DLG1_MOUSE
ID DLG1_MOUSE Reviewed; 905 AA.
AC Q811D0; Q62402; Q6PGB5; Q8CGN7;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Disks large homolog 1;
DE AltName: Full=Embryo-dlg/synapse-associated protein 97;
DE Short=E-dlg/SAP97;
DE AltName: Full=Synapse-associated protein 97;
DE Short=SAP-97;
DE Short=SAP97;
GN Name=Dlg1; Synonyms=Dlgh1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Bone marrow;
RX PubMed=9434093; DOI=10.1016/s0925-4439(97)00059-8;
RA Lin L., Sahr K.E., Chishti A.H.;
RT "Identification of the mouse homologue of human discs large and rat SAP97
RT genes.";
RL Biochim. Biophys. Acta 1362:1-5(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RA Mao P., Tao Y.-X., Levine C., Tao F., Li D., Johns R.A.;
RT "Cloning and characterization of a novel mouse homolog E-dlg/SAP97 of the
RT Drosophila discs large tumor suppressor binds to SAP102.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH EZR.
RX PubMed=8922391; DOI=10.1083/jcb.135.4.1125;
RA Lue R.A., Brandin E., Chan E.P., Branton D.;
RT "Two independent domains of hDlg are sufficient for subcellular targeting:
RT the PDZ1-2 conformational unit and an alternatively spliced domain.";
RL J. Cell Biol. 135:1125-1137(1996).
RN [5]
RP INTERACTION WITH APC AND CTNNB1.
RX PubMed=8638125; DOI=10.1126/science.272.5264.1020;
RA Matsumine A., Ogai A., Senda T., Okumura N., Satoh K., Baeg G.-H.,
RA Kawahara T., Kobayashi S., Okada M., Toyoshima K., Akiyama T.;
RT "Binding of APC to the human homolog of the Drosophila discs large tumor
RT suppressor protein.";
RL Science 272:1020-1023(1996).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11238884; DOI=10.1128/mcb.21.5.1475-1483.2001;
RA Caruana G., Bernstein A.;
RT "Craniofacial dysmorphogenesis including cleft palate in mice with an
RT insertional mutation in the discs large gene.";
RL Mol. Cell. Biol. 21:1475-1483(2001).
RN [7]
RP INTERACTION WITH KCNA5 AND CAV3.
RX PubMed=15277200; DOI=10.1152/ajpheart.00152.2004;
RA Folco E.J., Liu G.-X., Koren G.;
RT "Caveolin-3 and SAP97 form a scaffolding protein complex that regulates the
RT voltage-gated potassium channel Kv1.5.";
RL Am. J. Physiol. 287:H681-H690(2004).
RN [8]
RP INTERACTION WITH HTR2A.
RX PubMed=14988405; DOI=10.1074/jbc.m312106200;
RA Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A.,
RA Bockaert J., Marin P.;
RT "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of
RT PDZ proteins.";
RL J. Biol. Chem. 279:20257-20266(2004).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=16519681; DOI=10.1111/j.1742-4658.2006.05140.x;
RA Kantardzhieva A., Alexeeva S., Versteeg I., Wijnholds J.;
RT "MPP3 is recruited to the MPP5 protein scaffold at the retinal outer
RT limiting membrane.";
RL FEBS J. 273:1152-1165(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-399, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-573; SER-575;
RP SER-598 AND SER-619, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION, INTERACTION WITH ADAM10, AND TISSUE SPECIFICITY.
RX PubMed=23676497; DOI=10.1172/jci65401;
RA Marcello E., Saraceno C., Musardo S., Vara H., de la Fuente A.G.,
RA Pelucchi S., Di Marino D., Borroni B., Tramontano A., Perez-Otano I.,
RA Padovani A., Giustetto M., Gardoni F., Di Luca M.;
RT "Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's
RT disease.";
RL J. Clin. Invest. 123:2523-2538(2013).
RN [14]
RP INTERACTION WITH ADGRA2.
