DLGP4_MOUSE
ID DLGP4_MOUSE Reviewed; 992 AA.
AC B1AZP2; B1AZP3; B7ZNS1; Q3KQQ8; Q6PD44; Q6XBF1; Q80TN3; Q8R3U9;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Disks large-associated protein 4;
DE Short=DAP-4;
DE AltName: Full=PSD-95/SAP90-binding protein 4;
DE AltName: Full=SAP90/PSD-95-associated protein 4;
DE Short=SAPAP-4;
GN Name=Dlgap4; Synonyms=Kiaa0964, Sapap4;
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] (ISOFORM 1).
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] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, FVB/N, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
RP 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-384; SER-388;
RP SER-405; SER-415; SER-421; SER-580; SER-581; SER-609; SER-611; SER-665;
RP SER-744; THR-915 AND SER-973, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, Spleen, and Testis;
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 [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-290, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DLG1 and DLG4/PSD-95. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=B1AZP2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B1AZP2-2; Sequence=VSP_034909;
CC Name=3;
CC IsoId=B1AZP2-3; Sequence=VSP_034907, VSP_034908;
CC -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65690.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AK122408; BAC65690.2; ALT_SEQ; Transcribed_RNA.
DR EMBL; AY243849; AAO89220.2; -; mRNA.
DR EMBL; BX004793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX571766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024558; AAH24558.1; -; mRNA.
DR EMBL; BC058948; AAH58948.1; -; mRNA.
DR EMBL; BC085475; AAH85475.1; -; mRNA.
DR EMBL; BC106094; AAI06095.1; -; mRNA.
DR EMBL; BC141110; AAI41111.1; -; mRNA.
DR EMBL; BC145394; AAI45395.1; -; mRNA.
DR CCDS; CCDS16968.1; -. [B1AZP2-1]
DR CCDS; CCDS38299.1; -. [B1AZP2-3]
DR CCDS; CCDS71171.1; -. [B1AZP2-2]
DR RefSeq; NP_001035952.1; NM_001042487.1. [B1AZP2-3]
DR RefSeq; NP_001035953.1; NM_001042488.2.
DR RefSeq; NP_001264115.1; NM_001277186.1. [B1AZP2-2]
DR RefSeq; NP_001264116.1; NM_001277187.1.
DR RefSeq; NP_666240.4; NM_146128.6. [B1AZP2-1]
DR RefSeq; XP_006499403.1; XM_006499340.3. [B1AZP2-1]
DR AlphaFoldDB; B1AZP2; -.
DR SMR; B1AZP2; -.
DR BioGRID; 230780; 15.
DR IntAct; B1AZP2; 12.
DR STRING; 10090.ENSMUSP00000126980; -.
DR iPTMnet; B1AZP2; -.
DR PhosphoSitePlus; B1AZP2; -.
DR SwissPalm; B1AZP2; -.
DR EPD; B1AZP2; -.
DR jPOST; B1AZP2; -.
DR MaxQB; B1AZP2; -.
DR PaxDb; B1AZP2; -.
DR PRIDE; B1AZP2; -.
DR ProteomicsDB; 279424; -. [B1AZP2-1]
DR ProteomicsDB; 279425; -. [B1AZP2-2]
DR ProteomicsDB; 279426; -. [B1AZP2-3]
DR Antibodypedia; 26505; 123 antibodies from 26 providers.
DR Ensembl; ENSMUST00000070782; ENSMUSP00000068745; ENSMUSG00000061689. [B1AZP2-2]
DR Ensembl; ENSMUST00000099145; ENSMUSP00000096749; ENSMUSG00000061689. [B1AZP2-3]
DR Ensembl; ENSMUST00000109567; ENSMUSP00000105195; ENSMUSG00000061689. [B1AZP2-2]
DR Ensembl; ENSMUST00000169464; ENSMUSP00000126980; ENSMUSG00000061689. [B1AZP2-1]
DR GeneID; 228836; -.
DR KEGG; mmu:228836; -.
DR UCSC; uc008nnr.2; mouse. [B1AZP2-1]
DR UCSC; uc008nnv.1; mouse. [B1AZP2-3]
DR UCSC; uc012chv.2; mouse. [B1AZP2-2]
DR CTD; 22839; -.
DR MGI; MGI:2138865; Dlgap4.
DR VEuPathDB; HostDB:ENSMUSG00000061689; -.
DR eggNOG; KOG3971; Eukaryota.
DR GeneTree; ENSGT00940000155308; -.
DR HOGENOM; CLU_010880_3_0_1; -.
