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Database: UniProt
Entry: Q62696
LinkDB: Q62696
Original site: Q62696 
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   25-APR-2018, entry version 172.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Brain;
RX   PubMed=7891172;
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-
RT   4-propionic acid receptor GluR1 subunit.";
RL   J. Biol. Chem. 273:19518-19524(1998).
RN   [4]
RP   INTERACTION WITH MAP1A.
RX   PubMed=9786987;
RA   Brenman J.E., Topinka J.R., Cooper E.C., McGee A.W., Rosen J.,
RA   Milroy T., 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.,
RA   Trimmer J.S.;
RT   "PSD-95 and SAP97 exhibit distinct mechanisms for regulating K(+)
RT   channel 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
RT   Lin-2/CASK binds and recruits SAP97 to the lateral surface of
RT   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
RT   cortical neurons.";
RL   Dev. Biol. 263:216-230(2003).
RN   [8]
RP   MUTAGENESIS OF SER-232, PHOSPHORYLATION AT SER-232, AND INTERACTION
RP   WITH 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
RP   FUNCTION.
RX   PubMed=14960569; DOI=10.1074/jbc.M400284200;
RA   Leonoudakis D., Conti L.R., Radeke C.M., McGuire L.M.,
RA   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
RP   LOCATION, AND 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
RT   SAP97 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
RT   serine/threonine 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.,
RA   Wenthold R.J.;
RT   "A novel family of adhesion-like molecules that interacts with the
RT   NMDA 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.,
RA   Kaang B.-K., Kim E.;
RT   "SALM synaptic cell adhesion-like molecules regulate the
RT   differentiation of excitatory synapses.";
RL   Neuron 50:233-245(2006).
RN   [15]
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.,
RA   Kang G.B., 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   [16]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH 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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-138; SER-618
RP   AND SER-841, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Essential multidomain scaffolding protein required for
CC       normal development (By similarity). Recruits channels, receptors
CC       and signaling molecules to discrete plasma membrane domains in
CC       polarized cells. Regulates the excitability of cardiac myocytes by
CC       modulating the functional expression of Kv4 channels. Functional
CC       regulator of Kv1.5 channel (By similarity). May play a role in
CC       adherens junction assembly, signal transduction, cell
CC       proliferation, synaptogenesis and lymphocyte activation.
CC       {ECO:0000250, 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-
CC       like domain) with DLGAP1, DLGAP2, DLGAP3, DLGAP4 and MAP1A
CC       (PubMed:9115257, PubMed:9786987). Interacts (via guanylate kinase-
CC       like domain) with KIF13B (By similarity). May interact with HTR2A
CC       (By similarity). Interacts (via PDZ domains) with GRIA1
CC       (PubMed:9677374). Interacts (via PDZ domains) with GRIN2A
CC       (PubMed:12933808). Interacts (via PDZ domains) with KCND2 and
CC       KCND3 (PubMed:19213956). Interacts (via PDZ domains) with KCNA1,
CC       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
CC       with cytoskeleton-associated protein EPB41 (By similarity).
CC       Interacts with cytoskeleton-associated protein EZR (By
CC       similarity). Found in a complex with KCNA5 and CAV3 (By
CC       similarity). Found in a complex with APC and CTNNB1 (By
CC       similarity). Interacts with CDH1 through binding to PIK3R1 (By
CC       similarity). Forms multiprotein complexes with CASK, LIN7A, LIN7B,
CC       LIN7C, APBA1, and KCNJ12 (PubMed:11865057, PubMed:14960569).
CC       Interacts with TOPK (By similarity). Forms a tripartite complex
CC       composed of DLG1, MPP7 and LIN7 (LIN7A or LIN7C) (By similarity).
CC       May interact with TJAP1 (By similarity). Interacts with PTEN
CC       (PubMed:15951562). Interacts with FRMPD4 (via C-terminus)
CC       (PubMed:19118189). Interacts with LRFN1 and LRFN2
CC       (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). {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:9115257,
CC       ECO:0000269|PubMed:9677374, ECO:0000269|PubMed:9786987,
CC       ECO:0000305}.
