DLGP1_RAT
ID DLGP1_RAT Reviewed; 992 AA.
AC P97836; O54773; P97841;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Disks large-associated protein 1 {ECO:0000305};
DE Short=DAP-1;
DE AltName: Full=Guanylate kinase-associated protein;
DE Short=rGKAP {ECO:0000303|PubMed:27756895};
DE AltName: Full=PSD-95/SAP90-binding protein 1;
DE AltName: Full=SAP90/PSD-95-associated protein 1;
DE Short=SAPAP1;
GN Name=Dlgap1 {ECO:0000312|RGD:620223};
GN Synonyms=Gkap {ECO:0000303|PubMed:27756895};
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] (ISOFORMS 2; 3 AND 4), AND INTERACTION WITH
RP DLG1; DLG2; DLG3 AND DLG4.
RC TISSUE=Brain;
RX PubMed=9024696; DOI=10.1083/jcb.136.3.669;
RA Kim E., Naisbitt S., Hsueh Y.-P., Rao A., Rothschild A., Craig A.M.,
RA Sheng M.;
RT "GKAP, a novel synaptic protein that interacts with the guanylate kinase-
RT like domain of the PSD-95/SAP90 family of channel clustering molecules.";
RL J. Cell Biol. 136:669-678(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 5 AND 6), AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9428732; DOI=10.1016/s0014-5793(97)01399-9;
RA Kawashima N., Takamiya K., Sun J., Kitabatake A., Sobue K.;
RT "Differential expression of isoforms of PSD-95 binding protein
RT (GKAP/SAPAP1) during rat brain development.";
RL FEBS Lett. 418:301-304(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [4]
RP INTERACTION WITH BEGAIN AND DLG4.
RX PubMed=9756850; DOI=10.1074/jbc.273.41.26269;
RA Deguchi M., Hata Y., Takeuchi M., Ide N., Hirao K., Yao I., Irie M.,
RA Toyoda A., Takai Y.;
RT "BEGAIN (brain-enriched guanylate kinase-associated protein), a novel
RT neuronal PSD-95/SAP90-binding protein.";
RL J. Biol. Chem. 273:26269-26272(1998).
RN [5]
RP INTERACTION WITH DLG4 AND SHANK PROTEINS.
RX PubMed=10527873; DOI=10.1006/bbrc.1999.1489;
RA Boeckers T.M., Winter C., Smalla K.-H., Kreutz M.R., Bockmann J.,
RA Seidenbecher C., Garner C.C., Gundelfinger E.D.;
RT "Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with
RT synaptic proteins of the SAPAP/GKAP family.";
RL Biochem. Biophys. Res. Commun. 264:247-252(1999).
RN [6]
RP INTERACTION WITH DLG4 AND SHANK1.
RC TISSUE=Brain;
RX PubMed=10488079; DOI=10.1074/jbc.274.39.27463;
RA Yao I., Hata Y., Hirao K., Deguchi M., Ide N., Takeuchi M., Takai Y.;
RT "Synamon, a novel neuronal protein interacting with synapse-associated
RT protein 90/postsynaptic density-95-associated protein.";
RL J. Biol. Chem. 274:27463-27466(1999).
RN [7]
RP INTERACTION WITH SHANK PROTEINS, AND MUTAGENESIS OF THR-990; ARG-991 AND
RP LEU-992.
RX PubMed=10433268; DOI=10.1016/s0896-6273(00)80809-0;
RA Naisbitt S., Kim E., Tu J.C., Xiao B., Sala C., Valtschanoff J.,
RA Weinberg R.J., Worley P.F., Sheng M.;
RT "Shank, a novel family of postsynaptic density proteins that binds to the
RT NMDA receptor/PSD-95/GKAP complex and cortactin.";
RL Neuron 23:569-582(1999).
RN [8]
RP INTERACTION WITH AIP1.
RX PubMed=9694864; DOI=10.1074/jbc.273.33.21105;
RA Hirao K., Hata Y., Ide N., Takeuchi M., Irie M., Yao I., Deguchi M.,
RA Toyoda A., Suedhof T.C., Takai Y.;
RT "A novel multiple PDZ domain-containing molecule interacting with N-methyl-
RT d-aspartate receptors and neuronal cell adhesion proteins.";
RL J. Biol. Chem. 273:21105-21110(1998).
