ID DLG1_DROME Reviewed; 970 AA. AC P31007; A4V4A8; A4V4B0; A8JUR9; A8JUS0; C7LAH6; Q7KV38; Q7KV39; Q7KV40; AC Q7YXH8; Q8SY37; Q8T0C6; Q95TF5; Q9VYZ4; Q9VYZ5; Q9VYZ6; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 2. DT 27-MAR-2024, entry version 239. DE RecName: Full=Disks large 1 tumor suppressor protein; DE Short=Dlg {ECO:0000303|PubMed:24768049}; GN Name=dlg1; Synonyms=l(1)dlg1; ORFNames=CG1725; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), FUNCTION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=Oregon-R; TISSUE=Embryo; RX PubMed=1651169; DOI=10.1016/0092-8674(81)90009-x; RA Woods D.F., Bryant P.J.; RT "The discs-large tumor suppressor gene of Drosophila encodes a guanylate RT kinase homolog localized at septate junctions."; RL Cell 66:451-464(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; F; H; I AND L), FUNCTION, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Embryo; RX PubMed=12657668; DOI=10.1523/jneurosci.23-06-02093.2003; RA Mendoza C., Olguin P., Lafferte G., Thomas U., Ebitsch S., RA Gundelfinger E.D., Kukuljan M., Sierralta J.; RT "Novel isoforms of Dlg are fundamental for neuronal development in RT Drosophila."; RL J. Neurosci. 23:2093-2101(2003). 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, AND ALTERNATIVE SPLICING. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS F AND I), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 711-970 (ISOFORM G). RC STRAIN=Berkeley; TISSUE=Embryo, and Head; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM G). RC STRAIN=Berkeley; TISSUE=Embryo; RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=10884224; DOI=10.1126/science.289.5476.113; RA Bilder D., Li M., Perrimon N.; RT "Cooperative regulation of cell polarity and growth by Drosophila tumor RT suppressors."; RL Science 289:113-116(2000). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496 AND THR-714, 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 [9] RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX PubMed=24768049; DOI=10.1016/j.cub.2014.03.056; RA Claret S., Jouette J., Benoit B., Legent K., Guichet A.; RT "PI(4,5)P2 produced by the PI4P5K SKTL controls apical size by tethering RT PAR-3 in Drosophila epithelial cells."; RL Curr. Biol. 24:1071-1079(2014). CC -!- FUNCTION: During embryonic development, some isoforms are essential for CC proper neuronal differentiation and organization. Required for cell CC polarity; maintenance of apicobasal polarity. Plays a critical role at CC septate junctions in cellular growth control during larval development. CC The presence of a guanylate kinase domain suggests involvement in CC cellular adhesion as well as signal transduction to control cellular CC proliferation. {ECO:0000269|PubMed:10884224, CC ECO:0000269|PubMed:12657668, ECO:0000269|PubMed:1651169}. CC -!- INTERACTION: CC P31007; Q4AB30: gukh; NbExp=4; IntAct=EBI-389374, EBI-8282973; CC P31007; P08510: Sh; NbExp=3; IntAct=EBI-389374, EBI-85074; CC P31007-1; Q9VE13: gukh; NbExp=11; IntAct=EBI-389394, EBI-3414026; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12959}. Cell CC membrane {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:1651169}; CC Peripheral membrane protein {ECO:0000269|PubMed:10884224, CC ECO:0000269|PubMed:1651169}; Cytoplasmic side CC {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:1651169}. Basolateral CC cell membrane {ECO:0000269|PubMed:24768049}; Peripheral membrane CC protein {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:1651169}; CC Cytoplasmic side {ECO:0000269|PubMed:10884224, CC ECO:0000269|PubMed:1651169}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:1651169}. Cell CC junction, septate junction {ECO:0000269|PubMed:10884224, CC ECO:0000269|PubMed:1651169}. Note=Cytoskeleton- and membrane- CC associated. Located at the cytoplasmic face of the membrane in the CC cellular blastoderm and becomes associated with septate junctions which CC begin to form between epithelial cells at the time of dorsal closure. CC In adult flies, located at the apical-lateral membrane boundary of CC epithelial cells. {ECO:0000269|PubMed:10884224}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=B; CC IsoId=P31007-2; Sequence=Displayed; CC Name=A; CC IsoId=P31007-3; Sequence=VSP_011403, VSP_011405, VSP_011410, CC VSP_011414; CC Name=E; Synonyms=Dlg-A, D; CC IsoId=P31007-1; Sequence=VSP_011402, VSP_011404, VSP_011410, CC VSP_011414; CC Name=F; CC IsoId=P31007-4; Sequence=VSP_011401, VSP_011411, VSP_011412; CC Name=G; CC IsoId=P31007-5; Sequence=VSP_011402, VSP_011404, VSP_011410, CC VSP_011413; CC Name=H; CC IsoId=P31007-6; Sequence=VSP_011406; CC Name=I; Synonyms=C, J; CC IsoId=P31007-7; Sequence=VSP_011406, VSP_011408, VSP_011409; CC Name=K; CC IsoId=P31007-9; Sequence=VSP_039402, VSP_011406; CC Name=L; Synonyms=S97; CC IsoId=P31007-8; Sequence=VSP_011406, VSP_011407, VSP_011415; CC -!- TISSUE SPECIFICITY: During the cellular blastoderm stage, isoform B, CC isoform F, isoform H, isoform I and isoform L expression is localized CC to the cell borders. From stage 11 onwards, expression is found CC predominantly in the developing nervous system: axon bundles in the CC ventral cord and the brain. Stage 14 and 15 embryos exhibit expression CC in the developing body wall muscle. Expression in neuropil regions of CC the CNS and at NMJs persists through to larval development. Other CC isoforms show expression in embryonic epithelial cells. In larvae, CC expression is seen as a belt around salivary glands, imaginal disks and CC proventriculus. Expressed in adult reproductive tissues. In epithelia, CC coexpressed with scrib throughout development. CC {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:12657668, CC ECO:0000269|PubMed:1651169}. CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically CC throughout development (PubMed:1651169). Expressed in follicular CC epithelium in stage 9/10 of oogenesis (PubMed:24768049). CC {ECO:0000269|PubMed:1651169, ECO:0000269|PubMed:24768049}. CC -!- MISCELLANEOUS: [Isoform B]: Contains the N-terminal domain essential CC for correct neuronal development. CC -!- MISCELLANEOUS: [Isoform F]: Contains the N-terminal domain essential CC for correct neuronal development. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform H]: Contains the N-terminal domain essential CC for correct neuronal development. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform I]: Contains the N-terminal domain essential CC for correct neuronal development. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform L]: Contains the N-terminal domain essential CC for correct neuronal development. