DLGP3_MOUSE
ID DLGP3_MOUSE Reviewed; 977 AA.
AC Q6PFD5; Q6PDX0; Q6XBF2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Disks large-associated protein 3;
DE Short=DAP-3;
DE AltName: Full=PSD-95/SAP90-binding protein 3;
DE AltName: Full=SAP90/PSD-95-associated protein 3;
DE Short=SAPAP3;
GN Name=Dlgap3; Synonyms=Dap3;
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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=ICR;
RX PubMed=15024750; DOI=10.1002/cne.20060;
RA Welch J.M., Wang D., Feng G.;
RT "Differential mRNA expression and protein localization of the SAP90/PSD-95-
RT associated proteins (SAPAPs) in the nervous system of the mouse.";
RL J. Comp. Neurol. 472:24-39(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-965, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404; SER-407; SER-410;
RP SER-414; SER-641 AND SER-643, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: May play a role in the molecular organization of synapses and
CC neuronal cell signaling. Could be an adapter protein linking ion
CC channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-
CC 95/SAP90 at the plasma membrane.
CC -!- SUBUNIT: Interacts with DLG4/PSD-95. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15024750};
CC Peripheral membrane protein {ECO:0000269|PubMed:15024750}. Postsynaptic
CC density {ECO:0000269|PubMed:15024750}. Synapse
CC {ECO:0000269|PubMed:15024750}. Note=Postsynaptic density of neuronal
CC cells.
CC -!- TISSUE SPECIFICITY: Highly expressed in central and peripherical
CC nervous system (at protein level). {ECO:0000269|PubMed:15024750}.
CC -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
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DR EMBL; AY243848; AAO89219.2; -; mRNA.
DR EMBL; BC057615; AAH57615.1; -; mRNA.
DR EMBL; BC058433; AAH58433.1; -; mRNA.
DR CCDS; CCDS18665.1; -.
DR RefSeq; NP_001289010.1; NM_001302081.1.
DR RefSeq; NP_941020.1; NM_198618.5.
DR RefSeq; XP_011238839.1; XM_011240537.2.
DR PDB; 5IZU; X-ray; 2.49 A; B/D=963-977.
DR PDBsum; 5IZU; -.
DR AlphaFoldDB; Q6PFD5; -.
DR SMR; Q6PFD5; -.
DR BioGRID; 232440; 12.
DR IntAct; Q6PFD5; 8.
DR MINT; Q6PFD5; -.
DR STRING; 10090.ENSMUSP00000101700; -.
DR iPTMnet; Q6PFD5; -.
DR PhosphoSitePlus; Q6PFD5; -.
DR MaxQB; Q6PFD5; -.
DR PaxDb; Q6PFD5; -.
DR PRIDE; Q6PFD5; -.
DR ProteomicsDB; 277464; -.
DR ABCD; Q6PFD5; 1 sequenced antibody.
DR Antibodypedia; 17231; 129 antibodies from 28 providers.
DR DNASU; 242667; -.
DR Ensembl; ENSMUST00000046659; ENSMUSP00000039724; ENSMUSG00000042388.
DR Ensembl; ENSMUST00000106094; ENSMUSP00000101700; ENSMUSG00000042388.
DR GeneID; 242667; -.
DR KEGG; mmu:242667; -.
DR UCSC; uc008uuo.3; mouse.
DR CTD; 58512; -.
DR MGI; MGI:3039563; Dlgap3.
DR VEuPathDB; HostDB:ENSMUSG00000042388; -.
DR eggNOG; KOG3971; Eukaryota.
DR GeneTree; ENSGT00940000159513; -.
DR HOGENOM; CLU_010880_0_0_1; -.
DR InParanoid; Q6PFD5; -.
DR OMA; EDYQLQY; -.
DR OrthoDB; 197925at2759; -.
DR PhylomeDB; Q6PFD5; -.
DR TreeFam; TF321382; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 242667; 7 hits in 71 CRISPR screens.
DR ChiTaRS; Dap3; mouse.
DR PRO; PR:Q6PFD5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6PFD5; protein.
DR Bgee; ENSMUSG00000042388; Expressed in superior frontal gyrus and 76 other tissues.
DR ExpressionAtlas; Q6PFD5; baseline and differential.
DR Genevisible; Q6PFD5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0099572; C:postsynaptic specialization; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0099563; P:modification of synaptic structure; IDA:SynGO.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; IEA:InterPro.
DR InterPro; IPR030526; DLGAP3.
DR InterPro; IPR005026; SAPAP.
DR PANTHER; PTHR12353; PTHR12353; 1.
DR PANTHER; PTHR12353:SF4; PTHR12353:SF4; 1.
DR Pfam; PF03359; GKAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Phosphoprotein; Reference proteome;
KW Synapse.
FT CHAIN 1..977
FT /note="Disks large-associated protein 3"
FT /id="PRO_0000174295"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..246
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..763
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97838"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97838"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT CONFLICT 436
FT /note="N -> S (in Ref. 1; AAO89219)"
FT /evidence="ECO:0000305"
FT STRAND 964..977
FT /evidence="ECO:0007829|PDB:5IZU"
SQ SEQUENCE 977 AA; 105873 MW; 26665D623D49E4C3 CRC64;
MRGYHGDRGS HPRPARFADQ QHMDVGPAAR APYLLGSREA FSTEPRFCAP RAGLGHLSPE
GPLSLSEGPS SVGPEGGPGG VGAGGGSSTF PRMYPGQGPF DTCEDCVGHP QGKGATRLPP
TLLDQFEKQL PVQQDGFHTL PYQRGPAGPG PGPGSGAAPE ARSESPSRIR HLVHSVQKLF
AKSHSLEAPG KRDYNGPKAD GRGSSGGDSY SGPGSGGTPT SHHHHHHHHH HHHQSRHGKR
SKSKDRKGDG RHQTKATGWW SSDDNLDSDS GFLGGRPPGE PGGPFCLDAP DGSYRDLSFK
GRSGGSEGRC LACTGMSMSL DGQSVKRSAW HTMMVSQGRD GYPGAGPGKG LLGPETKAKA
RTYHYLQVPQ DDWGGYPTGG KDGEIPCRRM RSGSYIKAMG DEESGDSDGS PKTSPKALAR
RFASRRSSSV DTARINCCVP PRIHPRSSIP GYSRSLTTGQ LSEEFNQQLE AVCGSVFGEL
ESQAVDALDL PGCFRMRSHS YLRAIQAGCS QDDDCLPLLA APASVSGRPG SSFNFRKAPP
PIPPGSQAPP RISITAQSST DSAHESFTAA EGPARRCSSA DGLDGPTMGA RTLELAPVPP
RASPKPPTLI IKTIPGREEL RSLARQRKWR PSIGVQVETI SDSDTENRSR REFHSIGVQV
EEDKRRARFK RSNSVTAGVQ ADLELEGLAG LATVATEDKA LQFGRSFQRH ASEPQPGPRA
PTYSVFRTVH TQGQWAYREG YPLPYEPPAT DGSPGPTPVP APGPGSGRRD SWMERGSRSL
PDSGRTSPCP RDGEWFIKML RAEVEKLEHW CQQMEREAED YELPEEILEK IRSAVGSTQL
LLSQKVQQFF RLCQQSLDPT AFPVPTFQDL AGFWDLLQLS IEDVTLKFLE LQQLKANSWK
LLEPKEEKKV PPPIPKKPSR GRGVPVKERS LDSVDRQRQE ARKRLLAAKR AASFRHSSAT
ESADSIEIYI PEAQTRL