RN [9]
RP INTERACTION WITH DYL2.
RX PubMed=14760703; DOI=10.1002/pmic.200300528;
RA Navarro-Lerida I., Martinez Moreno M., Roncal F., Gavilanes F., Albar J.P.,
RA Rodriguez-Crespo I.;
RT "Proteomic identification of brain proteins that interact with dynein light
RT chain LC8.";
RL Proteomics 4:339-346(2004).
RN [10]
RP INTERACTION WITH LRFN1.
RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K.,
RA Kim E.;
RT "SALM synaptic cell adhesion-like molecules regulate the differentiation of
RT excitatory synapses.";
RL Neuron 50:233-245(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-365; SER-389;
RP SER-418; SER-421; SER-425; SER-428; SER-437; SER-509; SER-605; SER-608;
RP SER-611 AND SER-947, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [12]
RP INTERACTION WITH MPP2.
RX PubMed=27756895; DOI=10.1038/srep35283;
RA Rademacher N., Schmerl B., Lardong J.A., Wahl M.C., Shoichet S.A.;
RT "MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1 cell
RT adhesion molecules to core components of the postsynaptic density.";
RL Sci. Rep. 6:35283-35283(2016).
CC -!- FUNCTION: Part of the postsynaptic scaffold in neuronal cells.
CC -!- SUBUNIT: Interacts with guanylate kinase-like domain of DLG1, DLG2,
CC DLG3, DLG4 and AIP1. Interacts with the PDZ domain of SHANK1, SHANK2
CC and SHANK3. Found in a complex with DLG4 and SHANK1, SHANK2 or SHANK3.
CC Found in a complex with DLG4 and BEGAIN. Interacts with DYL2 and LRFN1.
CC Interacts with MPP2 (via the SH3-Guanylate kinase-like sub-module)
CC (PubMed:27756895). {ECO:0000269|PubMed:10433268,
CC ECO:0000269|PubMed:10488079, ECO:0000269|PubMed:10527873,
CC ECO:0000269|PubMed:14760703, ECO:0000269|PubMed:16630835,
CC ECO:0000269|PubMed:27756895, ECO:0000269|PubMed:9024696,
CC ECO:0000269|PubMed:9694864, ECO:0000269|PubMed:9756850}.
CC -!- INTERACTION:
CC P97836; P31016: Dlg4; NbExp=9; IntAct=EBI-80901, EBI-375655;
CC P97836; O88382: Magi2; NbExp=3; IntAct=EBI-80901, EBI-696179;
CC P97836; Q9WV48: Shank1; NbExp=6; IntAct=EBI-80901, EBI-80909;
CC P97836-5; Q9WV48: Shank1; NbExp=2; IntAct=EBI-6269434, EBI-80909;
CC P97836-5; P78352: DLG4; Xeno; NbExp=3; IntAct=EBI-6269434, EBI-80389;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Postsynaptic density. Synapse.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=SAPAP1;
CC IsoId=P97836-1; Sequence=Displayed;
CC Name=2; Synonyms=GKAP C, 2A;
CC IsoId=P97836-4; Sequence=VSP_015415, VSP_015416;
CC Name=3; Synonyms=GKAP A, GKAP1a;
CC IsoId=P97836-5; Sequence=VSP_015415, VSP_015416, VSP_015420;
CC Name=4; Synonyms=GKAP B, 2C;
CC IsoId=P97836-6; Sequence=VSP_015415, VSP_015416, VSP_015419;
CC Name=5; Synonyms=2B;
CC IsoId=P97836-7; Sequence=VSP_015415, VSP_015418;
CC Name=6; Synonyms=2D;
CC IsoId=P97836-8; Sequence=VSP_015415, VSP_015417;
CC -!- TISSUE SPECIFICITY: Expressed in brain and testis.