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL39553.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M73529; AAA28468.1; -; mRNA. DR EMBL; AY332243; AAQ01226.1; -; mRNA. DR EMBL; AE014298; AAF48037.2; -; Genomic_DNA. DR EMBL; AE014298; AAF48038.2; -; Genomic_DNA. DR EMBL; AE014298; AAF48039.2; -; Genomic_DNA. DR EMBL; AE014298; AAN09630.1; -; Genomic_DNA. DR EMBL; AE014298; AAS65308.1; -; Genomic_DNA. DR EMBL; AE014298; AAS65309.1; -; Genomic_DNA. DR EMBL; AE014298; AAS65310.1; -; Genomic_DNA. DR EMBL; AE014298; AAS65311.1; -; Genomic_DNA. DR EMBL; AE014298; AAS65312.1; -; Genomic_DNA. DR EMBL; AE014298; AAS65313.1; -; Genomic_DNA. DR EMBL; AE014298; ABW09394.1; -; Genomic_DNA. DR EMBL; AE014298; ABW09395.1; -; Genomic_DNA. DR EMBL; AY059433; AAL13339.1; -; mRNA. DR EMBL; AY069408; AAL39553.1; ALT_INIT; mRNA. DR EMBL; AY075410; AAL68235.1; -; mRNA. DR EMBL; BT099726; ACV53090.1; -; mRNA. DR PIR; A39651; A39651. DR RefSeq; NP_001096955.1; NM_001103485.3. [P31007-9] DR RefSeq; NP_001096956.1; NM_001103486.3. [P31007-8] DR RefSeq; NP_001162719.1; NM_001169248.2. [P31007-1] DR RefSeq; NP_001245623.1; NM_001258694.2. [P31007-5] DR RefSeq; NP_001259447.1; NM_001272518.1. [P31007-1] DR RefSeq; NP_511120.2; NM_078565.5. [P31007-1] DR RefSeq; NP_727518.1; NM_167280.2. [P31007-7] DR RefSeq; NP_727519.1; NM_167281.2. [P31007-4] DR RefSeq; NP_727520.1; NM_167282.4. [P31007-3] DR RefSeq; NP_996402.1; NM_206679.2. [P31007-7] DR RefSeq; NP_996403.1; NM_206680.2. [P31007-7] DR RefSeq; NP_996404.1; NM_206681.4. [P31007-6] DR RefSeq; NP_996405.1; NM_206682.4. [P31007-5] DR RefSeq; NP_996406.1; NM_206683.4. [P31007-2] DR RefSeq; NP_996407.1; NM_206684.4. [P31007-1] DR PDB; 3TVT; X-ray; 1.60 A; A=618-970. DR PDB; 4RP3; X-ray; 1.36 A; A/B=1-97. DR PDB; 4RP4; X-ray; 1.42 A; A/B=1-97. DR PDB; 4RP5; X-ray; 1.65 A; A/B=1-97. DR PDBsum; 3TVT; -. DR PDBsum; 4RP3; -. DR PDBsum; 4RP4; -. DR PDBsum; 4RP5; -. DR AlphaFoldDB; P31007; -. DR SMR; P31007; -. DR BioGRID; 58494; 67. DR ComplexPortal; CPX-2410; Scribble cell polarity complex. DR DIP; DIP-31531N; -. DR IntAct; P31007; 44. DR MINT; P31007; -. DR STRING; 7227.FBpp0290503; -. DR TCDB; 1.H.2.1.1; the invertebrate pmp22-claudin (claudin2) family. DR iPTMnet; P31007; -. DR PaxDb; 7227-FBpp0290503; -. DR DNASU; 32083; -. DR EnsemblMetazoa; FBtr0073483; FBpp0073339; FBgn0001624. [P31007-7] DR EnsemblMetazoa; FBtr0073484; FBpp0073340; FBgn0001624. [P31007-4] DR EnsemblMetazoa; FBtr0073485; FBpp0073341; FBgn0001624. [P31007-1] DR EnsemblMetazoa; FBtr0073486; FBpp0073342; FBgn0001624. [P31007-3] DR EnsemblMetazoa; FBtr0073487; FBpp0089350; FBgn0001624. [P31007-1] DR EnsemblMetazoa; FBtr0073488; FBpp0089351; FBgn0001624. [P31007-2] DR EnsemblMetazoa; FBtr0073489; FBpp0089352; FBgn0001624. [P31007-5] DR EnsemblMetazoa; FBtr0073490; FBpp0089353; FBgn0001624. [P31007-6] DR EnsemblMetazoa; FBtr0073491; FBpp0089348; FBgn0001624. [P31007-7] DR EnsemblMetazoa; FBtr0073492; FBpp0089349; FBgn0001624. [P31007-7] DR EnsemblMetazoa; FBtr0112812; FBpp0111724; FBgn0001624. [P31007-9] DR EnsemblMetazoa; FBtr0112813; FBpp0111725; FBgn0001624. [P31007-8] DR EnsemblMetazoa; FBtr0301289; FBpp0290504; FBgn0001624. [P31007-1] DR EnsemblMetazoa; FBtr0308089; FBpp0300432; FBgn0001624. [P31007-5] DR EnsemblMetazoa; FBtr0333261; FBpp0305459; FBgn0001624. [P31007-1] DR