ID   DLGP2_MOUSE             Reviewed;        1059 AA.
AC   Q8BJ42; Q6XBF3;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   24-JAN-2024, entry version 142.
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|MGI:MGI:2443181}; Synonyms=Dap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 80-1059 (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   STRAIN=ICR;
RX   PubMed=15024750; DOI=10.1002/cne.20060;
RA   Welch J.M., Wang D., Feng G.;
RT   "Differential mRNA expression and protein localization of the SAP90/PSD-95-
RT   associated proteins (SAPAPs) in the nervous system of the mouse.";
RL   J. Comp. Neurol. 472:24-39(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1012, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302; SER-456; SER-667;
RP   SER-670; SER-673; SER-720; THR-743; SER-745; SER-776 AND SER-811, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse
CC       {ECO:0000250}. Note=Postsynaptic density of neuronal cells.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BJ42-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BJ42-2; Sequence=VSP_014817;
CC   -!- TISSUE SPECIFICITY: Expressed in various brain areas.
CC       {ECO:0000269|PubMed:15024750}.
CC   -!- SIMILARITY: Belongs to the SAPAP family. {ECO:0000305}.
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DR   EMBL; AK032564; BAC27927.1; -; mRNA.
DR   EMBL; AY243847; AAO89218.3; -; mRNA.
DR   CCDS; CCDS52492.1; -. [Q8BJ42-1]
DR   RefSeq; NP_001139437.1; NM_001145965.1.
DR   RefSeq; NP_766498.2; NM_172910.3. [Q8BJ42-1]
DR   RefSeq; XP_017168275.1; XM_017312786.1.
DR   AlphaFoldDB; Q8BJ42; -.
DR   SMR; Q8BJ42; -.
DR   BioGRID; 232634; 16.
DR   IntAct; Q8BJ42; 6.
DR   MINT; Q8BJ42; -.
DR   STRING; 10090.ENSMUSP00000123078; -.
DR   GlyGen; Q8BJ42; 7 sites, 1 O-linked glycan (7 sites).
DR   iPTMnet; Q8BJ42; -.
DR   MetOSite; Q8BJ42; -.
DR   PhosphoSitePlus; Q8BJ42; -.
DR   SwissPalm; Q8BJ42; -.
DR   MaxQB; Q8BJ42; -.
DR   PaxDb; 10090-ENSMUSP00000123078; -.
DR   PeptideAtlas; Q8BJ42; -.
DR   ProteomicsDB; 277462; -. [Q8BJ42-1]
DR   ProteomicsDB; 277463; -. [Q8BJ42-2]
DR   ABCD; Q8BJ42; 1 sequenced antibody.
DR   Antibodypedia; 21955; 104 antibodies from 26 providers.
DR   DNASU; 244310; -.
DR   Ensembl; ENSMUST00000043279.9; ENSMUSP00000039647.9; ENSMUSG00000047495.16. [Q8BJ42-1]
DR   Ensembl; ENSMUST00000133298.8; ENSMUSP00000119613.2; ENSMUSG00000047495.16. [Q8BJ42-1]
DR   Ensembl; ENSMUST00000150247.8; ENSMUSP00000123104.2; ENSMUSG00000047495.16. [Q8BJ42-2]
DR   GeneID; 244310; -.
DR   KEGG; mmu:244310; -.
DR   UCSC; uc009kyy.2; mouse. [Q8BJ42-1]
DR   UCSC; uc009kza.2; mouse. [Q8BJ42-2]
DR   AGR; MGI:2443181; -.
DR   CTD; 9228; -.
DR   MGI; MGI:2443181; Dlgap2.
DR   VEuPathDB; HostDB:ENSMUSG00000047495; -.
DR   eggNOG; KOG3971; Eukaryota.
DR   GeneTree; ENSGT00940000157913; -.
DR   HOGENOM; CLU_010880_0_0_1; -.
DR   InParanoid; Q8BJ42; -.
DR   OrthoDB; 4153339at2759; -.
DR   PhylomeDB; Q8BJ42; -.
DR   Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR   BioGRID-ORCS; 244310; 1 hit in 77 CRISPR screens.
