DLG3_RAT
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 03-AUG-2022, entry version 180.
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; F1MAB7: Dgki; NbExp=2; IntAct=EBI-349596, EBI-8523614;
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; 28.
DR MINT; Q62936; -.
DR STRING; 10116.ENSRNOP00000003741; -.
DR iPTMnet; Q62936; -.
DR PhosphoSitePlus; Q62936; -.
DR PaxDb; Q62936; -.
DR PRIDE; Q62936; -.
DR ABCD; Q62936; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000003741; ENSRNOP00000003741; ENSRNOG00000002767. [Q62936-1]
DR Ensembl; ENSRNOT00000045082; ENSRNOP00000047310; ENSRNOG00000002767. [Q62936-2]
DR GeneID; 58948; -.
DR KEGG; rno:58948; -.
DR UCSC; RGD:68423; rat. [Q62936-1]
DR CTD; 1741; -.
DR RGD; 68423; Dlg3.
DR eggNOG; KOG0708; Eukaryota.
DR GeneTree; ENSGT00940000159565; -.
DR InParanoid; Q62936; -.
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 tissues.
DR ExpressionAtlas; Q62936; baseline and differential.
DR Genevisible; Q62936; RN.
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:0030054; C:cell junction; IBA:GO_Central.
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: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: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:0008022; F:protein C-terminus binding; IPI: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: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; cd12029; SH3_DLG3; 1.
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; 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; 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; 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; 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; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
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