GeneID; 32083; -. DR KEGG; dme:Dmel_CG1725; -. DR UCSC; CG1725-RE; d. melanogaster. DR UCSC; CG1725-RI; d. melanogaster. DR UCSC; CG1725-RK; d. melanogaster. DR UCSC; CG1725-RL; d. melanogaster. DR AGR; FB:FBgn0001624; -. DR CTD; 1739; -. DR FlyBase; FBgn0001624; dlg1. DR VEuPathDB; VectorBase:FBgn0001624; -. DR GeneTree; ENSGT00940000167723; -. DR InParanoid; P31007; -. DR OMA; WIASSDF; -. DR PhylomeDB; P31007; -. DR Reactome; R-DME-438066; Unblocking of NMDA receptors, glutamate binding and activation. DR Reactome; R-DME-451308; Activation of Ca-permeable Kainate Receptor. DR Reactome; R-DME-5625900; RHO GTPases activate CIT. DR Reactome; R-DME-6794361; Neurexins and neuroligins. DR Reactome; R-DME-8849932; Synaptic adhesion-like molecules. DR SignaLink; P31007; -. DR BioGRID-ORCS; 32083; 0 hits in 3 CRISPR screens. DR ChiTaRS; dlg1; fly. DR GenomeRNAi; 32083; -. DR PRO; PR:P31007; -. DR Proteomes; UP000000803; Chromosome X. DR Bgee; FBgn0001624; Expressed in head capsule and 23 other cell types or tissues. DR ExpressionAtlas; P31007; baseline and differential. DR GO; GO:0045179; C:apical cortex; IDA:FlyBase. DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase. DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central. DR GO; GO:0005938; C:cell cortex; IDA:FlyBase. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0016328; C:lateral plasma membrane; IDA:FlyBase. DR GO; GO:0031256; C:leading edge membrane; IDA:FlyBase. DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase. DR GO; GO:0005886; C:plasma membrane; IMP:FlyBase. DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central. DR GO; GO:0045211; C:postsynaptic membrane; IDA:FlyBase. DR GO; GO:0005918; C:septate junction; IDA:FlyBase. DR GO; GO:0005920; C:smooth septate junction; IDA:FlyBase. DR GO; GO:0071212; C:subsynaptic reticulum; IDA:FlyBase. DR GO; GO:0045202; C:synapse; IDA:FlyBase. DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase. DR GO; GO:0061689; C:tricellular tight junction; IDA:FlyBase. DR GO; GO:0061174; C:type I terminal bouton; IDA:FlyBase. DR GO; GO:0061176; C:type Ib terminal bouton; IDA:FlyBase. DR GO; GO:0004385; F:guanylate kinase activity; TAS:FlyBase. DR GO; GO:0019900; F:kinase binding; IEA:InterPro. DR GO; GO:0030714; P:anterior/posterior axis specification, follicular epithelium; IMP:BHF-UCL. DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:FlyBase. DR GO; GO:0045175; P:basal protein localization; IMP:FlyBase. DR GO; GO:0048149; P:behavioral response to ethanol; IMP:FlyBase. DR GO; GO:0060581; P:cell fate commitment involved in pattern specification; IMP:BHF-UCL. DR GO; GO:0001708; P:cell fate specification; IMP:BHF-UCL. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase. DR GO; GO:0007391; P:dorsal closure; TAS:FlyBase. DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:FlyBase. DR GO; GO:0051294; P:establishment of spindle orientation; IMP:FlyBase. DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central. DR GO; GO:0016334; P:establishment or maintenance of polarity of follicular epithelium; IGI:FlyBase. DR GO; GO:0016336; P:establishment or maintenance of polarity of larval imaginal disc epithelium; IMP:FlyBase. DR GO; GO:0030707; P:follicle cell of egg chamber development; IMP:BHF-UCL. DR