RX PubMed=25558062; DOI=10.1016/j.celrep.2014.12.020;
RA Posokhova E., Shukla A., Seaman S., Volate S., Hilton M.B., Wu B.,
RA Morris H., Swing D.A., Zhou M., Zudaire E., Rubin J.S., St Croix B.;
RT "GPR124 functions as a WNT7-specific coactivator of canonical beta-catenin
RT signaling.";
RL Cell Rep. 10:123-130(2015).
CC -!- FUNCTION: Essential multidomain scaffolding protein required for normal
CC development. Recruits channels, receptors and signaling molecules to
CC discrete plasma membrane domains in polarized cells. Regulates the
CC excitability of cardiac myocytes by modulating the functional
CC expression of Kv4 channels (By similarity). Functional regulator of
CC Kv1.5 channel (By similarity). May play a role in adherens junction
CC assembly, signal transduction, cell proliferation, synaptogenesis and
CC lymphocyte activation. During long-term depression in hippocampal
CC neurons, it recruits ADAM10 to the plasma membrane (PubMed:23676497).
CC {ECO:0000250, ECO:0000269|PubMed:11238884,
CC ECO:0000269|PubMed:23676497}.
CC -!- SUBUNIT: Homotetramer (Probable). Interacts (via guanylate kinase-like
CC domain) with DLGAP1, DLGAP2, DLGAP3, DLGAP4, and MAP1A (By similarity).
CC Interacts (via guanylate kinase-like domain) with KIF13B (By
CC similarity). May interact with HTR2A (PubMed:14988405). Interacts (via
CC PDZ domains) with GRIA1 (By similarity). Interacts (via PDZ domains)
CC with GRIN2A (By similarity). Interacts (via PDZ domains) with KCND2 and
CC KCND3 (By similarity). Interacts (via PDZ domains) with KCNA1, KCNA2,
CC KCNA3, KCNA4, and ADGRA3 (By similarity). Interacts with KCNF1 (By
CC similarity). Interacts with CAMK2 (By similarity). Interacts with
CC cytoskeleton-associated protein EPB41 (By similarity). Interacts with
CC cytoskeleton-associated protein EZR (PubMed:8922391). Found in a
CC complex with KCNA5 and CAV3 (PubMed:15277200). Found in a complex with
CC APC and CTNNB1 (PubMed:8638125). Interacts with CDH1 through binding to
CC PIK3R1 (By similarity). Forms multiprotein complexes with CASK, LIN7A,
CC LIN7B, LIN7C, APBA1, and KCNJ12 (By similarity). Interacts with TOPK
CC (By similarity). Forms a tripartite complex composed of DLG1, MPP7 and
CC LIN7 (LIN7A or LIN7C) (By similarity). May interact with TJAP1 (By
CC similarity). Interacts with PTEN (By similarity). Interacts with LRFN1,
CC LRFN2, LRFN4 and SFPQ (By similarity). Interacts with FRMPD4 (via C-
CC terminus) (By similarity). Interacts (via PDZ domains) with ADGRA2 (via
CC PDZ-binding motif) (PubMed:25558062). Interacts with ADAM10; this
CC interaction recruits ADAM10 to the cell membrane during long-term
CC depression in hippocampal neurons (PubMed:23676497). Interacts with
CC DGKI (via PDZ-binding motif) (By similarity). Interacts (via PDZ
CC domains) with MARCHF2 (via PDZ domain); the interaction leads to DLG1
CC ubiqtuitination and degradation (By similarity).
CC {ECO:0000250|UniProtKB:Q12959, ECO:0000250|UniProtKB:Q62696,
CC ECO:0000269|PubMed:14988405, ECO:0000269|PubMed:15277200,
CC ECO:0000269|PubMed:23676497, ECO:0000269|PubMed:25558062,
CC ECO:0000269|PubMed:8638125, ECO:0000269|PubMed:8922391, ECO:0000305}.
