MYC_DROME
ID MYC_DROME Reviewed; 717 AA.
AC Q9W4S7; O96903; P91665;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Myc protein {ECO:0000312|FlyBase:FBgn0262656};
DE AltName: Full=Diminutive protein {ECO:0000303|PubMed:8929412};
DE AltName: Full=dMyc1 {ECO:0000303|PubMed:8929412};
GN Name=Myc {ECO:0000303|PubMed:8929412, ECO:0000312|FlyBase:FBgn0262656};
GN Synonyms=dm {ECO:0000303|PubMed:8929412};
GN ORFNames=CG10798 {ECO:0000312|FlyBase:FBgn0262656};
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 {ECO:0000312|EMBL:AAF45866.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R {ECO:0000269|PubMed:8929412};
RX PubMed=8929412; DOI=10.1126/science.274.5292.1523;
RA Gallant P., Shiio Y., Cheng P.F., Parkhurst S.M., Eisenman R.N.;
RT "Myc and Max homologs in Drosophila.";
RL Science 274:1523-1527(1996).
RN [2] {ECO:0000305}
RP SEQUENCE REVISION TO 274.
RA Gallant P., Shiio Y., Cheng P.F., Parkhurst S.M., Eisenman R.N.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=9037036; DOI=10.1073/pnas.94.4.1235;
RA Schreiber-Agus N., Stein D., Chen K., Goltz J.S., Stevens L., DePinho R.A.;
RT "Drosophila Myc is oncogenic in mammalian cells and plays a role in the
RT diminutive phenotype.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:1235-1240(1997).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [5] {ECO:0000305}
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 [6] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R {ECO:0000269|PubMed:10731137};
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 [7] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP FUNCTION, AND INTERACTION WITH AGO.
RX PubMed=15182669; DOI=10.1016/j.cub.2004.04.040;
RA Moberg K.H., Mukherjee A., Veraksa A., Artavanis-Tsakonas S.,
RA Hariharan I.K.;
RT "The Drosophila F box protein archipelago regulates dMyc protein levels in
RT vivo.";
RL Curr. Biol. 14:965-974(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH PONT AND REPT.
RX PubMed=16087886; DOI=10.1073/pnas.0408945102;
RA Bellosta P., Hulf T., Balla Diop S., Usseglio F., Pradel J., Aragnol D.,
RA Gallant P.;
RT "Myc interacts genetically with Tip48/Reptin and Tip49/Pontin to control
RT growth and proliferation during Drosophila development.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11799-11804(2005).
RN [10]
RP FUNCTION, INTERACTION WITH LID, AND IDENTIFICATION IN COMPLEX WITH LID AND
RP ASH2.
RX PubMed=17311883; DOI=10.1101/gad.1523007;
RA Secombe J., Li L., Carlos L., Eisenman R.N.;
RT "The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase
RT required for dMyc-induced cell growth.";
RL Genes Dev. 21:537-551(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217 AND SER-220, AND
RP IDENTIFICATION 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 [12]
RP FUNCTION, AND INTERACTION WITH AGO AND PUF.
RX PubMed=24173801; DOI=10.1242/dev.096941;
RA Li L., Anderson S., Secombe J., Eisenman R.N.;
RT "The Drosophila ubiquitin-specific protease Puffyeye regulates dMyc-
RT mediated growth.";
RL Development 140:4776-4787(2013).
RN [13]
RP FUNCTION.
RX PubMed=24615015; DOI=10.1128/mcb.00658-13;
RA Hovhanyan A., Herter E.K., Pfannstiel J., Gallant P., Raabe T.;
RT "Drosophila mbm is a nucleolar myc and casein kinase 2 target required for
RT ribosome biogenesis and cell growth of central brain neuroblasts.";
RL Mol. Cell. Biol. 34:1878-1891(2014).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25999153; DOI=10.1038/srep10339;
RA Kuo Y., Huang H., Cai T., Wang T.;
RT "Target of Rapamycin Complex 2 regulates cell growth via Myc in
RT Drosophila.";
RL Sci. Rep. 5:10339-10339(2015).
RN [15]
RP FUNCTION.
RX PubMed=25858587; DOI=10.1074/jbc.m114.607036;
RA Kim W., Kim H.D., Jung Y., Kim J., Chung J.;
RT "Drosophila Low Temperature Viability Protein 1 (LTV1) Is Required for
RT Ribosome Biogenesis and Cell Growth Downstream of Drosophila Myc (dMyc).";
RL J. Biol. Chem. 290:13591-13604(2015).
