DLGP3_RAT
ID DLGP3_RAT Reviewed; 977 AA.
AC P97838; Q6QQA8; Q6QQA9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 131.
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 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 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH DLG4.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=15207911; DOI=10.1016/j.molbrainres.2004.03.014;
RA Kindler S., Rehbein M., Classen B., Richter D., Boeckers T.M.;
RT "Distinct spatiotemporal expression of SAPAP transcripts in the developing
RT rat brain: a novel dendritically localized mRNA.";
RL Brain Res. Mol. Brain Res. 126:14-21(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930 AND SER-933, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 DLG1 and DLG4/PSD-95. {ECO:0000250}.
CC -!- INTERACTION:
CC P97838; Q8R4T5: Tamalin; NbExp=3; IntAct=EBI-375673, EBI-7361884;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9115257};
CC Peripheral membrane protein {ECO:0000269|PubMed:9115257}. Postsynaptic
CC density {ECO:0000269|PubMed:9115257}. Synapse
CC {ECO:0000269|PubMed:9115257}. Note=Postsynaptic density of neuronal
CC cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=SAPAP3+;
CC IsoId=P97838-1; Sequence=Displayed;
CC Name=2; Synonyms=SAPAP3-;
CC IsoId=P97838-2; Sequence=VSP_014818;
CC -!- TISSUE SPECIFICITY: Expressed in most brain regions.
CC {ECO:0000269|PubMed:15207911, ECO:0000269|PubMed:9115257}.
CC -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
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DR EMBL; U67139; AAB48589.1; -; mRNA.
DR EMBL; AY530298; AAS90634.1; -; mRNA.
DR EMBL; AY530299; AAS90635.1; -; mRNA.
DR AlphaFoldDB; P97838; -.
DR SMR; P97838; -.
DR IntAct; P97838; 7.
DR MINT; P97838; -.
DR STRING; 10116.ENSRNOP00000019214; -.
DR iPTMnet; P97838; -.
DR PhosphoSitePlus; P97838; -.
DR PaxDb; P97838; -.
DR PRIDE; P97838; -.
DR ABCD; P97838; 1 sequenced antibody.
DR RGD; 708349; Dlgap3.
DR eggNOG; KOG3971; Eukaryota.
DR InParanoid; P97838; -.
DR PhylomeDB; P97838; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR PRO; PR:P97838; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098981; C:cholinergic synapse; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
DR GO; GO:0099572; C:postsynaptic specialization; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; IPI:BHF-UCL.
DR GO; GO:0030165; F:PDZ domain binding; IPI:BHF-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0099563; P:modification of synaptic structure; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:BHF-UCL.
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 Alternative splicing; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..977
FT /note="Disks large-associated protein 3"
FT /id="PRO_0000174296"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..90
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 202..216
FT /note="Polar 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..764
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:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PFD5"
FT VAR_SEQ 858..868
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15207911"
FT /id="VSP_014818"
FT CONFLICT 77
FT /note="G -> S (in Ref. 1; AAB48589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 977 AA; 105990 MW; AD65DB11E1D4F723 CRC64;
MRGYHGDRGS HPRPARFADQ QHMDVGPAAR APYLLGSREA FSTEPRFCAP RAGLGHLSPE
GPLSLSEGPS SVGPEGGPGG VGAGGSSSTF PRMYPGQGPF DTCEDCVGHP QGKGATRLLP
TFLDQFEKQL PVQQDGFHTL PYQRGPAGPG PGPGSGAAPE ARSESPSRIR HLVHSVQKLF
AKSHSLEAPG KRDYNGPKAE GRSSSGGDSY SGPGSGGPPT 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 LQFGRPFQRQ ASEPQPGPRA
PTYSVFRTVH TQGQWAYREG YPLPYEPPAT DGSPGPPPVP APGPGSGRRD SWMERGSRSL
PDSGRTSPCP RDGEWFIKML RAEVEKLEHW CQQMEREAED YELPEEILEK IRSAVGSTQL
LLSQKVQQFF RLCQQSLDPT AFPVPTFQDL AGFWDLLQLS IEDVTLKFLE LQQLKANSWK
LLEPKEEKKV PPPIPKKPSR GRGVPVKERS LDSVDRQRQE ARKRLLAAKR AASFRHSSAT
ESADSIEIYI PEAQTRL