GO; GO:0042332; P:gravitaxis; IMP:FlyBase. DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase. DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase. DR GO; GO:0007617; P:mating behavior; IMP:FlyBase. DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; TAS:FlyBase. DR GO; GO:0016333; P:morphogenesis of follicular epithelium; IMP:FlyBase. DR GO; GO:0016335; P:morphogenesis of larval imaginal disc epithelium; TAS:FlyBase. DR GO; GO:0045571; P:negative regulation of imaginal disc growth; IMP:FlyBase. DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase. DR GO; GO:0007399; P:nervous system development; IMP:FlyBase. DR GO; GO:0007318; P:pole plasm protein localization; IMP:BHF-UCL. DR GO; GO:0046956; P:positive phototaxis; IMP:FlyBase. DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase. DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central. DR GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central. DR GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0019991; P:septate junction assembly; TAS:FlyBase. DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW. DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:FlyBase. DR CDD; cd00071; GMPK; 1. DR CDD; cd00992; PDZ_signaling; 3. DR CDD; cd11861; SH3_DLG-like; 1. DR Gene3D; 2.30.42.10; -; 3. DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1. DR Gene3D; 1.10.287.470; Helix hairpin bin; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 2. DR InterPro; IPR016313; DLG1-like. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR015143; L27_1. DR InterPro; IPR004172; L27_dom. DR InterPro; IPR036892; L27_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR23119; DISCS LARGE; 1. DR PANTHER; PTHR23119:SF51; DISKS LARGE 1 TUMOR SUPPRESSOR PROTEIN; 1. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF09058; L27_1; 1. DR Pfam; PF00595; PDZ; 3. DR Pfam; PF00018; SH3_1; 1. DR PIRSF; PIRSF001741; MAGUK_DLGH; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM00569; L27; 1. DR SMART; SM00228; PDZ; 3. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF101288; L27 domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 3. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS51022; L27; 1. DR PROSITE; PS50106; PDZ; 3. DR PROSITE; PS50002; SH3; 1. DR Genevisible; P31007; DM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction; KW Cell membrane; Cytoplasm; Cytoskeleton; Developmental protein; KW Differentiation; Membrane; Neurogenesis; Phosphoprotein; KW Reference proteome; Repeat; SH3 domain; Transducer. FT CHAIN 1..970 FT /note="Disks large 1 tumor suppressor protein" FT /id="PRO_0000094538" FT DOMAIN 4..64 FT /note="L27" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365" FT DOMAIN 216..303 FT /note="PDZ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 330..421 FT /note="PDZ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 506..587 FT /note="PDZ 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 620..690 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 780..955 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100" FT REGION 161..209 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 424..477 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 168..209 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 496 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18327897" FT MOD_RES 714 