DLG1_RAT
ID DLG1_RAT Reviewed; 911 AA.
AC Q62696;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Disks large homolog 1;
DE AltName: Full=Synapse-associated protein 97;
DE Short=SAP-97;
DE Short=SAP97;
GN Name=Dlg1; Synonyms=Dlgh1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=7891172; DOI=10.1523/jneurosci.15-03-02354.1995;
RA Mueller B.M., Kistner U., Veh R.W., Cases-Langhoff C., Becker B.,
RA Gundelfinger E.D., Garner C.C.;
RT "Molecular characterization and spatial distribution of SAP97, a novel
RT presynaptic protein homologous to SAP90 and the Drosophila discs-large
RT tumor suppressor protein.";
RL J. Neurosci. 15:2354-2366(1995).
RN [2]
RP INTERACTION WITH DLGAP1; DLGAP2; DLGAP3 AND DLGAP4.
RX PubMed=9115257; DOI=10.1074/jbc.272.18.11943;
RA Takeuchi M., Hata Y., Hirao K., Toyoda A., Irie M., Takai Y.;
RT "SAPAPs. A family of PSD-95/SAP90-associated proteins localized at
RT postsynaptic density.";
RL J. Biol. Chem. 272:11943-11951(1997).
RN [3]
RP INTERACTION WITH GRIA1.
RX PubMed=9677374; DOI=10.1074/jbc.273.31.19518;
RA Leonard A.S., Davare M.A., Horne M.C., Garner C.C., Hell J.W.;
RT "SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-
RT propionic acid receptor GluR1 subunit.";
RL J. Biol. Chem. 273:19518-19524(1998).
RN [4]
RP INTERACTION WITH MAP1A.
RX PubMed=9786987; DOI=10.1523/jneurosci.18-21-08805.1998;
RA Brenman J.E., Topinka J.R., Cooper E.C., McGee A.W., Rosen J., Milroy T.,
RA Ralston H.J., Bredt D.S.;
RT "Localization of postsynaptic density-93 to dendritic microtubules and
RT interaction with microtubule-associated protein 1A.";
RL J. Neurosci. 18:8805-8813(1998).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=10629225; DOI=10.1083/jcb.148.1.147;
RA Tiffany A.M., Manganas L.N., Kim E., Hsueh Y.P., Sheng M., Trimmer J.S.;
RT "PSD-95 and SAP97 exhibit distinct mechanisms for regulating K(+) channel
RT surface expression and clustering.";
RL J. Cell Biol. 148:147-158(2000).
RN [6]
RP INTERACTION WITH CASK, AND SUBCELLULAR LOCATION.
RX PubMed=11865057; DOI=10.1128/mcb.22.6.1778-1791.2002;
RA Lee S., Fan S., Makarova O., Straight S., Margolis B.;
RT "A novel and conserved protein-protein interaction domain of mammalian Lin-
RT 2/CASK binds and recruits SAP97 to the lateral surface of epithelia.";
RL Mol. Cell. Biol. 22:1778-1791(2002).
RN [7]
RP INDUCTION BY BDNF.
RX PubMed=14597197; DOI=10.1016/j.ydbio.2003.07.008;
RA Jourdi H., Iwakura Y., Narisawa-Saito M., Ibaraki K., Xiong H.,
RA Watanabe M., Hayashi Y., Takei N., Nawa H.;
RT "Brain-derived neurotrophic factor signal enhances and maintains the
RT expression of AMPA receptor-associated PDZ proteins in developing cortical
RT neurons.";
RL Dev. Biol. 263:216-230(2003).
RN [8]
RP MUTAGENESIS OF SER-232, PHOSPHORYLATION AT SER-232, AND INTERACTION WITH
RP GRIN2A.
