ID   DLG3_RAT                Reviewed;         849 AA.
AC   Q62936; P70547;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 187.
DE   RecName: Full=Disks large homolog 3;
DE   AltName: Full=PSD-95/SAP90-related protein 1;
DE   AltName: Full=Synapse-associated protein 102;
DE            Short=SAP-102;
DE            Short=SAP102;
GN   Name=Dlg3; Synonyms=Dlgh3;
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] (ISOFORM LONG), AND INTERACTION WITH GRIN2B.
RC   TISSUE=Brain;
RX   PubMed=8780649; DOI=10.1016/s0896-6273(00)80157-9;
RA   Mueller B.M., Kistner U., Kindler S., Chung W.J., Kuhlendahl S.,
RA   Fenster S.D., Lau L.-F., Veh R.W., Huganir R.L., Gundelfinger E.D.,
RA   Garner C.C.;
RT   "SAP102, a novel postsynaptic protein that interacts with NMDA receptor
RT   complexes in vivo.";
RL   Neuron 17:255-265(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT), AND INTERACTION WITH
RP   DLGAP1; DLGAP2; DLGAP3 AND DLGAP4.
RC   TISSUE=Brain;
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 SYNGAP1.
RX   PubMed=9581761; DOI=10.1016/s0896-6273(00)81008-9;
RA   Kim J.H., Liao D., Lau L.-F., Huganir R.L.;
RT   "SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein
RT   family.";
RL   Neuron 20:683-691(1998).
RN   [4]
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   [5]
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   [6]
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).
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 and APC.
CC       Interacts through its first two PDZ domains with ERBB4. Interacts
CC       through its third PDZ domain with NLGN1, and probably with NLGN2 and
CC       NLGN3 (By similarity). Interacts through its PDZ domains with GRIN2B
CC       and SYNGAP1. Interacts through its guanylate kinase-like domain with
CC       DLGAP1, DLGAP2, DLGAP3 and DLGAP4. Interacts with FRMPD4 (via C-
CC       terminus). Interacts with LRFN2. Interacts with LRFN1 and LRFN4.
CC       Interacts with FLTP (By similarity). Interacts with DGKI (via PDZ-
CC       binding motif) (PubMed:21119615). {ECO:0000250|UniProtKB:P70175,
CC       ECO:0000250|UniProtKB:Q92796, ECO:0000269|PubMed:21119615}.
CC   -!- INTERACTION:
CC       Q62936; O08560: Dgkz; NbExp=4; IntAct=EBI-349596, EBI-8570505;
CC       Q62936; Q00960: Grin2b; NbExp=6; IntAct=EBI-349596, EBI-396905;
CC       Q62936; Q460M5: Lrfn2; NbExp=2; IntAct=EBI-349596, EBI-877185;
CC       Q62936; P23634-6: ATP2B4; Xeno; NbExp=2; IntAct=EBI-349596, EBI-1174437;
CC       Q62936; Q9P021: CRIPT; Xeno; NbExp=5; IntAct=EBI-349596, EBI-946968;
CC       Q62936; Q05586-2: GRIN1; Xeno; NbExp=3; IntAct=EBI-349596, EBI-8286218;
CC       Q62936; Q12879: GRIN2A; Xeno; NbExp=5; IntAct=EBI-349596, EBI-7249937;
CC       Q62936; Q13224: GRIN2B; Xeno; NbExp=4; IntAct=EBI-349596, EBI-2256942;
CC       Q62936; Q14957: GRIN2C; Xeno; NbExp=6; IntAct=EBI-349596, EBI-8285963;
CC       Q62936; O15399: GRIN2D; Xeno; NbExp=2; IntAct=EBI-349596, EBI-1754030;
CC       Q62936; Q09470: KCNA1; Xeno; NbExp=2; IntAct=EBI-349596, EBI-8286599;
CC       Q62936; P22459: KCNA4; Xeno; NbExp=4; IntAct=EBI-349596, EBI-631235;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q62936-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q62936-2; Sequence=VSP_003151;
CC   -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR   EMBL; U50147; AAA93031.1; -; mRNA.
DR   EMBL; U53367; AAB48561.1; -; Genomic_DNA.
DR   RefSeq; NP_113827.1; NM_031639.1. [Q62936-1]
DR   RefSeq; XP_006257144.1; XM_006257082.3. [Q62936-2]
DR   PDB; 3JXT; X-ray; 1.50 A; A/B=393-493.
DR   PDBsum; 3JXT; -.
DR   AlphaFoldDB; Q62936; -.
DR   SMR; Q62936; -.
DR   BioGRID; 248683; 10.
DR   CORUM; Q62936; -.
DR   ELM; Q62936; -.
DR   IntAct; Q62936; 29.
DR   MINT; Q62936; -.
DR   STRING; 10116.ENSRNOP00000003741; -.
DR   iPTMnet; Q62936; -.