CC -!- DEVELOPMENTAL STAGE: Highest level of isoform 1 in the brain of newborn
CC rats. Increasing levels of isoforms 2, 3, 4, and 5 in the brain of
CC newborn rats from birth to 6 weeks of postnatal development. Increasing
CC but low level of isoform 6 is expressed in the brain from 2 to 6 weeks
CC of postnatal development. {ECO:0000269|PubMed:9428732}.
CC -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
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DR EMBL; U67987; AAC53054.1; -; mRNA.
DR EMBL; AB003594; BAA24265.1; -; mRNA.
DR EMBL; U67137; AAB48587.1; -; mRNA.
DR PIR; T00025; T00025.
DR RefSeq; NP_001291216.1; NM_001304287.1. [P97836-7]
DR RefSeq; XP_008765652.1; XM_008767430.2. [P97836-4]
DR RefSeq; XP_008765654.1; XM_008767432.2. [P97836-8]
DR PDB; 4R0Y; X-ray; 2.00 A; A/B=807-916, A/B=946-971.
DR PDB; 5OVC; X-ray; 1.55 A; B=987-992.
DR PDBsum; 4R0Y; -.
DR PDBsum; 5OVC; -.
DR AlphaFoldDB; P97836; -.
DR SMR; P97836; -.
DR BioGRID; 249233; 9.
DR CORUM; P97836; -.
DR ELM; P97836; -.
DR IntAct; P97836; 16.
DR MINT; P97836; -.
DR STRING; 10116.ENSRNOP00000022351; -.
DR iPTMnet; P97836; -.
DR PhosphoSitePlus; P97836; -.
DR PaxDb; P97836; -.
DR PRIDE; P97836; -.
DR ABCD; P97836; 3 sequenced antibodies.
DR Ensembl; ENSRNOT00000087592; ENSRNOP00000072852; ENSRNOG00000016196. [P97836-7]
DR GeneID; 65040; -.
DR KEGG; rno:65040; -.
DR UCSC; RGD:620223; rat. [P97836-1]
DR CTD; 9229; -.
DR RGD; 620223; Dlgap1.
DR VEuPathDB; HostDB:ENSRNOG00000016196; -.
DR eggNOG; KOG3971; Eukaryota.
DR GeneTree; ENSGT00940000156220; -.
DR InParanoid; P97836; -.
DR PhylomeDB; P97836; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR PRO; PR:P97836; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000016196; Expressed in frontal cortex and 14 other tissues.
DR ExpressionAtlas; P97836; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:BHF-UCL.
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:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; IDA:SynGO.
DR GO; GO:0070842; P:aggresome assembly; IMP:BHF-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0099562; P:maintenance of postsynaptic density structure; IC:SynGO.
DR GO; GO:0035418; P:protein localization to synapse; IMP:BHF-UCL.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IMP:BHF-UCL.
DR InterPro; IPR030524; DLGAP1.
DR InterPro; IPR005026; SAPAP.
DR PANTHER; PTHR12353; PTHR12353; 1.
DR PANTHER; PTHR12353:SF7; PTHR12353:SF7; 1.
DR Pfam; PF03359; GKAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Membrane;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..992
FT /note="Disks large-associated protein 1"
FT /id="PRO_0000174290"
FT REGION 154..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..676
FT /note="Interaction with DYL2"
FT /evidence="ECO:0000269|PubMed:14760703"
FT REGION 687..698
FT /note="Interaction with DYL2"
FT /evidence="ECO:0000269|PubMed:14760703"
FT REGION 914..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 990..992
FT /note="PDZ-binding"
FT COMPBIAS 178..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 418
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 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 579
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 606
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9D415"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..298
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:9024696,
FT ECO:0000303|PubMed:9428732"
FT /id="VSP_015415"
FT VAR_SEQ 299..325
FT /note="QKASVNMDQAVVKSEACQQERSCQYLQ -> MIDLFKAEWVSSVCVQVSRNG
FT RTDQVW (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9024696,
FT ECO:0000303|PubMed:9428732"
FT /id="VSP_015416"
FT VAR_SEQ 299..325
FT /note="QKASVNMDQAVVKSEACQQERSCQYLQ -> MNLIFHKDILFGVSATK (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:9428732"
FT /id="VSP_015417"
FT VAR_SEQ 299..324
FT /note="QKASVNMDQAVVKSEACQQERSCQYL -> MIDLFKAEWVSSVCVQVSRNGR
FT TD (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9428732"
FT /id="VSP_015418"
FT VAR_SEQ 537..546
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9024696,
FT ECO:0000303|PubMed:9428732"
FT /id="VSP_015419"
FT VAR_SEQ 547..574
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9024696"
FT /id="VSP_015420"
FT MUTAGEN 990
FT /note="T->A: Abolishes interaction with SHANK1."