RX PubMed=12933808; DOI=10.1074/jbc.m303576200;
RA Gardoni F., Mauceri D., Fiorentini C., Bellone C., Missale C.,
RA Cattabeni F., Di Luca M.;
RT "CaMKII-dependent phosphorylation regulates SAP97/NR2A interaction.";
RL J. Biol. Chem. 278:44745-44752(2003).
RN [9]
RP INTERACTION WITH CASK; LIN7A; LIN7B; LIN7C; APBA1 AND KCNJ12, AND FUNCTION.
RX PubMed=14960569; DOI=10.1074/jbc.m400284200;
RA Leonoudakis D., Conti L.R., Radeke C.M., McGuire L.M., Vandenberg C.A.;
RT "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and
RT Mint1 is associated with inward rectifier Kir2 potassium channels.";
RL J. Biol. Chem. 279:19051-19063(2004).
RN [10]
RP MUTAGENESIS OF SER-39, PHOSPHORYLATION AT SER-39, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=15044483; DOI=10.1074/jbc.m402796200;
RA Mauceri D., Cattabeni F., Di Luca M., Gardoni F.;
RT "Calcium/calmodulin-dependent protein kinase II phosphorylation drives
RT synapse-associated protein 97 into spines.";
RL J. Biol. Chem. 279:23813-23821(2004).
RN [11]
RP FUNCTION.
RX PubMed=15504326; DOI=10.1016/j.neuron.2004.10.012;
RA Nakagawa T., Futai K., Lashuel H.A., Lo I., Okamoto K., Walz T.,
RA Hayashi Y., Sheng M.;
RT "Quaternary structure, protein dynamics, and synaptic function of SAP97
RT controlled by L27 domain interactions.";
RL Neuron 44:453-467(2004).
RN [12]
RP INTERACTION WITH PTEN.
RX PubMed=15951562; DOI=10.1074/jbc.m504761200;
RA Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C.,
RA Antonarakis S.E., Pulido R.;
RT "Binding of PTEN to specific PDZ domains contributes to PTEN protein
RT stability and phosphorylation by microtubule-associated serine/threonine
RT kinases.";
RL J. Biol. Chem. 280:28936-28943(2005).
RN [13]
RP INTERACTION WITH LRFN2.
RX PubMed=16495444; DOI=10.1523/jneurosci.3799-05.2006;
RA Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K., Wenthold R.J.;
RT "A novel family of adhesion-like molecules that interacts with the NMDA
RT receptor.";
RL J. Neurosci. 26:2174-2183(2006).
RN [14]
RP INTERACTION WITH LRFN1.
RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K.,
RA Kim E.;
RT "SALM synaptic cell adhesion-like molecules regulate the differentiation of
RT excitatory synapses.";
RL Neuron 50:233-245(2006).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=17980554; DOI=10.1016/j.cellsig.2007.08.019;
RA Cao Z., Huett A., Kuballa P., Giallourakis C., Xavier R.J.;
RT "DLG1 is an anchor for the E3 ligase MARCH2 at sites of cell-cell
RT contact.";
RL Cell. Signal. 20:73-82(2008).
RN [16]
RP INTERACTION WITH FRMPD4.
RX PubMed=19118189; DOI=10.1523/jneurosci.3112-08.2008;
RA Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B.,
RA Eom S.H., Kim H., Kim E.;
RT "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
RT regulates dendritic spine morphogenesis.";
RL J. Neurosci. 28:14546-14556(2008).
RN [17]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP KCND2; KCND3 AND CAMK2.
RX PubMed=19213956; DOI=10.1161/circresaha.108.191007;
RA El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H.,
RA Coulombe A., Jeromin A., Hatem S.N.;
RT "Kv4 potassium channels form a tripartite complex with the anchoring
RT protein SAP97 and CaMKII in cardiac myocytes.";
RL Circ. Res. 104:758-769(2009).
RN [18]
RP INTERACTION WITH DGKI.
