ID   DLGP2_RAT               Reviewed;        1059 AA.
AC   P97837;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 3.
DT   28-JAN-2026, entry version 144.
DE   RecName: Full=Disks large-associated protein 2 {ECO:0000250|UniProtKB:Q9P1A6};
DE            Short=DAP-2;
DE   AltName: Full=PSD-95/SAP90-binding protein 2;
DE   AltName: Full=SAP90/PSD-95-associated protein 2;
DE            Short=SAPAP2;
GN   Name=Dlgap2 {ECO:0000312|RGD:620224}; Synonyms=Dap2;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP   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   PROTEIN SEQUENCE OF 234-241 AND 710-715, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U., Lubec S.;
RL   Submitted (SEP-2007) to UniProtKB.
RN   [3]
RP   TISSUE SPECIFICITY.
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-308; SER-390;
RP   SER-670; SER-673; THR-743; SER-745 AND SER-983, AND IDENTIFICATION BY MASS
RP   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 DLG4/PSD-95. {ECO:0000269|PubMed:9115257}.
CC   -!- INTERACTION:
CC       P97837; P31016: Dlg4; NbExp=2; IntAct=EBI-81025, EBI-375655;
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   -!- TISSUE SPECIFICITY: Expressed in various brain areas.
CC       {ECO:0000269|PubMed:15207911, ECO:0000269|PubMed:9115257}.
CC   -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB48588.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U67138; AAB48588.1; ALT_INIT; mRNA.
DR   RefSeq; NP_446353.3; NM_053901.2.
DR   AlphaFoldDB; P97837; -.
DR   SMR; P97837; -.
DR   BioGRID; 250564; 6.
DR   FunCoup; P97837; 1266.
DR   IntAct; P97837; 8.
DR   MINT; P97837; -.
DR   STRING; 10116.ENSRNOP00000054654; -.
DR   iPTMnet; P97837; -.
DR   PhosphoSitePlus; P97837; -.
DR   SwissPalm; P97837; -.
DR   PaxDb; 10116-ENSRNOP00000054654; -.
DR   ABCD; P97837; 10 sequenced antibodies.
DR   GeneID; 116681; -.
DR   KEGG; rno:116681; -.
DR   UCSC; RGD:620224; rat.
DR   AGR; RGD:620224; -.
DR   CTD; 9228; -.
DR   RGD; 620224; Dlgap2.
DR   eggNOG; KOG3971; Eukaryota.
DR   InParanoid; P97837; -.
DR   PhylomeDB; P97837; -.
DR   Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR   PRO; PR:P97837; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0005883; C:neurofilament; NAS:UniProtKB.
DR   GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:RGD.
DR   GO; GO:0045211; C:postsynaptic membrane; NAS:RGD.
DR   GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central.
DR   GO; GO:0004385; F:GMP kinase activity; NAS: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:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0007270; P:neuron-neuron synaptic transmission; NAS:UniProtKB.
DR   InterPro; IPR005026; SAPAP.
DR   PANTHER; PTHR12353:SF3; DISKS LARGE-ASSOCIATED PROTEIN 2; 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   Cell membrane; Direct protein sequencing; Membrane; Phosphoprotein;
KW   Reference proteome; Synapse.
FT   CHAIN           1..1059
FT                   /note="Disks large-associated protein 2"
FT                   /id="PRO_0000174293"
FT   REGION          31..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          985..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..285
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..645
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..756
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1024
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         308
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         390
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         456
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BJ42"
FT   MOD_RES         667
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BJ42"
FT   MOD_RES         670
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         673
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         720
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BJ42"
FT   MOD_RES         743
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         745
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         776
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BJ42"
FT   MOD_RES         811
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BJ42"
FT   MOD_RES         983
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1012
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BJ42"
SQ   SEQUENCE   1059 AA;  118978 MW;  8AB2A3667AD79434 CRC64;
     MGTAQVLPGI LQKHCCILPD RNTESQCTLC GEPEEEEGGD LAQPGLSFPG PAEEDIDQQY
     SWSPTQHFSE ERYSPAPRNM KGLTGSRNQP QLCVGHTCGL SPTDECEHPH DHVRHGPDVR
     QPYLLSPAES CPMDHHRCSP RSSVHSECMM MPVMLGDHVS SSTFPRMHYS SHYDTRDDCA
     TSHASTKVNR IPANLLDQFE KQLPLHRDGF HTLQYHRASA ATEQRNESPG RIRHLVHSVQ
     KLFTKSHSLE GSSKSNINGT KSEGRMDDHH QSHLSKHSKR SKSKERKPES KHKSGMSSWW
     SSDDNLDSDS TYRTPSVAHR HHMDHIPHCY PEALQSPFGD LSLKTSKSNS DVKCSACEGL
     ALTPDTRYMK RSSWSTLTVS QAKEAYRKSS LNLDKPLVHP EIKPSLQPCH YLQVPQDDWG
     AYPTGGKEEE IPCRRMRSGS YIKAMGDEES GESDSSPKTS PTVALRPEPL LKSIIQRPLG
     DHQTQSYLQA ATEVPVGHSL DPSVNYNSPK FRSRNQSYMR AVSTLSQASC VSQMSEAEVN
     GQFESVCESV FSEVESQAMD ALDLPGCFRT RSHSYLRAIQ AGYSQDDECI PVMTPSNMTS
     TIRSTAAVSY TNYKKTPPPV PPRTTSKPLI SVTAQSSTES TQDAYQDSRA QRMSPWPQDS
     RGGLYNSMDS LDSNKAMNLA LESAAAQRHA ADTQSSSTRS IDKAVLVSKA EELLKSRCSS
     IGVQDSEFPD HQPYPRSDVE TATDSDTESR GLREYHSVGV QVEDEKRHGR FKRSNSVTAA
     VQADLELEGF PGHVSMEDKG LQFGSSFQRH SEPSTPTQYG ALRTVRTQGL FSYREDYRTQ
     VDTSTLPPPD PWLEPSLDTV ETGRMSPCRR DGSWFLKLLH TETKKMEGWC KEMEREAEEN
     DLSEEILGKI RSAVGSAQLL MSQKFQQFYW LCQQNMDPSA MPRPTSQDLA GYWDMLQLSV
     EDVSMKFDEL HQLKLNDWKI MESPERKEER KIPPPIPKKP PKGKFPITRE KSLDLPDRQR
     QEARRRLMAA KRAASFRQNS ATERADSIEI YIPEAQTRL
//