525}.
FT   DISULFID   1536   1552       {ECO:0000255|PROSITE-ProRule:PRU00525}.
FT   DISULFID   1559   1585       {ECO:0000255|PROSITE-ProRule:PRU00525}.
FT   DISULFID   1567   1580       {ECO:0000255|PROSITE-ProRule:PRU00525}.
FT   DISULFID   1576   1592       {ECO:0000255|PROSITE-ProRule:PRU00525}.
FT   VARIANT     578    578       I -> T.
FT   VARIANT    2044   2044       I -> R.
FT   VARIANT    2265   2265       A -> V.
FT   VARIANT    2407   2407       H -> R.
FT   VARIANT    2445   2445       R -> L.
FT   VARIANT    2568   2568       Q -> QQQQQ.
FT   MUTAGEN     739    739       C->Y: In mcd5; induces loss of
FT                                microchaetae sensory precursors.
FT   MUTAGEN    2060   2060       A->V: In su42c; deltex-like mutation that
FT                                induces outstreched wings and
FT                                variability-fused ocelli.
FT   MUTAGEN    2328   2328       Y->F: Abolishes interaction with Nedd4
FT                                and reduces ubiquitination.
FT                                {ECO:0000269|PubMed:15620649}.
FT   CONFLICT      9      9       R -> G (in Ref. 5; CAB37610).
FT                                {ECO:0000305}.
FT   CONFLICT     84     84       A -> G (in Ref. 5; CAB37610).
FT                                {ECO:0000305}.
FT   CONFLICT    103    103       M -> I (in Ref. 1; AAB59220).
FT                                {ECO:0000305}.
FT   CONFLICT    119    119       R -> H (in Ref. 2; AAA28725).
FT                                {ECO:0000305}.
FT   CONFLICT    231    231       T -> I (in Ref. 1; AAB59220).
FT                                {ECO:0000305}.
FT   CONFLICT    240    240       Q -> R (in Ref. 5; CAB37610).
FT                                {ECO:0000305}.
FT   CONFLICT    267    267       G -> A (in Ref. 1; AAB59220).
FT                                {ECO:0000305}.
FT   CONFLICT   1561   1561       S -> T (in Ref. 1; AAB59220 and 2;
FT                                AAA28725). {ECO:0000305}.
FT   CONFLICT   2257   2257       G -> S (in Ref. 2; AAA28725).
FT                                {ECO:0000305}.
FT   CONFLICT   2577   2577       A -> E (in Ref. 7; AAA74496).
FT                                {ECO:0000305}.
FT   HELIX      1930   1950       {ECO:0000244|PDB:1OT8}.
FT   HELIX      1954   1960       {ECO:0000244|PDB:1OT8}.
FT   HELIX      1964   1972       {ECO:0000244|PDB:1OT8}.
FT   HELIX      1987   1993       {ECO:0000244|PDB:1OT8}.
FT   HELIX      1997   2004       {ECO:0000244|PDB:1OT8}.
FT   HELIX      2021   2027       {ECO:0000244|PDB:1OT8}.
FT   HELIX      2033   2039       {ECO:0000244|PDB:1OT8}.
FT   HELIX      2054   2060       {ECO:0000244|PDB:1OT8}.
FT   HELIX      2064   2072       {ECO:0000244|PDB:1OT8}.
FT   HELIX      2087   2093       {ECO:0000244|PDB:1OT8}.
FT   HELIX      2097   2105       {ECO:0000244|PDB:1OT8}.
FT   HELIX      2120   2126       {ECO:0000244|PDB:1OT8}.
FT   HELIX      2130   2136       {ECO:0000244|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
//
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