RX PubMed=21119615; DOI=10.1038/emboj.2010.286;
RA Yang J., Seo J., Nair R., Han S., Jang S., Kim K., Han K., Paik S.K.,
RA Choi J., Lee S., Bae Y.C., Topham M.K., Prescott S.M., Rhee J.S.,
RA Choi S.Y., Kim E.;
RT "DGKiota regulates presynaptic release during mGluR-dependent LTD.";
RL EMBO J. 30:165-180(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-138; SER-618 AND
RP SER-841, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Essential multidomain scaffolding protein required for normal
CC development (By similarity). Recruits channels, receptors and signaling
CC molecules to discrete plasma membrane domains in polarized cells.
CC Regulates the excitability of cardiac myocytes by modulating the
CC functional expression of Kv4 channels. Functional regulator of Kv1.5
CC channel (By similarity). May play a role in adherens junction assembly,
CC signal transduction, cell proliferation, synaptogenesis and lymphocyte
CC activation. During long-term depression in hippocampal neurons, it
CC recruits ADAM10 to the plasma membrane (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q12959, ECO:0000269|PubMed:14960569,
CC ECO:0000269|PubMed:15044483, ECO:0000269|PubMed:15504326,
CC ECO:0000269|PubMed:19213956}.
CC -!- SUBUNIT: Homotetramer (Probable). Interacts (via guanylate kinase-like
CC domain) with DLGAP1, DLGAP2, DLGAP3, DLGAP4 and MAP1A (PubMed:9115257,
CC PubMed:9786987). Interacts (via guanylate kinase-like domain) with
CC KIF13B (By similarity). May interact with HTR2A (By similarity).
CC Interacts (via PDZ domains) with GRIA1 (PubMed:9677374). Interacts (via
CC PDZ domains) with GRIN2A (PubMed:12933808). Interacts (via PDZ domains)
CC with KCND2 and KCND3 (PubMed:19213956). Interacts (via PDZ domains)
CC with KCNA1, KCNA2, KCNA3 and KCNA4 (By similarity). Interacts (via PDZ
CC domains) with ADGRA3 (By similarity). Interacts with KCNF1 (By
CC similarity). Interacts with CAMK2 (PubMed:19213956). Interacts with
CC cytoskeleton-associated protein EPB41 (By similarity). Interacts with
CC cytoskeleton-associated protein EZR (By similarity). Found in a complex
CC with KCNA5 and CAV3 (By similarity). Found in a complex with APC and
CC CTNNB1 (By similarity). Interacts with CDH1 through binding to PIK3R1
CC (By similarity). Forms multiprotein complexes with CASK, LIN7A, LIN7B,
CC LIN7C, APBA1, and KCNJ12 (PubMed:11865057, PubMed:14960569). Interacts
CC with TOPK (By similarity). Forms a tripartite complex composed of DLG1,
CC MPP7 and LIN7 (LIN7A or LIN7C) (By similarity). May interact with TJAP1
CC (By similarity). Interacts with PTEN (PubMed:15951562). Interacts with
CC FRMPD4 (via C-terminus) (PubMed:19118189). Interacts with LRFN1 and
CC LRFN2 (PubMed:16495444, PubMed:16630835). Interacts with LRFN4 and SFPQ
CC (By similarity). Interacts (via PDZ domains) with ADGRA2 (via PDZ-
CC binding motif) (By similarity). Interacts with ADAM10; this interaction
CC recruits ADAM10 to the cell membrane during long-term depression in
CC hippocampal neurons (By similarity). Interacts with DGKI (via PDZ-
CC binding motif) (PubMed:21119615). Interacts (via PDZ domains) with
CC MARCHF2 (via PDZ domain); the interaction leads to DLG1 ubiqtuitination
CC and degradation (By similarity). {ECO:0000250|UniProtKB:Q12959,
CC ECO:0000250|UniProtKB:Q811D0, ECO:0000269|PubMed:11865057,
CC ECO:0000269|PubMed:12933808, ECO:0000269|PubMed:14960569,
CC ECO:0000269|PubMed:15951562, ECO:0000269|PubMed:16495444,
CC ECO:0000269|PubMed:16630835, ECO:0000269|PubMed:19118189,
CC ECO:0000269|PubMed:19213956, ECO:0000269|PubMed:21119615,
CC ECO:0000269|PubMed:9115257, ECO:0000269|PubMed:9677374,
CC ECO:0000269|PubMed:9786987, ECO:0000305}.
