DLGP2_RAT
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 03-AUG-2022, entry version 137.
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};
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DR EMBL; U67138; AAB48588.1; ALT_INIT; mRNA.
DR RefSeq; NP_446353.2; NM_053901.1.
DR AlphaFoldDB; P97837; -.
DR SMR; P97837; -.
DR BioGRID; 250564; 6.
DR IntAct; P97837; 8.
DR MINT; P97837; -.
DR STRING; 10116.ENSRNOP00000054654; -.
DR iPTMnet; P97837; -.
DR PhosphoSitePlus; P97837; -.
DR SwissPalm; P97837; -.
DR PaxDb; P97837; -.
DR PRIDE; P97837; -.
DR ABCD; P97837; 10 sequenced antibodies.
DR GeneID; 116681; -.
DR KEGG; rno:116681; -.
DR UCSC; RGD:620224; rat.
DR CTD; 9228; -.
DR RGD; 620224; Dlgap2.
DR eggNOG; KOG3971; Eukaryota.
DR InParanoid; P97837; -.
DR OrthoDB; 197925at2759; -.
DR PhylomeDB; P97837; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR PRO; PR:P97837; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0005883; C:neurofilament; NAS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; NAS:RGD.
DR GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central.
DR GO; GO:0004385; F:guanylate 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:0007270; P:neuron-neuron synaptic transmission; NAS:UniProtKB.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; ISO:RGD.
DR InterPro; IPR030525; DLGAP2.
DR InterPro; IPR005026; SAPAP.
DR PANTHER; PTHR12353; PTHR12353; 1.
DR PANTHER; PTHR12353:SF3; PTHR12353:SF3; 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..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..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