FT /evidence="ECO:0000269|PubMed:10433268"
FT MUTAGEN 991
FT /note="R->D: Abolishes interaction with SHANK1."
FT /evidence="ECO:0000269|PubMed:10433268"
FT MUTAGEN 992
FT /note="L->A: Abolishes interaction with SHANK1."
FT /evidence="ECO:0000269|PubMed:10433268"
FT CONFLICT 636
FT /note="S -> T (in Ref. 1; AAC53054 and 2; BAA24265)"
FT /evidence="ECO:0000305"
FT HELIX 808..835
FT /evidence="ECO:0007829|PDB:4R0Y"
FT HELIX 841..858
FT /evidence="ECO:0007829|PDB:4R0Y"
FT HELIX 860..871
FT /evidence="ECO:0007829|PDB:4R0Y"
FT HELIX 882..907
FT /evidence="ECO:0007829|PDB:4R0Y"
FT STRAND 988..991
FT /evidence="ECO:0007829|PDB:5OVC"
SQ SEQUENCE 992 AA; 110178 MW; 44BAF9BC0C14C099 CRC64;
MKGLSGSRSH HHGITCESAC DSLSHHSDHK PYLLSPVDHH PADHPYYTQR NSFQAECVGP
FSDPLASSTF PRRHYTSQQE LKDESALVPR TLATKANRLP TNLLDQFERQ LPLSRDGYHT
LQYKRTAVEH RSDSPGRIRH LVHSVQKLFT KSHSLEGASK GGVNGGKASP DGSQTVRYGK
RSKSKERRSE PKARSNASNA SPTSPSWWSS DDNLDGDMCL YHTPSGVMTM GRCPDRSVSQ
YFMGAYNTIS EQAVKASRSN NDVKCSTCAN LPVTLDAPLL KKSAWSSTLT VSRAREVYQK
ASVNMDQAVV KSEACQQERS CQYLQVPQDE WTGYTPRGKD DEIPCRRMRS GSYIKAMGDE
DSGDSDTSPK PSPKVAARRE SYLKATQPSL TELTTLKISN EHSPKLQIRS HSYLRAVSEV
SINRSLDSLD PAGLLTSPKF RSRNESYMRA MSTISQVSEM EVNGQFESVC ESVFSELESQ
AVEALDLPMP GCFRMRSHSY VRAIEKGCSQ DDECVSLRSS SPPRTTTTVR TIQSSTGVIK
LSSAVEVSSC ITTYKKTPPP VPPRTTTKPF ISITAQSSTE SAQDAYMDGQ GQRGDMISQS
GLSNSTESLD SMKALTAAIE AANAQIHGPA SQHMGSNAAA VTTTTTIATV TTEDRKKDFK
KNRCLSIGIQ VDDAEESEKM AESKTSSKFQ SVGVQVEEEK CFRRFTRSNS VTTAVQADLD
FHDNLENSLE SIEDNSCPGP MARQFSRDAS TSTVSIQGSG NHYHACAADD DFDTDFDPSI
LPPPDPWIDS ITEDPLEAVQ RSVCHRDGHW FLKLLQAERD RMEGWCKQME REERENNLPE
DILGKIRTAV GSAQLLMAQK FYQFRELCEE NLNPNAHPRP TSQDLAGFWD MLQLSIENIS
MKFDELHQLK ANNWKQMDPL DKKERRAPPP VPKKPAKGPA PLIRERSLES SQRQEARKRL
MAAKRAASVR QNSATESAES IEIYIPEAQT RL