CC   -!- INTERACTION:
CC       Q9Y297:BTRC (xeno); NbExp=3; IntAct=EBI-389325, EBI-307461;
CC       Q810C5:Dgki; NbExp=3; IntAct=EBI-389325, EBI-8523614;
CC       O08560:Dgkz; NbExp=4; IntAct=EBI-389325, EBI-8570505;
CC       P31016:Dlg4; NbExp=2; IntAct=EBI-389325, EBI-375655;
CC       O14490:DLGAP1 (xeno); NbExp=2; IntAct=EBI-389325, EBI-1753207;
CC       P89079:E4 (xeno); NbExp=7; IntAct=EBI-389325, EBI-7401124;
CC       Q8VDU0:Gpsm2 (xeno); NbExp=7; IntAct=EBI-389325, EBI-7575403;
CC       P52188:Kcnj12; NbExp=11; IntAct=EBI-389325, EBI-704583;
CC       P35561:Kcnj2 (xeno); NbExp=2; IntAct=EBI-389325, EBI-703793;
CC       Q64273:Kcnj2; NbExp=3; IntAct=EBI-389325, EBI-703577;
CC       P48050:KCNJ4 (xeno); NbExp=2; IntAct=EBI-389325, EBI-706117;
CC       E9Q4K7:Kif13b (xeno); NbExp=2; IntAct=EBI-389325, EBI-9085496;
CC       Q460M5:Lrfn2; NbExp=2; IntAct=EBI-389325, EBI-877185;
CC       P34926:Map1a; NbExp=2; IntAct=EBI-389325, EBI-631571;
CC       P60484:PTEN (xeno); NbExp=2; IntAct=EBI-389325, EBI-696162;
CC       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}.
CC       Basolateral cell membrane {ECO:0000269|PubMed:11865057}.
CC       Endoplasmic reticulum membrane {ECO:0000269|PubMed:10629225,
CC       ECO:0000269|PubMed:15044483}. Cell junction, synapse, postsynaptic
CC       cell membrane, postsynaptic density {ECO:0000269|PubMed:15044483}.
CC       Cell junction, synapse {ECO:0000269|PubMed:10629225}. Cell
CC       membrane, sarcolemma {ECO:0000269|PubMed:19213956}. 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
CC       regions 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
CC       neurons soma, moderately found at postsynaptic densities
CC       (PubMed:15044483). {ECO:0000250|UniProtKB:Q12959,
CC       ECO:0000269|PubMed:10629225, ECO:0000269|PubMed:11865057,
CC       ECO:0000269|PubMed:15044483}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Strongly expressed in
CC       epithelial cells, in the small intestine it is only detected in
CC       the vili. Expressed in brain, heart (at protein level), muscle,
CC       lung and liver. In the brain it was detected in olfactory bulbs,
CC       cerebral cortex, 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
CC       by binding to EPB41 and ADGRA2 together with the L27 domain that
CC       binds 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
CC       several SH3 domains and also moderates the level of protein
CC       oligomerization (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated by MAPK12 (By similarity). Phosphorylation of
CC       Ser-39 modulates transport to the plasma membrane and
CC       phosphorylation of Ser-232 regulates association with GRIN2A.
CC       {ECO:0000250, ECO:0000269|PubMed:12933808,
CC       ECO:0000269|PubMed:15044483}.
CC   -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
DR   EMBL; U14950; AAA79976.1; -; mRNA.
DR   PIR; I56552; I56552.
DR   RefSeq; NP_036920.1; NM_012788.1.
DR   UniGene; Rn.89331; -.
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   ProteinModelPortal; Q62696; -.
DR   SMR; Q62696; -.
DR   BioGrid; 247292; 16.
DR   CORUM; Q62696; -.
DR   DIP; DIP-31527N; -.
DR   ELM; Q62696; -.
DR   IntAct; Q62696; 31.
DR   MINT; Q62696; -.
DR   STRING; 10116.ENSRNOP00000055672; -.
DR   iPTMnet; Q62696; -.
DR   PhosphoSitePlus; Q62696; -.
DR   SwissPalm; Q62696; -.