CC -!- INTERACTION:
CC Q62696; F1MAB7: Dgki; NbExp=3; IntAct=EBI-389325, EBI-8523614;
CC Q62696; O08560: Dgkz; NbExp=4; IntAct=EBI-389325, EBI-8570505;
CC Q62696; P31016: Dlg4; NbExp=2; IntAct=EBI-389325, EBI-375655;
CC Q62696; Q64273: Kcnj2; NbExp=3; IntAct=EBI-389325, EBI-703577;
CC Q62696; Q460M5: Lrfn2; NbExp=2; IntAct=EBI-389325, EBI-877185;
CC Q62696; P34926: Map1a; NbExp=2; IntAct=EBI-389325, EBI-631571;
CC Q62696; Q9Y297: BTRC; Xeno; NbExp=3; IntAct=EBI-389325, EBI-307461;
CC Q62696; P35347: Crhr1; Xeno; NbExp=3; IntAct=EBI-389325, EBI-16879653;
CC Q62696; O14490: DLGAP1; Xeno; NbExp=2; IntAct=EBI-389325, EBI-1753207;
CC Q62696; P89079: E4; Xeno; NbExp=4; IntAct=EBI-389325, EBI-7401124;
CC Q62696; Q8VDU0: Gpsm2; Xeno; NbExp=7; IntAct=EBI-389325, EBI-7575403;
CC Q62696; E9Q4K7: Kif13b; Xeno; NbExp=2; IntAct=EBI-389325, EBI-9085496;
CC Q62696; P60484: PTEN; Xeno; NbExp=2; IntAct=EBI-389325, EBI-696162;
CC Q62696; B1AYL1: Scn7a; Xeno; NbExp=3; IntAct=EBI-389325, EBI-8068354;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19213956};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q12959}. Basolateral
CC cell membrane {ECO:0000269|PubMed:11865057}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:10629225, ECO:0000269|PubMed:15044483}.
CC Postsynaptic density {ECO:0000269|PubMed:15044483}. Synapse
CC {ECO:0000269|PubMed:10629225}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:19213956}. Cell junction
CC {ECO:0000269|PubMed:17980554}. 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
CC (PubMed:11865057). May also associate with endoplasmic reticulum
CC membranes (PubMed:10629225, PubMed:15044483). Mainly found in neurons
CC soma, moderately found at postsynaptic densities (PubMed:15044483).
CC {ECO:0000250|UniProtKB:Q12959, ECO:0000269|PubMed:10629225,
CC ECO:0000269|PubMed:11865057, ECO:0000269|PubMed:15044483}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Strongly expressed in epithelial
CC cells, in the small intestine it is only detected in the vili.
CC Expressed in brain, heart (at protein level), muscle, lung and liver.
CC In the brain it was detected in olfactory bulbs, cerebral cortex,
CC hippocampus, and spinal cord (at protein level).
CC {ECO:0000269|PubMed:19213956, ECO:0000269|PubMed:7891172}.
CC -!- INDUCTION: By BDNF. {ECO:0000269|PubMed:14597197}.
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 (By similarity). Phosphorylation of Ser-
CC 39 modulates transport to the plasma membrane and phosphorylation of
CC Ser-232 regulates association with GRIN2A. {ECO:0000250,
CC ECO:0000269|PubMed:12933808, ECO:0000269|PubMed:15044483}.
