DLG1_DROME
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 03-AUG-2022, entry version 230.
DE RecName: Full=Disks large 1 tumor suppressor protein;
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).
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}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:10884224, ECO:0000269|PubMed:1651169}.
CC Cell 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. {ECO:0000269|PubMed:1651169}.
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};
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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 DIP; DIP-31531N; -.
DR IntAct; P31007; 44.
DR MINT; P31007; -.
DR STRING; 7227.FBpp0290503; -.
DR iPTMnet; P31007; -.
DR PaxDb; P31007; -.
DR PRIDE; P31007; -.
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 CTD; 1739; -.
DR FlyBase; FBgn0001624; dlg1.
DR VEuPathDB; VectorBase:FBgn0001624; -.
DR GeneTree; ENSGT00940000167723; -.
DR InParanoid; P31007; -.
DR OMA; XYARFEA; -.
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-6798695; Neutrophil degranulation.
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 tissues.
DR ExpressionAtlas; P31007; baseline and differential.
DR Genevisible; P31007; DM.
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:0030054; C:cell junction; IBA:GO_Central.
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: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: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:0030707; P:ovarian follicle cell development; IMP:BHF-UCL.
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:0008104; P:protein localization; 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 Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
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 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; SSF101288; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 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.
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