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18327897" FT VAR_SEQ 1..92 FT /note="MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERVIRIFKSRLFQALLDI FT QEFYELTLLDDSKSIQQKTAETLQIATKWEKDGQAVKIAD -> MIDWVSIVRHSRRRF FT SNYVGSRSPVRMRRRRRQLTAPPPQQQQQQHYHQQQQQDQHQSRERQKKDKEKEKETEK FT DNESGGGIGSRYACCCAN (in isoform K)" FT /evidence="ECO:0000305" FT /id="VSP_039402" FT VAR_SEQ 1..37 FT /note="MPVKKQEAHRALELLEDYHARLSEPQDRALRIAIERV -> MTTRKKKRDGG FT GSGGGFIKKVSSLFNLDSLHKASSTK (in isoform A)" FT /evidence="ECO:0000305" FT /id="VSP_011403" FT VAR_SEQ 1..29 FT /note="MPVKKQEAHRALELLEDYHARLSEPQDRA -> MTTRKKKRDGGGSGGGFIK FT KVSSLFNLDS (in isoform E and isoform G)" FT /evidence="ECO:0000303|PubMed:12537569, FT ECO:0000303|PubMed:1651169, ECO:0000303|Ref.6" FT /id="VSP_011402" FT VAR_SEQ 1..7 FT /note="MPVKKQE -> MDSDTDSEREKSSDPNEGLLSSDDKTFHDDDEPAEDSSPAD FT DEEEPEEEECLLPQKKAQIRCDQDQPPLVVLVQPSAEAIEVRQEIDDTNPVAVAAKASD FT MDGDSQLEVMEHQMETVTEPDPEPPKCPTSLRDSVRESVECFYSAQDLLEYGHMLSSTS FT MVRTPDVESGYFEKSESDASRDEWEGPSSSSSGAARCRLLSGISGLSVSSSSRHSAEGL FT RMELSRFRTMIETLERESLEKSQSELQLKAKSKAKPKPKQRSHVQDAAGESGSEQGSER FT GFWSTIFGQAGLAISQDEEERIADIQK (in isoform F)" FT /evidence="ECO:0000303|PubMed:12537569, FT ECO:0000303|PubMed:12657668" FT /id="VSP_011401" FT VAR_SEQ 30..205 FT /note="Missing (in isoform E and isoform G)" FT /evidence="ECO:0000303|PubMed:12537569, FT ECO:0000303|PubMed:1651169, ECO:0000303|Ref.6" FT /id="VSP_011404" FT VAR_SEQ 38..205 FT /note="Missing (in isoform A)" FT /evidence="ECO:0000305" FT /id="VSP_011405" FT VAR_SEQ 93..151 FT /note="Missing (in isoform I, isoform H, isoform K and FT isoform L)" FT /evidence="ECO:0000303|PubMed:12537569, FT ECO:0000303|PubMed:12657668" FT /id="VSP_011406" FT VAR_SEQ 205 FT /note="T -> TLHKASSTK (in isoform L)" FT /evidence="ECO:0000303|PubMed:12657668" FT /id="VSP_011407" FT VAR_SEQ 206..267 FT /note="VNGDDSWLYEDIQLERGNSGLGFSIAGGTDNPHIGTDTSIYITKLISGGAAA FT ADGRLSINDI -> SQIQIQSLTQTYPNAHQRKRVLVSLHPHQHQHQSQIQHQHHYQLR FT HNNGIQAKMLKRAFEST (in isoform I)" FT /evidence="ECO:0000303|PubMed:12537569, FT ECO:0000303|PubMed:12657668" FT /id="VSP_011408" FT VAR_SEQ 268..970 FT /note="Missing (in isoform I)" FT /evidence="ECO:0000303|PubMed:12537569, FT ECO:0000303|PubMed:12657668" FT /id="VSP_011409" FT VAR_SEQ 473..519 FT /note="EPGSRYASTNVLAAVPPGTPRAVSTEDITREPRTITIQKGPQGLGFN -> A FT FMLCYTQDDANAEGGEIIYRVELPDMEQITLIYLENNDADYRKSSI (in isoform FT F)" FT /evidence="ECO:0000303|PubMed:12537569, FT ECO:0000303|PubMed:12657668" FT /id="VSP_011411" FT VAR_SEQ 473 FT /note="E -> GALNSMGQTVVDSPSIPQAAAAVAAAANASASASVIASNNTISNTTV FT TTVTATATASNSSSKLPPSLGANSSISISNSNSNSNSNNINNINSINNNNSSSSSTTAT FT VAAATPTAASAAAAAASSPPANSFYNNASMPALPVESNQTNNRSQSPQPRQ (in FT isoform A, isoform E and isoform G)" FT /evidence="ECO:0000303|PubMed:12537569, FT ECO:0000303|PubMed:1651169, ECO:0000303|Ref.6" FT /id="VSP_011410" FT VAR_SEQ 520..970 FT /note="Missing (in isoform F)" FT /evidence="ECO:0000303|PubMed:12537569, FT ECO:0000303|PubMed:12657668" FT /id="VSP_011412" FT VAR_SEQ 746 FT /note="P -> PNGVVSSTSEIDINNVNNNQSNEPQP (in isoform G)" FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.6" FT /id="VSP_011413" FT VAR_SEQ 747..761 FT /note="FMLCYTQDDANAEGA -> NGVVSSTSEIDINNVNNNQSNEPQP (in FT isoform A and isoform E)" FT /evidence="ECO:0000303|PubMed:1651169" FT /id="VSP_011414" FT VAR_SEQ 761 FT /note="A -> GEIIYRVELPDMEQITLIYLENNDADYP (in isoform L)" FT /evidence="ECO:0000303|PubMed:12657668" FT /id="VSP_011415" FT CONFLICT 365 FT /note="M -> T (in Ref. 1; AAA28468 and 2; AAQ01226)" FT /evidence="ECO:0000305" FT CONFLICT 369 FT /note="A -> R (in Ref. 1; AAA28468 and 2; AAQ01226)" FT /evidence="ECO:0000305" FT CONFLICT 395 FT /note="E -> G (in Ref. 6; ACV53090)" FT /evidence="ECO:0000305" FT HELIX 8..10 FT /evidence="ECO:0007829|PDB:4RP3" FT HELIX 11..21 FT /evidence="ECO:0007829|PDB:4RP3" FT HELIX 25..27 FT /evidence="ECO:0007829|PDB:4RP3" FT HELIX 28..58 FT /evidence="ECO:0007829|PDB:4RP3" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:4RP3" FT HELIX 67..83 FT /evidence="ECO:0007829|PDB:4RP3" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:4RP3" FT STRAND 87..90 FT /evidence="ECO:0007829|PDB:4RP3" FT STRAND 624..627 FT /evidence="ECO:0007829|PDB:3TVT" FT STRAND 651..656 FT /evidence="ECO:0007829|PDB:3TVT" FT STRAND 659..665 FT /evidence="ECO:0007829|PDB:3TVT" FT STRAND 679..681 FT /evidence="ECO:0007829|PDB:3TVT" FT HELIX 683..691 FT /evidence="ECO:0007829|PDB:3TVT" FT STRAND 769..776 FT /evidence="ECO:0007829|PDB:3TVT" FT STRAND 783..787 FT /evidence="ECO:0007829|PDB:3TVT" FT HELIX 790..800 FT /evidence="ECO:0007829|PDB:3TVT" FT TURN 802..804 FT /evidence="ECO:0007829|PDB:3TVT" FT TURN 822..824 FT /evidence="ECO:0007829|PDB:3TVT" FT HELIX 832..840 FT /evidence="ECO:0007829|PDB:3TVT" FT STRAND 844..850 FT /evidence="ECO:0007829|PDB:3TVT" FT STRAND 853..858 FT /evidence="ECO:0007829|PDB:3TVT" FT HELIX 859..868 FT /evidence="ECO:0007829|PDB:3TVT" FT STRAND 871..874 FT /evidence="ECO:0007829|PDB:3TVT" FT HELIX 879..886 FT /evidence="ECO:0007829|PDB:3TVT" FT STRAND 892..896 FT /evidence="ECO:0007829|PDB:3TVT" FT HELIX 901..906 FT /evidence="ECO:0007829|PDB:3TVT" FT HELIX 915..930 FT /evidence="ECO:0007829|PDB:3TVT" FT TURN 931..933 FT /evidence="ECO:0007829|PDB:3TVT" FT STRAND 935..938 FT /evidence="ECO:0007829|PDB:3TVT" FT HELIX 943..957 FT /evidence="ECO:0007829|PDB:3TVT" FT STRAND 960..965 FT /evidence="ECO:0007829|PDB:3TVT" FT CONFLICT P31007-1:355 FT /note="S -> D (in Ref. 1; AAA28468)" FT /evidence="ECO:0000305" SQ SEQUENCE 970 AA; 106673 MW; 544D1E1AD03B0674 CRC64; MPVKKQEAHR ALELLEDYHA RLSEPQDRAL RIAIERVIRI FKSRLFQALL DIQEFYELTL LDDSKSIQQK TAETLQIATK WEKDGQAVKI ADFIKSSNLN RNCAYEFNND ASSNQTNQSA LNQNPIANNV SAQAQAEALS RTFKSELEEI LNQRMRIESD TENAKEPTVE QQQKQQQAQQ RSSRSPQQQN PQQQQGSKSR SGSQTVNGDD SWLYEDIQLE RGNSGLGFSI AGGTDNPHIG TDTSIYITKL ISGGAAAADG RLSINDIIVS VNDVSVVDVP HASAVDALKK AGNVVKLHVK RKRGTATTPA AGSAAGDARD SAASGPKVIE IDLVKGGKGL GFSIAGGIGN QHIPGDNGIY VTKLMDGGAA QVDGRLSIGD KLIAVRTNGS EKNLENVTHE LAVATLKSIT DKVTLIIGKT QHLTTSASGG GGGGLSSGQQ LSQSQSQLAT SQSQSQVHQQ QHATPMVNSQ STEPGSRYAS TNVLAAVPPG TPRAVSTEDI TREPRTITIQ KGPQGLGFNI VGGEDGQGIY VSFILAGGPA DLGSELKRGD QLLSVNNVNL THATHEEAAQ ALKTSGGVVT LLAQYRPEEY NRFEARIQEL KQQAALGAGG SGTLLRTTQK RSLYVRALFD YDPNRDDGLP SRGLPFKHGD ILHVTNASDD EWWQARRVLG DNEDEQIGIV PSKRRWERKM RARDRSVKFQ GHAAANNNLD KQSTLDRKKK NFTFSRKFPF MKSRDEKNED GSDQEPFMLC YTQDDANAEG ASEENVLSYE AVQRLSINYT RPVIILGPLK DRINDDLISE YPDKFGSCVP HTTRPKREYE VDGRDYHFVS SREQMERDIQ NHLFIEAGQY NDNLYGTSVA SVREVAEKGK HCILDVSGNA IKRLQVAQLY PVAVFIKPKS VDSVMEMNRR MTEEQAKKTY ERAIKMEQEF GEYFTGVVQG DTIEEIYSKV KSMIWSQSGP TIWVPSKESL //