DLGP4_RAT
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 25-MAY-2022, entry version 117.
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_775168.1; NM_173145.1.
DR AlphaFoldDB; P97839; -.
DR SMR; P97839; -.
DR BioGRID; 251921; 1.
DR IntAct; P97839; 5.
DR MINT; P97839; -.
DR STRING; 10116.ENSRNOP00000034166; -.
DR CarbonylDB; P97839; -.
DR iPTMnet; P97839; -.
DR PhosphoSitePlus; P97839; -.
DR PaxDb; P97839; -.
DR PRIDE; P97839; -.
DR GeneID; 286930; -.
DR KEGG; rno:286930; -.
DR UCSC; RGD:708350; rat.
DR CTD; 22839; -.
DR RGD; 708350; Dlgap4.
DR eggNOG; KOG3971; Eukaryota.
DR InParanoid; P97839; -.
DR OrthoDB; 285447at2759; -.
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: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: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: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 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..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 395..412
FT /note="Polar 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: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