CC -!- INTERACTION:
CC Q811D0; Q62108: Dlg4; NbExp=4; IntAct=EBI-514290, EBI-300895;
CC Q811D0; Q80TG9: Lrfn2; NbExp=3; IntAct=EBI-514290, EBI-877092;
CC Q811D0; Q810U4: Nrcam; NbExp=6; IntAct=EBI-514290, EBI-8321816;
CC Q811D0; P06463: E6; Xeno; NbExp=2; IntAct=EBI-514290, EBI-1186926;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q62696};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q12959}. Basolateral
CC cell membrane {ECO:0000250|UniProtKB:Q62696}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q62696}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q62696}. Synapse {ECO:0000250|UniProtKB:Q62696}.
CC Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q62696}. Cell junction
CC {ECO:0000250|UniProtKB:Q12959}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q12959}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q12959}. Note=Colocalizes with EPB41 at regions
CC of intercellular contacts. Basolateral in epithelial cells. May also
CC associate with endoplasmic reticulum membranes. Mainly found in neurons
CC soma, moderately found at postsynaptic densities.
CC {ECO:0000250|UniProtKB:Q12959, ECO:0000250|UniProtKB:Q62696}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q811D0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q811D0-2; Sequence=VSP_012866, VSP_012867;
CC Name=3;
CC IsoId=Q811D0-3; Sequence=VSP_012868;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level)
CC (PubMed:23676497). Expressed in the outer limiting membrane and outer
CC plexiform layer in the retina (at protein level) (PubMed:16519681).
CC Expressed in epithelial, mesenchymal, neuronal, endothelial and
CC hematopoietic cells during embryogenesis. Expressed in fibroblasts and
CC T-cells. Widely expressed in adult mice. {ECO:0000269|PubMed:11238884,
CC ECO:0000269|PubMed:16519681, ECO:0000269|PubMed:23676497}.
CC -!- DOMAIN: The PDZ domains may also mediate association to membranes by
CC binding to EPB41 and ADGRA2 together with the L27 domain that binds
CC CASK and DLG2. {ECO:0000250}.
CC -!- DOMAIN: The L27 domain may regulate DLG1 self-association. The N-
CC terminal alternatively spliced region is capable of binding several SH3
CC domains and also moderates the level of protein oligomerization (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by MAPK12. Phosphorylation of Ser-232 regulates
CC association with GRIN2A (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated; by MARCHF2 which results in its degradation.
CC {ECO:0000250|UniProtKB:Q12959}.
CC -!- DISRUPTION PHENOTYPE: Mice have craniofacial abnormalities as well as a
CC cleft palate. They are smaller than heterozygous littermates, unable to
CC feed and die within 24 hours of birth. {ECO:0000269|PubMed:11238884}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; U93309; AAC31653.1; -; mRNA.
DR EMBL; AY159380; AAN87264.1; -; mRNA.
DR EMBL; BC047142; AAH47142.1; -; mRNA.
DR EMBL; BC057118; AAH57118.1; -; mRNA.
DR CCDS; CCDS28107.1; -. [Q811D0-3]
DR CCDS; CCDS57025.1; -. [Q811D0-1]
DR RefSeq; NP_001239362.1; NM_001252433.1. [Q811D0-2]
DR RefSeq; NP_001239363.1; NM_001252434.1.
DR RefSeq; NP_001239364.1; NM_001252435.1. [Q811D0-1]
DR RefSeq; NP_031888.2; NM_007862.3. [Q811D0-3]
DR RefSeq; XP_006521831.1; XM_006521768.3. [Q811D0-1]
DR PDB; 4OAJ; X-ray; 2.30 A; A=317-406.
DR PDBsum; 4OAJ; -.
DR AlphaFoldDB; Q811D0; -.
DR SMR; Q811D0; -.
DR BioGRID; 199228; 40.
DR CORUM; Q811D0; -.
DR DIP; DIP-31591N; -.
DR IntAct; Q811D0; 21.
DR MINT; Q811D0; -.
DR STRING; 10090.ENSMUSP00000064280; -.
DR iPTMnet; Q811D0; -.
DR PhosphoSitePlus; Q811D0; -.
DR SwissPalm; Q811D0; -.
DR EPD; Q811D0; -.
DR jPOST; Q811D0; -.
DR MaxQB; Q811D0; -.