CC -!- FUNCTION: Participates in the regulation of gene transcription
CC (PubMed:8929412, PubMed:16087886, PubMed:24173801, PubMed:24615015,
CC PubMed:25999153, PubMed:25858587). Binds DNA in a non-specific manner,
CC yet also specifically recognizes the core sequence CAC[GA]TG
CC (PubMed:8929412). Seems to activate the transcription of growth-related
CC genes; required for cellular proliferation and growth (PubMed:16087886,
CC PubMed:25999153, PubMed:25858587). Functions in the TORC2-mediated
CC regulation of cell growth, acting downstream of the TORC2 complex
CC (PubMed:25999153). Inhibits the demethylase activity of Lid
CC (PubMed:17311883). Activates transcription of mbm (PubMed:24615015).
CC Has a role in ribosome biogenesis and endoreplication in fat body cells
CC by activating the transcription of LTV1 (PubMed:25858587). Able to
CC induce the SCF E3 ubiquitin-protein ligase member archipelago (ago)
CC which functions in its degradation (PubMed:15182669, PubMed:24173801).
CC It may therefore create a negative feedback loop with ago that is
CC regulated by the ubiquitin hydrolase puf (PubMed:24173801).
CC {ECO:0000269|PubMed:15182669, ECO:0000269|PubMed:16087886,
CC ECO:0000269|PubMed:17311883, ECO:0000269|PubMed:24173801,
CC ECO:0000269|PubMed:24615015, ECO:0000269|PubMed:25858587,
CC ECO:0000269|PubMed:25999153, ECO:0000269|PubMed:8929412}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein (PubMed:8929412). Binds DNA as a heterodimer with Max
CC (PubMed:8929412). Interacts with ago (PubMed:15182669,
CC PubMed:24173801). Interacts with lid (PubMed:17311883). Part of a
CC complex containing lid, Myc and ash2 (PubMed:17311883). Component of a
CC complex with pont and rept (PubMed:16087886). Interacts with puf
CC (PubMed:24173801). {ECO:0000269|PubMed:15182669,
CC ECO:0000269|PubMed:16087886, ECO:0000269|PubMed:17311883,
CC ECO:0000269|PubMed:24173801, ECO:0000269|PubMed:8929412}.
CC -!- INTERACTION:
CC Q9W4S7; Q9VZF4: ago; NbExp=2; IntAct=EBI-120162, EBI-138334;
CC Q9W4S7; P16371: gro; NbExp=3; IntAct=EBI-120162, EBI-153866;
CC Q9W4S7; P16371-2: gro; NbExp=3; IntAct=EBI-120162, EBI-15661898;
CC Q9W4S7; P91664: Max; NbExp=3; IntAct=EBI-120162, EBI-193577;
CC Q9W4S7; Q9VH07: pont; NbExp=4; IntAct=EBI-120162, EBI-234957;
CC Q9W4S7; Q9V3K3: rept; NbExp=4; IntAct=EBI-120162, EBI-192924;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25999153}. Cytoplasm
CC {ECO:0000269|PubMed:25999153}. Note=Translocation from the cytoplasm to
CC the nucleus may be promoted by the TORC2 complex (Lst8 and rictor).
CC {ECO:0000269|PubMed:25999153}.
CC -!- TISSUE SPECIFICITY: Low levels detected throughout embryo before
CC cellular blastoderm formation, particularly concentrated in pole plasm.
CC Zygotic expression detected during cellular blastoderm stage in
CC endodermal anlagen of anterior and posterior midgut at both poles.
CC After gastrulation, expression detected in invaginating ventral furrow
CC of mesoderm. Continued expression in anterior and posterior midgut and
CC mesoderm during germband extension. During late germ-band retraction,
CC expression remains detectable in fusing midgut and presumed developing
CC somatic musculature. {ECO:0000269|PubMed:8929412,
CC ECO:0000269|PubMed:9037036}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in
CC embryos. {ECO:0000269|PubMed:8929412, ECO:0000269|PubMed:9037036}.
CC -!- PTM: Probably targeted for ubiquitination by the SFC ubiquitin ligase
CC complex member ago, leading to its proteasomal degradation.
CC {ECO:0000305|PubMed:15182669}.
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DR EMBL; U77370; AAB39842.2; -; mRNA.
DR EMBL; U81384; AAD00517.1; -; mRNA.
DR EMBL; AE014298; AAF45866.2; -; Genomic_DNA.
DR EMBL; AL121800; CAD24780.1; -; Genomic_DNA.
DR EMBL; AY058627; AAL13856.1; -; mRNA.
DR RefSeq; NP_001259204.1; NM_001272275.1.
DR RefSeq; NP_525062.2; NM_080323.4.
DR AlphaFoldDB; Q9W4S7; -.
DR SMR; Q9W4S7; -.
DR BioGRID; 57835; 184.
DR DIP; DIP-18847N; -.
DR IntAct; Q9W4S7; 21.
DR MINT; Q9W4S7; -.
DR STRING; 7227.FBpp0303995; -.
DR iPTMnet; Q9W4S7; -.
DR PaxDb; Q9W4S7; -.
DR DNASU; 31310; -.
DR EnsemblMetazoa; FBtr0070525; FBpp0070501; FBgn0262656.
