DLGP2_MOUSE
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 03-AUG-2022, entry version 134.
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; 13.
DR IntAct; Q8BJ42; 6.
DR MINT; Q8BJ42; -.
DR STRING; 10090.ENSMUSP00000123078; -.
DR iPTMnet; Q8BJ42; -.
DR PhosphoSitePlus; Q8BJ42; -.
DR SwissPalm; Q8BJ42; -.
DR MaxQB; Q8BJ42; -.
DR PaxDb; Q8BJ42; -.
DR PeptideAtlas; Q8BJ42; -.
DR PRIDE; Q8BJ42; -.
DR ProteomicsDB; 277462; -. [Q8BJ42-1]
DR ProteomicsDB; 277463; -. [Q8BJ42-2]
DR ABCD; Q8BJ42; 1 sequenced antibody.
DR Antibodypedia; 21955; 89 antibodies from 26 providers.
DR DNASU; 244310; -.
DR Ensembl; ENSMUST00000043279; ENSMUSP00000039647; ENSMUSG00000047495. [Q8BJ42-1]
DR Ensembl; ENSMUST00000133298; ENSMUSP00000119613; ENSMUSG00000047495. [Q8BJ42-1]
DR Ensembl; ENSMUST00000150247; ENSMUSP00000123104; ENSMUSG00000047495. [Q8BJ42-2]
DR GeneID; 244310; -.
DR KEGG; mmu:244310; -.
DR UCSC; uc009kyy.2; mouse. [Q8BJ42-1]
DR UCSC; uc009kza.2; mouse. [Q8BJ42-2]
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; 197925at2759; -.
DR PhylomeDB; Q8BJ42; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 244310; 1 hit in 72 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 77 other tissues.
DR ExpressionAtlas; Q8BJ42; baseline and differential.
DR Genevisible; Q8BJ42; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
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:0007270; P:neuron-neuron synaptic transmission; IEA:InterPro.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IDA:SynGO.
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 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