DR   PaxDb; Q62696; -.
DR   PRIDE; Q62696; -.
DR   GeneID; 25252; -.
DR   KEGG; rno:25252; -.
DR   UCSC; RGD:2505; rat.
DR   CTD; 1739; -.
DR   RGD; 2505; Dlg1.
DR   eggNOG; KOG0708; Eukaryota.
DR   eggNOG; COG0194; LUCA.
DR   HOGENOM; HOG000232102; -.
DR   HOVERGEN; HBG107814; -.
DR   InParanoid; Q62696; -.
DR   KO; K12076; -.
DR   PhylomeDB; Q62696; -.
DR   BRENDA; 2.7.4.8; 5301.
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:0005605; C:basal lamina; ISO:RGD.
DR   GO; GO:0009925; C:basal plasma membrane; IDA: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; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; ISO:RGD.
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; ISO:RGD.
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: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: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:0030315; C:T-tubule; IDA:RGD.
DR   GO; GO:0045296; F:cadherin binding; ISO:RGD.
DR   GO; GO:0004385; F:guanylate kinase activity; IBA:GO_Central.
DR   GO; GO:0044325; F:ion channel binding; ISO: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: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:0032947; F:protein-containing complex scaffold activity; 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:0034629; P:cellular protein-containing complex localization; ISO:RGD.
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:0045930; P:negative regulation 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:0007399; P:nervous system development; IBA:GO_Central.
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 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: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: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:0002369; P:T cell cytokine production; ISO:RGD.
DR   GO; GO:0048729; P:tissue morphogenesis; ISO:RGD.
DR   GO; GO:0001657; P:ureteric bud development; ISO:RGD.
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; PF07653; SH3_2; 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; 2.
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; Complete proteome;
KW   Cytoplasm; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Reference proteome; Repeat; SH3 domain;
KW   Synapse.
FT   CHAIN         1    911       Disks large homolog 1.
FT                                /FTId=PRO_0000094550.
FT   DOMAIN        4     64       L27. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00365}.
FT   DOMAIN      224    310       PDZ 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   DOMAIN      318    404       PDZ 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   DOMAIN      465    545       PDZ 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   DOMAIN      580    650       SH3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00192}.
FT   DOMAIN      721    896       Guanylate kinase-like.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00100}.
FT   REGION      162    212       Interaction with SH3 domains.
FT                                {ECO:0000250}.
FT   MOD_RES      39     39       Phosphoserine; by CaMK2.
FT                                {ECO:0000269|PubMed:15044483}.
FT   MOD_RES     122    122       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     138    138       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     158    158       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q12959}.
FT   MOD_RES     232    232       Phosphoserine; by CaMK2.
FT                                {ECO:0000269|PubMed:12933808}.
FT   MOD_RES     398    398       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:Q811D0}.
FT   MOD_RES     567    567       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q12959}.
FT   MOD_RES     572    572       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q12959}.
FT   MOD_RES     574    574       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q12959}.
FT   MOD_RES     578    578       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q12959}.
FT   MOD_RES     597    597       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q811D0}.
FT   MOD_RES     618    618       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     684    684       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q12959}.
FT   MOD_RES     687    687       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q12959}.
FT   MOD_RES     841    841       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MUTAGEN      39     39       S->A: No enrichment in postsynaptic
FT                                density upon CaMK2 activation.
FT                                {ECO:0000269|PubMed:15044483}.
FT   MUTAGEN      39     39       S->D: Localizes at the postsynaptic
FT                                density. {ECO:0000269|PubMed:15044483}.
FT   MUTAGEN     232    232       S->A: No effect on association with
FT                                GRIN2B. {ECO:0000269|PubMed:12933808}.
FT   MUTAGEN     232    232       S->D: Partial loss of association with
FT                                GRIN2B. {ECO:0000269|PubMed:12933808}.
FT   HELIX         5     20       {ECO:0000244|PDB:1RSO}.
FT   STRAND       23     26       {ECO:0000244|PDB:1RSO}.
FT   HELIX        28     42       {ECO:0000244|PDB:1RSO}.