DR InParanoid; B1AZP2; -.
DR OMA; HAFFQVC; -.
DR OrthoDB; 285447at2759; -.
DR PhylomeDB; B1AZP2; -.
DR TreeFam; TF321382; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 228836; 6 hits in 68 CRISPR screens.
DR ChiTaRS; Dlgap4; mouse.
DR PRO; PR:B1AZP2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; B1AZP2; protein.
DR Bgee; ENSMUSG00000061689; Expressed in cortical plate and 267 other tissues.
DR ExpressionAtlas; B1AZP2; baseline and differential.
DR Genevisible; B1AZP2; MM.
DR GO; GO:0098981; C:cholinergic synapse; IDA:SynGO.
DR GO; GO:0030425; C:dendrite; 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:0099572; C:postsynaptic specialization; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; 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; IPR030527; DLGAP4.
DR InterPro; IPR005026; SAPAP.
DR PANTHER; PTHR12353; PTHR12353; 1.
DR PANTHER; PTHR12353:SF19; PTHR12353:SF19; 1.
DR Pfam; PF03359; GKAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..992
FT /note="Disks large-associated protein 4"
FT /id="PRO_0000345018"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97839"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97839"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 915
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..539
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034907"
FT VAR_SEQ 540..550
FT /note="GSLSNSRTLPS -> MALCLELLKQC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034908"
FT VAR_SEQ 671..700
FT /note="VDCIQPVPKEEPSPATKFQSIGIQVEDDWR -> ERTRRSGSHLSEDNGPKA
FT IDVMAPSSE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_034909"
FT CONFLICT 614
FT /note="S -> N (in Ref. 4; AAH24558)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="Missing (in Ref. 1; AAO89220)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="Q -> E (in Ref. 1; AAO89220)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="I -> V (in Ref. 1; AAO89220 and 4; AAH24558/
FT AAI06095)"
FT /evidence="ECO:0000305"
FT CONFLICT 774
FT /note="A -> V (in Ref. 4; AAH24558)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 992 AA; 108037 MW; A33016920922ABB9 CRC64;
MKGLGDSRPR HLSDSLDPPH EPLFAGPDRN PYLLSPTEAF AREARFPGQN TLPGDGLFPL
NNQLPPPSST FPRIHYNSHF EVPEESPFPS HAQATKINRL PANLLDQFEK QLPIHRDGFS
TLQFPRGEAK ARGESPGRIR HLVHSVQRLF FTKAPSMEGT AGKVGGNGSK KGGLEDGKGR
RAKSKERAKA GEPKRRSRSN ISGWWSSDDN LDGEGGAFRS GPASGLMTLG RQQERTQPRY
FMHAYNTISG HMLKTTKNTT TELTAPPPPP APPATCPSLG VGTDTNYVKR GSWSTLTLSH
AHEVCQKTSA TLDKSLLKSK SCHQGLAYHY LQVPGGGGEW STTLLSPRDM DSTAEGPIPC
RRMRSGSYIK AMGDEDSDES GGGSPKPSPK TAARRQSYLR ATQQSLGEQS NPRRSLDRLD
SVDMLLPSKC PSWEDDYNPI SDSLNDSSCI SQVFGQASLI PQLFGHDQQV READLSDQYE
AACESACSEA ESTTAEALDL PLPSYFRSRS HSYLRAIQAG CSQEEDSVSL QSLSPPPSTG
SLSNSRTLPS SSCLVAYKKT PPPVPPRTTS KPFISVTVQS STESAQDTYL DSQDHKSEVT
SQSGLSNSSD SLDSSTRPPS VTRGGITPGP EAPEPPPKHA ALKSEQGTLT SSESHSEAIP
KRKLSSIGIQ VDCIQPVPKE EPSPATKFQS IGIQVEDDWR SSAPSHSMSS RRDTDSDTQD
ANDSSCKSSE RSLPDCTSHP NSISIDAGPR QAPKIAQIKR NLSYGDNSDP ALEASSLPPP
DPWLETSSSS PAEPAQPGAC RRDGYWFLKL LQAETERLEG WCCQMDKETK ENNLSEEVLG
KVLSAVGSAQ LLMSQKFQQF RGLCEQNLNP DANPRPTAQD LAGFWDLLQL SIEDISMKFD
ELYHLKANSW QLVETPEKRK EEKKPPPPVP KKPAKSKAAV SRDKASDAGD KQRQEARKRL
LAAKRAASVR QNSATESADS IEIYVPEAQT RL