DR   PhosphoSitePlus; Q62936; -.
DR   PaxDb; 10116-ENSRNOP00000003741; -.
DR   ABCD; Q62936; 2 sequenced antibodies.
DR   Ensembl; ENSRNOT00000003741.7; ENSRNOP00000003741.2; ENSRNOG00000002767.9. [Q62936-1]
DR   Ensembl; ENSRNOT00000045082.7; ENSRNOP00000047310.3; ENSRNOG00000002767.9. [Q62936-2]
DR   Ensembl; ENSRNOT00055051598; ENSRNOP00055042541; ENSRNOG00055029646. [Q62936-1]
DR   Ensembl; ENSRNOT00060036469; ENSRNOP00060030011; ENSRNOG00060020593. [Q62936-1]
DR   Ensembl; ENSRNOT00065028480; ENSRNOP00065022535; ENSRNOG00065016962. [Q62936-1]
DR   GeneID; 58948; -.
DR   KEGG; rno:58948; -.
DR   UCSC; RGD:68423; rat. [Q62936-1]
DR   AGR; RGD:68423; -.
DR   CTD; 1741; -.
DR   RGD; 68423; Dlg3.
DR   eggNOG; KOG0708; Eukaryota.
DR   GeneTree; ENSGT00940000159565; -.
DR   InParanoid; Q62936; -.
DR   OrthoDB; 2879721at2759; -.
DR   PhylomeDB; Q62936; -.
DR   TreeFam; TF323171; -.
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-6794361; Neurexins and neuroligins.
DR   Reactome; R-RNO-8849932; Synaptic adhesion-like molecules.
DR   EvolutionaryTrace; Q62936; -.
DR   PRO; PR:Q62936; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000002767; Expressed in frontal cortex and 20 other cell types or tissues.
DR   ExpressionAtlas; Q62936; baseline and differential.
DR   GO; GO:0032281; C:AMPA glutamate receptor complex; ISO:RGD.
DR   GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR   GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR   GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0030426; C:growth cone; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
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:0045202; C:synapse; IDA:UniProtKB.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR   GO; GO:0019900; F: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:0019904; F:protein domain specific binding; IDA:RGD.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR   GO; GO:0098919; F:structural constituent of postsynaptic density; IDA:SynGO.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; ISO:RGD.
DR   GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:ARUK-UCL.
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; ISO:RGD.
DR   CDD; cd00071; GMPK; 1.
DR   CDD; cd00992; PDZ_signaling; 3.
DR   CDD; cd12029; SH3_DLG3; 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   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.
DR   Genevisible; Q62936; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Phosphoprotein; Reference proteome;
KW   Repeat; SH3 domain.
FT   CHAIN           1..849
FT                   /note="Disks large homolog 3"
FT                   /id="PRO_0000094559"
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        48..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70175"
FT   MOD_RES         705
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P70175"
FT   VAR_SEQ         627..640
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003151"
FT   STRAND          403..408
FT                   /evidence="ECO:0007829|PDB:3JXT"
FT   STRAND          413..420
FT                   /evidence="ECO:0007829|PDB:3JXT"
FT   STRAND          422..425
FT                   /evidence="ECO:0007829|PDB:3JXT"
FT   STRAND          427..432
FT                   /evidence="ECO:0007829|PDB:3JXT"
FT   HELIX           437..441
FT                   /evidence="ECO:0007829|PDB:3JXT"
FT   STRAND          448..453
FT                   /evidence="ECO:0007829|PDB:3JXT"
FT   HELIX           463..472
FT                   /evidence="ECO:0007829|PDB:3JXT"
FT   STRAND          476..483
FT                   /evidence="ECO:0007829|PDB:3JXT"
FT   HELIX           485..488
FT                   /evidence="ECO:0007829|PDB:3JXT"
FT   TURN            489..491
FT                   /evidence="ECO:0007829|PDB:3JXT"
SQ   SEQUENCE   849 AA;  93539 MW;  34DA9C46C7BB96DB CRC64;
     MHKHQHCCKC PECYEVTRLA ALRRLEPPGY GDWQVPDPYG PSGGNGASSG YGGYSSQTLP
     SQAGATPTPR TKAKLIPTGR DVGPVPPKPV PGKNTPKLNG SGPSWWPECT CTNRDWYEQA
     SPAPLLVNPE ALEPSLSVNG SDGMFKYEEI VLERGNSGLG FSIAGGIDNP HVPDDPGIFI
     TKIIPGGAAA MDGRLGVNDC VLRVNEVDVS EVVHSRAVEA LKEAGPVVRL VVRRRQPPPE
     TIMEVNLLKG PKGLGFSIAG GIGNQHIPGD NSIYITKIIE GGAAQKDGRL QIGDRLLAVN
     NTNLQDVRHE EAVASLKNTS DMVYLKVAKP GSLHLNDMYA 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
//