CC -!- PTM: Ubiquitinated; by MARCHF2 which results in its degradation.
CC {ECO:0000250|UniProtKB:Q12959}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; U14950; AAA79976.1; -; mRNA.
DR PIR; I56552; I56552.
DR RefSeq; NP_036920.1; NM_012788.1.
DR PDB; 1RSO; NMR; -; A/C=4-63.
DR PDB; 1ZOK; NMR; -; A=221-313.
DR PDB; 2AWU; X-ray; 2.44 A; A/B=314-409.
DR PDB; 2AWW; X-ray; 2.21 A; A/B=314-409.
DR PDB; 2AWX; X-ray; 1.80 A; A/B=314-409.
DR PDB; 2G2L; X-ray; 2.35 A; A/B=314-409.
DR PDB; 2I0I; X-ray; 2.80 A; A/B/C=459-543.
DR PDB; 2I0L; X-ray; 2.31 A; A/B=318-401.
DR PDB; 3UAT; X-ray; 2.70 A; A=578-911.
DR PDBsum; 1RSO; -.
DR PDBsum; 1ZOK; -.
DR PDBsum; 2AWU; -.
DR PDBsum; 2AWW; -.
DR PDBsum; 2AWX; -.
DR PDBsum; 2G2L; -.
DR PDBsum; 2I0I; -.
DR PDBsum; 2I0L; -.
DR PDBsum; 3UAT; -.
DR AlphaFoldDB; Q62696; -.
DR BMRB; Q62696; -.
DR SMR; Q62696; -.
DR BioGRID; 247292; 19.
DR CORUM; Q62696; -.
DR DIP; DIP-31527N; -.
DR ELM; Q62696; -.
DR IntAct; Q62696; 35.
DR MINT; Q62696; -.
DR STRING; 10116.ENSRNOP00000055672; -.
DR iPTMnet; Q62696; -.
DR PhosphoSitePlus; Q62696; -.
DR SwissPalm; Q62696; -.
DR jPOST; Q62696; -.
DR PaxDb; Q62696; -.
DR PRIDE; Q62696; -.
DR ABCD; Q62696; 2 sequenced antibodies.
DR GeneID; 25252; -.
DR KEGG; rno:25252; -.
DR UCSC; RGD:2505; rat.
DR CTD; 1739; -.
DR RGD; 2505; Dlg1.
DR eggNOG; KOG0708; Eukaryota.
DR InParanoid; Q62696; -.
DR OrthoDB; 807583at2759; -.
DR PhylomeDB; Q62696; -.
DR BRENDA; 2.7.4.8; 5301.
DR Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR Reactome; R-RNO-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR EvolutionaryTrace; Q62696; -.
DR PRO; PR:Q62696; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009925; C:basal plasma membrane; IDA:RGD.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0030054; C:cell junction; ISO:RGD.
DR GO; GO:0031253; C:cell projection membrane; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:SynGO-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0043219; C:lateral loop; ISO:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0097025; C:MPP7-DLG1-LIN7 complex; ISO:RGD.
DR GO; GO:0035748; C:myelin sheath abaxonal region; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0033268; C:node of Ranvier; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0033270; C:paranode region of axon; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO-UCL.
DR GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; TAS:RGD.
DR GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0097060; C:synaptic membrane; ISO:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0019894; F:kinesin binding; IPI:RGD.
DR GO; GO:0097016; F:L27 domain binding; ISO:RGD.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; ISO:RGD.
DR GO; GO:0042982; P:amyloid precursor protein metabolic process; ISO:RGD.
DR GO; GO:0030953; P:astral microtubule organization; ISO:RGD.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEP:RGD.
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:RGD.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0001935; P:endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0051660; P:establishment of centrosome localization; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0001771; P:immunological synapse formation; ISO:RGD.
DR GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD.
DR GO; GO:0031579; P:membrane raft organization; ISO:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD.
