ID   DLGP4_RAT               Reviewed;         992 AA.
AC   P97839;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   28-JAN-2026, entry version 126.
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=Dap4, Sapap4;
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].
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-207; SER-377;
RP   SER-380; SER-405; SER-415; SER-421; THR-915 AND SER-973, AND IDENTIFICATION
RP   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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain.
CC   -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
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DR   EMBL; U67140; AAB48590.1; -; mRNA.
DR   RefSeq; NP_775168.2; NM_173145.3.
DR   AlphaFoldDB; P97839; -.
DR   SMR; P97839; -.
DR   BioGRID; 251921; 1.
DR   FunCoup; P97839; 1679.
DR   IntAct; P97839; 5.
DR   MINT; P97839; -.
DR   STRING; 10116.ENSRNOP00000034166; -.
DR   CarbonylDB; P97839; -.
DR   GlyGen; P97839; 1 site.
DR   iPTMnet; P97839; -.
DR   PhosphoSitePlus; P97839; -.
DR   PaxDb; 10116-ENSRNOP00000034166; -.
DR   GeneID; 286930; -.
DR   KEGG; rno:286930; -.
DR   UCSC; RGD:708350; rat.
DR   AGR; RGD:708350; -.
DR   CTD; 22839; -.
DR   RGD; 708350; Dlgap4.
DR   eggNOG; KOG3971; Eukaryota.
DR   InParanoid; P97839; -.
DR   PhylomeDB; P97839; -.
DR   Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR   PRO; PR:P97839; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0098981; C:cholinergic synapse; ISO:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0099572; C:postsynaptic specialization; ISO:RGD.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR   GO; GO:0099010; P:modification of postsynaptic structure; ISO:RGD.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0090128; P:regulation of synapse maturation; ISO:RGD.
DR   GO; GO:0023052; P:signaling; IEA:InterPro.
DR   InterPro; IPR005026; SAPAP.
DR   PANTHER; PTHR12353:SF19; DISKS LARGE-ASSOCIATED PROTEIN 4; 1.
DR   PANTHER; PTHR12353; DISKS LARGE-ASSOCIATED PROTEIN DAP SAP90/PSD-95-ASSOCIATED PROTEIN; 1.
DR   Pfam; PF03359; GKAP; 1.
PE   1: Evidence at protein level;
KW   Membrane; Methylation; Phosphoprotein; Reference proteome.
FT   CHAIN           1..992
FT                   /note="Disks large-associated protein 4"
FT                   /id="PRO_0000174298"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          677..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..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..171
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..194
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..554
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..591
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..620
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        915..925
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..958
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..978
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         206
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         207
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         290
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT   MOD_RES         377
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         380
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT   MOD_RES         388
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT   MOD_RES         405
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         415
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         421
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         580
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT   MOD_RES         581
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT   MOD_RES         609
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT   MOD_RES         611
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:B1AZP2"
FT   MOD_RES         665
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2H0"
FT   MOD_RES         744
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2H0"
FT   MOD_RES         915
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         973
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   992 AA;  108035 MW;  8875B67C3FD71F04 CRC64;
     MKGLGDSRPR HLSDSLDPPH EPLFAGPDRN PYLLSPTEAF AREARFPGQN TLPGDGLFPL
     NNQLPPPSST FPRIHYNSHF EVPEESPFPS HAQATKINRL PANLLDQFEK QLPIHRDGFS
     TLQFPRGEAK ARGESPGRIR HLVHSVQRLF FTKAPSMEGT TGKVGGNGGK KGVLEDGKGR
     RAKSKERAKA GEPKRRSRSN ISGWWSSDDN LDGEGGAFRS GPASGLMTLG RQPERTQPRY
     FMHAYNTISG HMLKTTKNTT TELTAPPPPP APPATCPSLG VGTDTNYVKR GSWSTLTLSH
     AHEVCQKTSA TLDKSLLKSK SCHQGLAYHY LQVPGGGGEW STTLLSPRDM DSTAEGPIPC
     RRMRSGSYIK AMGDEDSDES GGGSPKPSPK TAARRQSYLR ATQQSLGEQS NPRRSLDRLD
     SVDMPLPSKY PSWEEDYNPI SDSLNDSGCI SQVFGQASLI PQLFGHDQQV READLSDQYE
     AACESACSEA ESTAAEALDL SLPSYFRSRS HSYLRAIQAG CSQEEDSVSL QSLSPPPSTG
     SLSNSRTLPS SSCLVAYKKT PPPVPPRTTS KPFISVTVQS STESAQDTYL DSQDHKSEVT
     SQSGLSNSSD SLDSSTRPPS VTRGGITPGP EAPEPPPKHA ALKSEHGTLT SSESHSEAVP
     KRKLSSIGIQ VDCIQPVPKE EPSPATKFQS IGVQVEDDWR SSAPSHSMSS RRDTDSDTQD
     ANDSSCKSSE RSLPDCTSHP NSISIDAGPR QAPKIAQIKR NLSYGDNSDP ALEASSLPPP
     DPWMETSSSS PAEPAQPGAC RRDGYWFLKL LQAETERLEG WCCQMDKETK ENNLSEEVLG
     KVLSAVGSAQ LLMSQKFQQF RGICEQNLNP DANPRPTAQD LAGFWDLLQL SIEDISMKFD
     ELYHLKANSW QLVETPEKRK EEKKPPPPVP KKPAKSKAAV SRDKASDAGD KQRQEARKRL
     LAAKRAASVR QNSATESADS IEIYVPEAQT RL
//