ID   DLG3_MOUSE              Reviewed;         849 AA.
AC   P70175;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   02-SEP-2026, entry version 205.
DE   RecName: Full=Disks large homolog 3;
DE   AltName: Full=Synapse-associated protein 102;
DE            Short=SAP-102;
DE            Short=SAP102;
GN   Name=Dlg3; Synonyms=Dlgh3;
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].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Kohmura N., Makino S., Yagi T.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, 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   [3]
RP   INTERACTION WITH NETO1.
RX   PubMed=19243221; DOI=10.1371/journal.pbio.1000041;
RA   Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M., Clapcote S.J.,
RA   Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M., Roder J.C.,
RA   Salter M.W., McInnes R.R.;
RT   "Neto1 is a novel CUB-domain NMDA receptor-interacting protein required for
RT   synaptic plasticity and learning.";
RL   PLoS Biol. 7:E41-E41(2009).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Kidney;
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   [5]
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   [6]
RP   INTERACTION WITH FLTP.
RX   PubMed=25296022; DOI=10.7554/elife.03842;
RA   Gegg M., Boettcher A., Burtscher I., Hasenoeder S., Van Campenhout C.,
RA   Aichler M., Walch A., Grant S.G., Lickert H.;
RT   "Flattop regulates basal body docking and positioning in mono- and
RT   multiciliated cells.";
RL   Elife 3:0-0(2014).
RN   [7]
RP   INTERACTION WITH GPR85.
RX   PubMed=25780553; DOI=10.1186/s13229-015-0012-5;
RA   Fujita-Jimbo E., Tanabe Y., Yu Z., Kojima K., Mori M., Li H., Iwamoto S.,
RA   Yamagata T., Momoi M.Y., Momoi T.;
RT   "The association of GPR85 with PSD-95-neuroligin complex and autism
RT   spectrum disorder: a molecular analysis.";
RL   Mol. Autism 6:17-17(2015).
CC   -!- FUNCTION: Required for learning most likely through its role in
CC       synaptic plasticity following NMDA receptor signaling. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts through its PDZ domains with NETO1, GRIN2B, SYNGAP1
CC       and APC. Interacts through its first two PDZ domains with ERBB4.
CC       Interacts through its third PDZ domain with NLGN1, and probably with
CC       NLGN2 and NLGN3. Interacts through its guanylate kinase-like domain
CC       with DLGAP1, DLGAP2, DLGAP3 and DLGAP4 (By similarity). Interacts with
CC       FRMPD4 (via C-terminus) (By similarity). Interacts with LRFN1, LRFN2
CC       and LRFN4 (By similarity). Interacts with FLTP. Interacts with GPR85
CC       (PubMed:25780553). Interacts with DGKI (via PDZ-binding motif)
CC       (PubMed:21119615). {ECO:0000250, ECO:0000269|PubMed:21119615,
CC       ECO:0000269|PubMed:25296022, ECO:0000269|PubMed:25780553}.
CC   -!- INTERACTION:
CC       P70175; P35347: Crhr1; NbExp=3; IntAct=EBI-396969, EBI-16879653;
CC       P70175; Q62108: Dlg4; NbExp=4; IntAct=EBI-396969, EBI-300895;
CC   -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR   EMBL; D87117; BAA13249.1; -; mRNA.
DR   CCDS; CCDS30307.1; -.
DR   RefSeq; NP_001171249.1; NM_001177778.3.
DR   RefSeq; NP_058027.1; NM_016747.5.
DR   AlphaFoldDB; P70175; -.
DR   SMR; P70175; -.
DR   BioGRID; 207274; 24.
DR   CORUM; P70175; -.
DR   DIP; DIP-31585N; -.
DR   FunCoup; P70175; 1118.
DR   IntAct; P70175; 14.
DR   MINT; P70175; -.
DR   STRING; 10090.ENSMUSP00000085299; -.
DR   GlyGen; P70175; 7 sites, 4 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P70175; -.
DR   PhosphoSitePlus; P70175; -.
DR   SwissPalm; P70175; -.
DR   PaxDb; 10090-ENSMUSP00000085299; -.
DR   PeptideAtlas; P70175; -.
DR   ProteomicsDB; 279683; -.
DR   Pumba; P70175; -.
DR   ABCD; P70175; 3 sequenced antibodies.
DR   Antibodypedia; 342; 334 antibodies from 35 providers.
DR   DNASU; 53310; -.
DR   Ensembl; ENSMUST00000087984.11; ENSMUSP00000085299.5; ENSMUSG00000000881.13.
DR   GeneID; 53310; -.
DR   KEGG; mmu:53310; -.
DR   UCSC; uc009twm.3; mouse.
DR   AGR; MGI:1888986; -.
DR   CTD; 1741; -.
DR   MGI; MGI:1888986; Dlg3.
DR   VEuPathDB; HostDB:ENSMUSG00000000881; -.
DR   eggNOG; KOG0708; Eukaryota.
DR   GeneTree; ENSGT00940000159565; -.
DR   InParanoid; P70175; -.
DR   OrthoDB; 78824at2759; -.
DR   PhylomeDB; P70175; -.
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-6794361; Neurexins and neuroligins.
DR   Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
DR   BioGRID-ORCS; 53310; 2 hits in 79 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:P70175; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; P70175; protein.