DR EnsemblMetazoa; FBtr0331605; FBpp0303995; FBgn0262656.
DR GeneID; 31310; -.
DR KEGG; dme:Dmel_CG10798; -.
DR UCSC; CG10798-RA; d. melanogaster.
DR CTD; 4609; -.
DR FlyBase; FBgn0262656; Myc.
DR VEuPathDB; VectorBase:FBgn0262656; -.
DR eggNOG; KOG2483; Eukaryota.
DR HOGENOM; CLU_016112_0_0_1; -.
DR InParanoid; Q9W4S7; -.
DR OMA; PEFRHNV; -.
DR OrthoDB; 1276360at2759; -.
DR PhylomeDB; Q9W4S7; -.
DR Reactome; R-DME-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
DR SignaLink; Q9W4S7; -.
DR BioGRID-ORCS; 31310; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 31310; -.
DR PRO; PR:Q9W4S7; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0262656; Expressed in spermathecum and 76 other tissues.
DR ExpressionAtlas; Q9W4S7; baseline and differential.
DR Genevisible; Q9W4S7; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
DR GO; GO:0035212; P:cell competition in a multicellular organism; IMP:FlyBase.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:FlyBase.
DR GO; GO:0031670; P:cellular response to nutrient; IDA:FlyBase.
DR GO; GO:0042023; P:DNA endoreduplication; IMP:FlyBase.
DR GO; GO:0009880; P:embryonic pattern specification; IGI:FlyBase.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0055088; P:lipid homeostasis; IMP:FlyBase.
DR GO; GO:0022008; P:neurogenesis; IGI:FlyBase.
DR GO; GO:0017126; P:nucleologenesis; IMP:FlyBase.
DR GO; GO:0030307; P:positive regulation of cell growth; IGI:FlyBase.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:UniProtKB.
DR GO; GO:0048639; P:positive regulation of developmental growth; IMP:FlyBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:FlyBase.
DR GO; GO:0045927; P:positive regulation of growth; IMP:FlyBase.
DR GO; GO:0045572; P:positive regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:FlyBase.
DR GO; GO:0046622; P:positive regulation of organ growth; IMP:FlyBase.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:FlyBase.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0010506; P:regulation of autophagy; IMP:FlyBase.
DR GO; GO:0046620; P:regulation of organ growth; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0090062; P:regulation of trehalose metabolic process; IMP:FlyBase.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR GO; GO:0042246; P:tissue regeneration; IMP:FlyBase.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..717
FT /note="Myc protein"
FT /id="PRO_0000127322"
FT DOMAIN 625..677
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 288..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 679..711
FT /evidence="ECO:0000255"
FT COMPBIAS 288..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 353
FT /note="G -> D (in Ref. 3; AAD00517)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="N -> S (in Ref. 3; AAD00517)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="S -> K (in Ref. 3; AAD00517)"
FT /evidence="ECO:0000305"
FT CONFLICT 369..373
FT /note="NNKLK -> IKNNN (in Ref. 3; AAD00517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 79308 MW; D6A74CF5D4B80150 CRC64;
MALYRSDPYS IMDDQLFSNI SIFDMDNDLY DMDKLLSSST IQSDLEKIED MESVFQDYDL
EEDMKPEIRN IDCMWPAMSS CLTSGNGNGI ESGNSAASSY SETGAVSLAM VSGSTNLYSA
YQRSQTTDNT QSNQQHVVNS AENMPVIIKK ELADLDYTVC QKRLRLSGGD KKSQIQDEVH
LIPPGGSLLR KRNNQDIIRK SGELSGSDSI KYQRPDTPHS LTDEVAASEF RHNVDLRACV
MGSNNISLTG NDSDVNYIKQ ISRELQNTGK DPLPVRYIPP INDVLDVLNQ HSNSTGGQQQ
LNQQQLDEQQ QAIDIATGRN TVDSPPTTGS DSDSDDGEPL NFDLRHHRTS KSGSNASITT
NNNNSNNKNN KLKNNSNGML HMMHITDHSY TRCNDMVDDG PNLETPSDSD EEIDVVSYTD
KKLPTNPSCH LMGALQFQMA HKISIDHMKQ KPRYNNFNLP YTPASSSPVK SVANSRYPSP
SSTPYQNCSS ASPSYSPLSV DSSNVSSSSS SSSSQSSFTT SSSNKGRKRS SLKDPGLLIS
SSSVYLPGVN NKVTHSSMMS KKSRGKKVVG TSSGNTSPIS SGQDVDAMDR NWQRRSGGIA
TSTSSNSSVH RKDFVLGFDE ADTIEKRNQH NDMERQRRIG LKNLFEALKK QIPTIRDKER
APKVNILREA AKLCIQLTQE EKELSMQRQL LSLQLKQRQD TLASYQMELN ESRSVSG