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:RGD.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0030432; P:peristalsis; ISO:RGD.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IMP:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0031503; P:protein-containing complex localization; ISO:RGD.
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:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0031641; P:regulation of myelination; ISO:RGD.
DR GO; GO:1903764; P:regulation of potassium ion export across plasma membrane; ISO:RGD.
DR GO; GO:1903286; P:regulation of potassium ion import; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:RGD.
DR GO; GO:1902473; P:regulation of protein localization to synapse; ISO:RGD.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:1903760; P:regulation of voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISO:RGD.
DR GO; GO:0048608; P:reproductive structure development; ISO:RGD.
DR GO; GO:0048745; P:smooth muscle tissue development; ISO:RGD.
DR GO; GO:0042110; P:T cell activation; ISO:RGD.
DR GO; GO:0048729; P:tissue morphogenesis; ISO:RGD.
DR GO; GO:0001657; P:ureteric bud development; ISO:RGD.
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; Cell junction; Cell membrane; Cytoplasm;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Synapse; Ubl conjugation.
FT CHAIN 1..911
FT /note="Disks large homolog 1"
FT /id="PRO_0000094550"
FT DOMAIN 4..64
FT /note="L27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 224..310
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 318..404
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 465..545
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 580..650
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 721..896
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 70..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..212
FT /note="Interaction with SH3 domains"
FT /evidence="ECO:0000250"
FT REGION 224..545
FT /note="Required for interaction with MARCHF2"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT REGION 419..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000269|PubMed:15044483"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 232
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000269|PubMed:12933808"
FT MOD_RES 398
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q811D0"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q811D0"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12959"
FT MOD_RES 841
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 39
FT /note="S->A: No enrichment in postsynaptic density upon
FT CaMK2 activation."
FT /evidence="ECO:0000269|PubMed:15044483"
FT MUTAGEN 39
FT /note="S->D: Localizes at the postsynaptic density."
FT /evidence="ECO:0000269|PubMed:15044483"
FT MUTAGEN 232
FT /note="S->A: No effect on association with GRIN2B."
FT /evidence="ECO:0000269|PubMed:12933808"
FT MUTAGEN 232
FT /note="S->D: Partial loss of association with GRIN2B."
FT /evidence="ECO:0000269|PubMed:12933808"
FT HELIX 5..20
FT /evidence="ECO:0007829|PDB:1RSO"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1RSO"
FT HELIX 28..42