FT   HELIX        44     52       {ECO:0000244|PDB:1RSO}.
FT   STRAND       55     61       {ECO:0000244|PDB:1RSO}.
FT   STRAND      225    227       {ECO:0000244|PDB:1ZOK}.
FT   STRAND      235    239       {ECO:0000244|PDB:1ZOK}.
FT   STRAND      242    246       {ECO:0000244|PDB:1ZOK}.
FT   STRAND      254    258       {ECO:0000244|PDB:1ZOK}.
FT   STRAND      260    262       {ECO:0000244|PDB:1ZOK}.
FT   HELIX       263    267       {ECO:0000244|PDB:1ZOK}.
FT   STRAND      277    279       {ECO:0000244|PDB:1ZOK}.
FT   HELIX       289    297       {ECO:0000244|PDB:1ZOK}.
FT   STRAND      301    306       {ECO:0000244|PDB:1ZOK}.
FT   STRAND      316    322       {ECO:0000244|PDB:2AWX}.
FT   STRAND      327    334       {ECO:0000244|PDB:2AWX}.
FT   STRAND      347    352       {ECO:0000244|PDB:2AWX}.
FT   HELIX       357    361       {ECO:0000244|PDB:2AWX}.
FT   STRAND      369    373       {ECO:0000244|PDB:2AWX}.
FT   HELIX       383    391       {ECO:0000244|PDB:2AWX}.
FT   STRAND      395    402       {ECO:0000244|PDB:2AWX}.
FT   STRAND      405    407       {ECO:0000244|PDB:2AWU}.
FT   STRAND      464    469       {ECO:0000244|PDB:2I0I}.
FT   STRAND      476    481       {ECO:0000244|PDB:2I0I}.
FT   STRAND      483    486       {ECO:0000244|PDB:2I0I}.
FT   STRAND      488    493       {ECO:0000244|PDB:2I0I}.
FT   HELIX       498    502       {ECO:0000244|PDB:2I0I}.
FT   HELIX       524    532       {ECO:0000244|PDB:2I0I}.
FT   STRAND      536    542       {ECO:0000244|PDB:2I0I}.
FT   STRAND      583    587       {ECO:0000244|PDB:3UAT}.
FT   TURN        593    595       {ECO:0000244|PDB:3UAT}.
FT   STRAND      611    616       {ECO:0000244|PDB:3UAT}.
FT   STRAND      619    628       {ECO:0000244|PDB:3UAT}.
FT   STRAND      638    641       {ECO:0000244|PDB:3UAT}.
FT   HELIX       643    651       {ECO:0000244|PDB:3UAT}.
FT   STRAND      709    717       {ECO:0000244|PDB:3UAT}.
FT   STRAND      724    728       {ECO:0000244|PDB:3UAT}.
FT   HELIX       731    741       {ECO:0000244|PDB:3UAT}.
FT   TURN        743    745       {ECO:0000244|PDB:3UAT}.
FT   TURN        763    765       {ECO:0000244|PDB:3UAT}.
FT   HELIX       773    781       {ECO:0000244|PDB:3UAT}.
FT   STRAND      785    791       {ECO:0000244|PDB:3UAT}.
FT   STRAND      794    799       {ECO:0000244|PDB:3UAT}.
FT   HELIX       800    807       {ECO:0000244|PDB:3UAT}.
FT   TURN        808    810       {ECO:0000244|PDB:3UAT}.
FT   STRAND      812    815       {ECO:0000244|PDB:3UAT}.
FT   HELIX       820    827       {ECO:0000244|PDB:3UAT}.
FT   STRAND      833    837       {ECO:0000244|PDB:3UAT}.
FT   HELIX       842    848       {ECO:0000244|PDB:3UAT}.
FT   HELIX       854    871       {ECO:0000244|PDB:3UAT}.
FT   HELIX       872    874       {ECO:0000244|PDB:3UAT}.
FT   STRAND      876    879       {ECO:0000244|PDB:3UAT}.
FT   HELIX       884    898       {ECO:0000244|PDB:3UAT}.
FT   STRAND      900    906       {ECO:0000244|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
//
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