DR PaxDb; Q811D0; -.
DR PeptideAtlas; Q811D0; -.
DR PRIDE; Q811D0; -.
DR ProteomicsDB; 279721; -. [Q811D0-1]
DR ProteomicsDB; 279722; -. [Q811D0-2]
DR ProteomicsDB; 279723; -. [Q811D0-3]
DR ABCD; Q811D0; 2 sequenced antibodies.
DR Antibodypedia; 4273; 293 antibodies from 41 providers.
DR DNASU; 13383; -.
DR Ensembl; ENSMUST00000064477; ENSMUSP00000064280; ENSMUSG00000022770. [Q811D0-3]
DR Ensembl; ENSMUST00000100001; ENSMUSP00000097581; ENSMUSG00000022770. [Q811D0-1]
DR Ensembl; ENSMUST00000115205; ENSMUSP00000110859; ENSMUSG00000022770. [Q811D0-1]
DR GeneID; 13383; -.
DR KEGG; mmu:13383; -.
DR UCSC; uc007yxo.2; mouse. [Q811D0-1]
DR UCSC; uc007yxp.2; mouse. [Q811D0-3]
DR UCSC; uc007yxs.2; mouse. [Q811D0-2]
DR CTD; 1739; -.
DR MGI; MGI:107231; Dlg1.
DR VEuPathDB; HostDB:ENSMUSG00000022770; -.
DR eggNOG; KOG0708; Eukaryota.
DR GeneTree; ENSGT00940000159409; -.
DR InParanoid; Q811D0; -.
DR OMA; TQHMENH; -.
DR OrthoDB; 807583at2759; -.
DR PhylomeDB; Q811D0; -.
DR TreeFam; TF323171; -.
DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-MMU-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR BioGRID-ORCS; 13383; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Dlg1; mouse.
DR PRO; PR:Q811D0; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q811D0; protein.
DR Bgee; ENSMUSG00000022770; Expressed in metanephric cortical collecting duct and 268 other tissues.
DR ExpressionAtlas; Q811D0; baseline and differential.
DR Genevisible; Q811D0; MM.
DR GO; GO:0005912; C:adherens junction; TAS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI.
DR GO; GO:0030054; C:cell junction; IDA:MGI.
DR GO; GO:0031253; C:cell projection membrane; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR GO; GO:0043219; C:lateral loop; IDA:BHF-UCL.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; ISO:MGI.
DR GO; GO:0035748; C:myelin sheath abaxonal region; IDA:BHF-UCL.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0033270; C:paranode region of axon; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0097060; C:synaptic membrane; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; IDA:MGI.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0097016; F:L27 domain binding; ISO:MGI.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; IMP:BHF-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; IDA:SynGO.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; IMP:MGI.
DR GO; GO:0032147; P:activation of protein kinase activity; IMP:MGI.
DR GO; GO:0042982; P:amyloid precursor protein metabolic process; IGI:MGI.
DR GO; GO:0030953; P:astral microtubule organization; ISO:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0043622; P:cortical microtubule organization; ISO:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0001935; P:endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0051660; P:establishment of centrosome localization; ISO:MGI.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0060022; P:hard palate development; IMP:MGI.
DR GO; GO:0001771; P:immunological synapse formation; IMP:MGI.
DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR GO; GO:0031579; P:membrane raft organization; IMP:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0030432; P:peristalsis; IMP:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0048639; P:positive regulation of developmental growth; TAS:UniProtKB.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; TAS:UniProtKB.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0031503; P:protein-containing complex localization; ISO:MGI.
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:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR GO; GO:0031641; P:regulation of myelination; IMP:MGI.
DR GO; GO:1903764; P:regulation of potassium ion export across plasma membrane; IMP:BHF-UCL.
DR GO; GO:1903286; P:regulation of potassium ion import; IMP:BHF-UCL.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:1902473; P:regulation of protein localization to synapse; IDA:UniProtKB.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:1903760; P:regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IMP:BHF-UCL.
