DLG3_MOUSE
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 03-AUG-2022, entry version 187.
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_001177778.2.
DR RefSeq; NP_058027.1; NM_016747.4.
DR AlphaFoldDB; P70175; -.
DR SMR; P70175; -.
DR BioGRID; 207274; 19.
DR CORUM; P70175; -.
DR DIP; DIP-31585N; -.
DR IntAct; P70175; 14.
DR MINT; P70175; -.
DR STRING; 10090.ENSMUSP00000085299; -.
DR iPTMnet; P70175; -.
DR PhosphoSitePlus; P70175; -.
DR MaxQB; P70175; -.
DR PaxDb; P70175; -.
DR PeptideAtlas; P70175; -.
DR PRIDE; P70175; -.
DR ProteomicsDB; 279683; -.
DR ABCD; P70175; 4 sequenced antibodies.
DR Antibodypedia; 342; 341 antibodies from 34 providers.
DR DNASU; 53310; -.
DR Ensembl; ENSMUST00000087984; ENSMUSP00000085299; ENSMUSG00000000881.
DR GeneID; 53310; -.
DR KEGG; mmu:53310; -.
DR UCSC; uc009twm.3; mouse.
DR CTD; 1741; -.
DR MGI; MGI:1888986; Dlg3.
DR VEuPathDB; HostDB:ENSMUSG00000000881; -.
DR eggNOG; KOG0708; Eukaryota.
DR GeneTree; ENSGT00940000159565; -.
DR InParanoid; P70175; -.
DR OrthoDB; 807583at2759; -.
DR PhylomeDB; P70175; -.
DR TreeFam; TF323171; -.
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 74 CRISPR screens.
DR ChiTaRS; Mpp3; mouse.
DR PRO; PR:P70175; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P70175; protein.
DR Bgee; ENSMUSG00000000881; Expressed in floor plate of midbrain and 235 other tissues.
DR ExpressionAtlas; P70175; baseline and differential.
DR Genevisible; P70175; MM.
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:0030054; C:cell junction; IBA:GO_Central.
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:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; ISO:MGI.
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: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:0061098; P:positive regulation of protein tyrosine kinase activity; ISO:MGI.
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; 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 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 48..68
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