DR   Bgee; ENSMUSG00000000881; Expressed in floor plate of midbrain and 239 other cell types or tissues.
DR   ExpressionAtlas; P70175; baseline and differential.
DR   GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR   GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0043198; C:dendritic shaft; ISO:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; ISO:GO_Central.
DR   GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; ISO:GO_Central.
DR   GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR   GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:GO_Central.
DR   GO; GO:0045202; C:synapse; ISO:GO_Central.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:GO_Central.
DR   GO; GO:0019900; F:kinase binding; ISO:MGI.
DR   GO; GO:0030165; F:PDZ domain binding; ISO:GO_Central.
DR   GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0019903; F:protein phosphatase binding; ISO:GO_Central.
DR   GO; GO:0098919; F:structural constituent of postsynaptic density; ISO:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:MGI.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0001736; P:establishment of planar polarity; IMP:MGI.
DR   GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:MGI.
DR   GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR   GO; GO:0035418; P:protein localization to synapse; IBA:GO_Central.
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:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO.
DR   CDD; cd00071; GMPK; 1.
DR   CDD; cd06723; PDZ1_Dlg1-2-4-like; 1.
DR   CDD; cd06724; PDZ2_Dlg1-2-4-like; 1.
DR   CDD; cd06795; PDZ3_Dlg1-2-4-like; 1.
DR   CDD; cd12029; SH3_DLG3; 1.
DR   FunFam; 3.40.50.300:FF:001402; Discs, large homolog 3 (Drosophila); 1.
DR   FunFam; 2.30.30.40:FF:000008; Disks large homolog 1 isoform 2; 1.
DR   FunFam; 2.30.42.10:FF:000001; Disks large homolog 1 isoform 2; 1.
DR   FunFam; 3.30.63.10:FF:000001; Disks large homolog 1 isoform 2; 1.
DR   FunFam; 2.30.42.10:FF:000091; disks large homolog 1 isoform X8; 1.
DR   FunFam; 2.30.30.40:FF:000027; Disks large homolog 3 isoform 1; 1.
DR   FunFam; 2.30.42.10:FF:000002; Disks large homolog 4 isoform 2; 1.
DR   Gene3D; 2.30.42.10; -; 3.
DR   Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR019583; DLG1-4_PDZ_assoc.
DR   InterPro; IPR016313; DLG1-like.
DR   InterPro; IPR019590; DLG1_PEST_dom.
DR   InterPro; IPR035763; DLG3_SH3.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
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   InterPro; IPR050614; Synaptic_Scaffolding_LAP-MAGUK.
DR   PANTHER; PTHR23119; DISCS LARGE; 1.
DR   PANTHER; PTHR23119:SF28; DISKS LARGE HOMOLOG 3; 1.
DR   Pfam; PF00625; Guanylate_kin; 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; SM01277; MAGUK_N_PEST; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 3.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT   CHAIN           1..849
FT                   /note="Disks large homolog 3"
FT                   /id="PRO_0000094558"
FT   DOMAIN          149..235
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          244..330
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          404..484
FT                   /note="PDZ 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          519..589
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          659..834
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT   REGION          32..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..53
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         705
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
SQ   SEQUENCE   849 AA;  93482 MW;  EF3EF2D7513538EE CRC64;
     MHKHQHCCKC PECYEVTRLA ALRRLEPPGY GDWQVPDPYG PSGGNGASSG YGGYSSQTLP
     SQAGATPTPR TKAKLIPTGR DVGPVPPKPV PGKSTPKLNG SGPGWWPECT CTNRDWYEQA
     SPAPLLVNPE ALEPSLSVNG SDGMFKYEEI VLERGNSGLG FSIAGGIDNP HVPDDPGIFI
     TKIIPGGAAA MDGRLGVNDC VLRVNEVDVS EVVHSRAVEA LKEAGPVVRL VVRRRQPPPE
     TIMEVNLLKG PKGLGFSIAG GIGNQHIPGD NSIYITKIIE GGAAQKDGRL QIGDRLLAVN
     NTNLQDVRHE EAVASLKNTS DMVYLKVAKP GSIHLNDMYA PPDYASTFTA LADNHISHNS
     SLGYLGAVES KVTYPAPPQV PPTRYSPIPR HMLAEEDFTR EPRKIILHKG STGLGFNIVG
     GEDGEGIFVS FILAGGPADL SGELRRGDRI LSVNGVNLRN ATHEQAAAAL KRAGQSVTIV
     AQYRPEEYSR FESKIHDLRE QMMNSSMSSG SGSLRTSEKR SLYVRALFDY DRTRDSCLPS
     QGLSFSYGDI LHVINASDDE WWQARLVTPH GESEQIGVIP SKKRVEKKER ARLKTVKFHA
     RTGMIESNRD FPGLSDDYYG AKNLKGVTSN TSDSESSSKG QEDAILSYEP VTRQEIHYAR
     PVIILGPMKD RVNDDLISEF PHKFGSCVPH TTRPRRDNEV DGQDYHFVVS REQMEKDIQD
     NKFIEAGQFN DNLYGTSIQS VRAVAERGKH CILDVSGNAI KRLQQAQLYP IAIFIKPKSI
     EALMEMNRRQ TYEQANKIFD KAMKLEQEFG EYFTAIVQGD SLEEIYNKIK QIIEDQSGHY
     IWVPSPEKL
//