DR GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
DR GO; GO:0042110; P:T cell activation; IMP:MGI.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR GO; GO:0048729; P:tissue morphogenesis; IMP:MGI.
DR GO; GO:0001657; P:ureteric bud development; IMP:MGI.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016313; DLG1-like.
DR InterPro; IPR019590; DLG1_PEST_dom.
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; IPR019583; PDZ_assoc.
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; PF10608; MAGUK_N_PEST; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF10600; PDZ_assoc; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 1.
DR SMART; SM01277; MAGUK_N_PEST; 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 junction; Cell membrane;
KW Cytoplasm; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Synapse; Ubl conjugation.
FT CHAIN 1..905
FT /note="Disks large homolog 1"
FT /id="PRO_0000094549"
FT DOMAIN 4..64
FT /note="L27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 224..311
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 319..406
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 466..547
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 581..651
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 715..890
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 162..212
FT /note="Interaction with SH3 domains"
FT /evidence="ECO:0000250"
FT REGION 224..546
FT /note="Required for interaction with MARCHF2"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT REGION 420..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62696"
FT MOD_RES 399
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 835
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62696"
FT VAR_SEQ 162..194
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012866"
FT VAR_SEQ 670..681
FT /note="EIPDDMGSKGLK -> SFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_012867"
FT VAR_SEQ 670..681
FT /note="EIPDDMGSKGLK -> QSFNDKRKKNLFSRKFPFYKNKDQSEQETSDADQ
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9434093"
FT /id="VSP_012868"
FT CONFLICT 263
FT /note="A -> R (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="I -> V (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="P -> L (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="V -> I (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="H -> R (in Ref. 2; AAN87264)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="G -> A (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 550..551
FT /note="YS -> SR (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="S -> R (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="L -> P (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="V -> A (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="Y -> C (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="Y -> I (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 769..770
FT /note="QM -> RV (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT CONFLICT 900
FT /note="P -> L (in Ref. 1; AAC31653)"
FT /evidence="ECO:0000305"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:4OAJ"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:4OAJ"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:4OAJ"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:4OAJ"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:4OAJ"
FT HELIX 384..392
FT /evidence="ECO:0007829|PDB:4OAJ"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:4OAJ"
FT MOD_RES Q811D0-2:676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES Q811D0-3:710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
SQ SEQUENCE 905 AA; 100120 MW; 950A465824AE3210 CRC64;
MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL
LDNPKCVDHS KQCEPVQPVT TWEIASLPST AVTSETLPGS LSPPVEKYRY QDEEVLPPEH
ISPQVTNEVL GPELVHVSEK NLSEIENVHG FVSHSHISPI KPTEAVPPSS PIVPVTPALP
VPAESTVVLP SAPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG
GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EADVRDVTHS KAVEALKEAG
SIVRLYVKRR KPASEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV TKIIEGGAAH
KDGKLQIGDK LLAVNSVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTSMYI NDGYAPPDIT
NSSSQSVDNH VSPSSCLGQT PTSPARYSPI SKAVLGDDEI TREPRKVVLH RGSTGLGFNI
VGGEDGEGIF ISFILAGGPA DLSGELRKGD RIISVNSVDL RAASHEQAAA ALKNAGQAVT
IVAQYRPEEY SRFEAKIHDL REQMMNSSVS SGSGSLRTSQ KRSLYVRALF DYDKTKDSGL
PSQGLNFRFG DILHVINASD DEWWQARQVT PDGESDEVGV IPSKRRVEKK ERARLKTVKF
NSKTRGDKGE IPDDMGSKGL KHVTSNASDS ESSYRGQEEY VLSYEPVNQQ EVNYTRPVII
LGPMKDRVND DLISEFPDKF GSCVPHTTRP KRDYEVDGRD YHFVTSREQM EKDIQEHKFI
EAGQYNNHLY GTSVQSVRAV AEKGKHCILD VSGNAIKRLQ IAQLYPISIF IKPKSMENIM
EMNKRLTEEQ ARKTFERAMK LEQEFTEHFT AIVQGDTLED IYNQVKQIIE EQSGPYIWVP
AKEKL