FT /evidence="ECO:0007829|PDB:1RSO"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:1RSO"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1RSO"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1ZOK"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:1ZOK"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:1ZOK"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:1ZOK"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:1ZOK"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:1ZOK"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1ZOK"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:1ZOK"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:1ZOK"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:2AWX"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:2AWX"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:2AWX"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:2AWX"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:2AWX"
FT HELIX 383..391
FT /evidence="ECO:0007829|PDB:2AWX"
FT STRAND 395..402
FT /evidence="ECO:0007829|PDB:2AWX"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:2AWU"
FT STRAND 464..469
FT /evidence="ECO:0007829|PDB:2I0I"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:2I0I"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:2I0I"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:2I0I"
FT HELIX 498..502
FT /evidence="ECO:0007829|PDB:2I0I"
FT HELIX 524..532
FT /evidence="ECO:0007829|PDB:2I0I"
FT STRAND 536..542
FT /evidence="ECO:0007829|PDB:2I0I"
FT STRAND 583..587
FT /evidence="ECO:0007829|PDB:3UAT"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:3UAT"
FT STRAND 611..616
FT /evidence="ECO:0007829|PDB:3UAT"
FT STRAND 619..628
FT /evidence="ECO:0007829|PDB:3UAT"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:3UAT"
FT HELIX 643..651
FT /evidence="ECO:0007829|PDB:3UAT"
FT STRAND 709..717
FT /evidence="ECO:0007829|PDB:3UAT"
FT STRAND 724..728
FT /evidence="ECO:0007829|PDB:3UAT"
FT HELIX 731..741
FT /evidence="ECO:0007829|PDB:3UAT"
FT TURN 743..745
FT /evidence="ECO:0007829|PDB:3UAT"
FT TURN 763..765
FT /evidence="ECO:0007829|PDB:3UAT"
FT HELIX 773..781
FT /evidence="ECO:0007829|PDB:3UAT"
FT STRAND 785..791
FT /evidence="ECO:0007829|PDB:3UAT"
FT STRAND 794..799
FT /evidence="ECO:0007829|PDB:3UAT"
FT HELIX 800..807
FT /evidence="ECO:0007829|PDB:3UAT"
FT TURN 808..810
FT /evidence="ECO:0007829|PDB:3UAT"
FT STRAND 812..815
FT /evidence="ECO:0007829|PDB:3UAT"
FT HELIX 820..827
FT /evidence="ECO:0007829|PDB:3UAT"
FT STRAND 833..837
FT /evidence="ECO:0007829|PDB:3UAT"
FT HELIX 842..848
FT /evidence="ECO:0007829|PDB:3UAT"
FT HELIX 854..871
FT /evidence="ECO:0007829|PDB:3UAT"
FT HELIX 872..874
FT /evidence="ECO:0007829|PDB:3UAT"
FT STRAND 876..879
FT /evidence="ECO:0007829|PDB:3UAT"
FT HELIX 884..898
FT /evidence="ECO:0007829|PDB:3UAT"
FT STRAND 900..906
FT /evidence="ECO:0007829|PDB:3UAT"
SQ SEQUENCE 911 AA; 100571 MW; 18CEBD31DD0CAF8B CRC64;
MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVISI FQSNLFQALI DIQEFYEVTL
LDNPKCVDHS KQCEPVQPGN PWESGSLSSA AVTSESLPGG LSPPVEKYRY QDEEVLPSER
ISPQVPNEVL GPELVHVSEK SLSEIENVHG FVSHSHISPI KPTEAVPPSS PIVPVTPALP
VPAESPVVLP STPQANPPPV LVNTDSLETP TYVNGTDADY EYEEITLERG NSGLGFSIAG
GTDNPHIGDD SSIFITKIIT GGAAAQDGRL RVNDCILRVN EADVRDVTHS KAVEALKEAG
SIVRLYVKRR KAFRKNHEIK LIKGPKGLGF SIAGGVGNQH IPGDNSIYVT KIIEGGAAHK
DGKLQIGDKL LAVNSVCLEE VTHEEAVTAL KNTSDFVYLK AAKPTSMYIN DGYAPPDITN
SSSQSVDNHV SPSSYLGQTP ASPARYSPIS KAVLGDDEIT REPRKVVLHR GSTGLGFNIV
GGEDGEGIFI SFILAGGPAD LSGELRKGDR IISVNSVDLR AASHEQAAAA LKNAGQAVTI
VAQYRPEEYS RFEAKIHDLR ETMMNSSVSS GSGSLRTSQK RSLYVRALFD YDKTKDSGLP
SQGLNFKFGD ILHVINASDD EWWQARQVTP DGESDEVGVI PSKRRVEKKE RARLKTVKFN
SKTRGDKGEI PDDMGSKGLK HVTSNASDSE SSYHEYGCSK GGQEEYVLSY EPVNQQEVNY
TRPVIILGPM KDRVNDDLIS EFPDKFGSCV PHTTRPKRDY EVDGRDYHFV TSREQMEKDI
QEHKFIEAGQ YNNHLYGTSV QSVRAVAEKG KHCILDVSGN AIKRLQIAQL YPISIFIKPK
SMENIMEMNK RLTDEQARKT FERAVRLEQE FTEHFTAIVQ GDTLEDIYNQ VKQIIEEQSG
PYIWVPAKEK L