DR   ChiTaRS; Dlgap2; mouse.
DR   PRO; PR:Q8BJ42; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8BJ42; Protein.
DR   Bgee; ENSMUSG00000047495; Expressed in lumbar subsegment of spinal cord and 78 other cell types or tissues.
DR   ExpressionAtlas; Q8BJ42; baseline and differential.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR   GO; GO:0099572; C:postsynaptic specialization; IBA:GO_Central.
DR   GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0023052; P:signaling; IEA:InterPro.
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.
DR   Genevisible; Q8BJ42; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Membrane; Phosphoprotein;
KW   Reference proteome; Synapse.
FT   CHAIN           1..1059
FT                   /note="Disks large-associated protein 2"
FT                   /id="PRO_0000174292"
FT   REGION          31..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..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..1025
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..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        626..669
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..1025
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:21183079"
FT   MOD_RES         308
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97837"
FT   MOD_RES         390
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97837"
FT   MOD_RES         456
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         667
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         670
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         673
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         720
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         743
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         745
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         776
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         811
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         983
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97837"
FT   MOD_RES         1012
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087"
FT   VAR_SEQ         725..738
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15024750"
FT                   /id="VSP_014817"
FT   CONFLICT        472
FT                   /note="K -> R (in Ref. 1; BAC27927)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        647
FT                   /note="D -> G (in Ref. 1; BAC27927)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1059 AA;  119074 MW;  692A878032026054 CRC64;
     MGTAQVLPGI LQKHCCILPD RNTESQCTLC GEPEEEEGGD LAQPGLSFPG PAEEDIDQQY
     SWSPTQHFNE ERYSPAPRNM KGLTGSRNQP QLCAGHTCGL SPPDDCEHPH DHMHHGSDVR
     QPYLLSPAES CPMDHHRCSP RSSVHSECMM MPVMLGDHVS SSTFPRMHYS SHYDTRDDCA
     MSHTSTKVNR IPANLLDQFE KQLPLHRDGF HTLQYQRASA ATEQRNESPG RIRHLVHSVQ
     KLFTKSHSLE GSSKSNINGT KSDSRVDDHH QSHLSKHSKR SKSKERKPES KHKSGMSSWW
     SSDDNLDSDS TYRTPSVAHR HHMDHIPHCY PEALQSPFGD LSLKTSKSNN DVKCSACEGL
     ALTPDTRYMK RSSWSTLTVS QAKEAYRKSS LNLDKPLVHP EIKPSLRPCH YLQVPQDDWG
     AYPTGGKEEE IPCRRMRSGS YIKAMGDEES GESDSSPKTS PTVAIRPEPL LKPIIQRPLG
     DHQTQSYLQA ATEVPVGHSL NPSINYNSPK FRSRNQSYMR AVSTLSQASC VSQMSEAEVN
     GQFESVCESV FSEVESQAMD ALDLPGCFRT RSHSYLRAIQ AGYSQDDECI PVMTSSNMTS
     TIRSTAAVSY TNYKKTPPPV PPRTTSKPLI SVTAQSSTES TQDAYQDSRA QRMSPWPQDS
     RGGLYNSMDS LDSNKAMNLA LETAAAQRHA ADTQSSSTRS IDKAVLASKA EELLKSRCSS
     IGVQDSEFPD HQPYPRSDVE TATDSDTESR GLREYHSVGV QVEDEKRHGR FKRSNSVTAA
     VQADLELEGF PGHVSMEDKG LQFGSSFQRH SEPSTPTQYG ALRTVRTQGL FSYREDYRTQ
     VDTSTLPPPD PWLEPSLDTV ETGRMSPCRR DGSWFLKLLH TETKRMEGWC KEMEREAEEN
     DLLEDILGKI RSAVGSAQLL MSQKFQQFYW LCQQNMDPSA MPRPTSQDLA GYWDMLQLSV
     EDVSMKFDEL HQLKLNDWKI IESPERKEER KIPPPIPKKP PKGKFPITRE KSLDLPDRQR
     QEARRRLMAA KRAASFRQNS ATERADSIEI YIPEAQTRL
//