ID DLG2_MOUSE Reviewed; 852 AA. AC Q91XM9; F8VQM7; Q8BXK7; Q8BYG5; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 27-MAR-2024, entry version 181. DE RecName: Full=Disks large homolog 2; DE AltName: Full=Channel-associated protein of synapse-110; DE Short=Chapsyn-110; DE AltName: Full=Postsynaptic density protein PSD-93; GN Name=Dlg2; Synonyms=Dlgh2; 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 [MRNA] (ISOFORM 1). RC STRAIN=BALB/cJ; TISSUE=Cerebellum; RA Yamashita T., Mochizuki C., Miyagi Y., Sonoda T., Kawamoto S.; RT "Cloning and sequencing of mouse PSD-93 cDNA."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 465-852 (ISOFORM 8). RC STRAIN=C57BL/6J; TISSUE=Adrenal gland, and Spinal cord; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP INTERACTION WITH KCNJ4. RX PubMed=11997254; DOI=10.1152/ajpcell.00615.2001; RA Inanobe A., Fujita A., Ito M., Tomoike H., Inageda K., Kurachi Y.; RT "Inward rectifier K+ channel Kir2.3 is localized at the postsynaptic RT membrane of excitatory synapses."; RL Am. J. Physiol. 282:C1396-C1403(2002). RN [5] RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=12890763; DOI=10.1523/jneurosci.23-17-06703.2003; RA Tao Y.-X., Rumbaugh G., Wang G.-D., Petralia R.S., Zhao C., Kauer F.W., RA Tao F., Zhuo M., Wenthold R.J., Raja S.N., Huganir R.L., Bredt D.S., RA Johns R.A.; RT "Impaired NMDA receptor-mediated postsynaptic function and blunted NMDA RT receptor-dependent persistent pain in mice lacking postsynaptic density-93 RT protein."; RL J. Neurosci. 23:6703-6712(2003). RN [6] RP TISSUE SPECIFICITY. RX PubMed=15304517; DOI=10.1074/jbc.m407575200; RA Leyland M.L., Dart C.; RT "An alternatively spliced isoform of PSD-93/chapsyn 110 binds to the RT inwardly rectifying potassium channel, Kir2.1."; RL J. Biol. Chem. 279:43427-43436(2004). RN [7] RP ALTERNATIVE SPLICING. RX PubMed=14724236; DOI=10.1523/jneurosci.3865-03.2004; RA Parker M.J., Zhao S., Bredt D.S., Sanes J.R., Feng G.; RT "PSD93 regulates synaptic stability at neuronal cholinergic synapses."; RL J. Neurosci. 24:378-388(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-414, AND RP IDENTIFICATION BY 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-58; SER-65; TYR-505; TYR-732 RP AND TYR-737, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [10] RP INTERACTION WITH NETO1. RX PubMed=19243221; DOI=10.1371/journal.pbio.1000041; RA Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M., Clapcote S.J., RA Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M., Roder J.C., RA Salter M.W., McInnes R.R.; RT "Neto1 is a novel CUB-domain NMDA receptor-interacting protein required for RT synaptic plasticity and learning."; RL PLoS Biol. 7:E41-E41(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-58; SER-65; SER-307; SER-328; RP SER-365 AND SER-553, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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). RN [12] RP INTERACTION WITH ADAM22. RX PubMed=20089912; DOI=10.1523/jneurosci.4661-09.2010; RA Ogawa Y., Oses-Prieto J., Kim M.Y., Horresh I., Peles E., Burlingame A.L., RA Trimmer J.S., Meijer D., Rasband M.N.; RT "ADAM22, a Kv1 channel-interacting protein, recruits membrane-associated RT guanylate kinases to juxtaparanodes of myelinated axons."; RL J. Neurosci. 30:1038-1048(2010). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 95-188. RX PubMed=20054121; DOI=10.1107/s1744309109043267; RA Fiorentini M., Nielsen A.K., Kristensen O., Kastrup J.S., Gajhede M.; RT "Structure of the first PDZ domain of human PSD-93."; RL Acta Crystallogr. F 65:1254-1257(2009). CC -!- FUNCTION: Required for perception of chronic pain through NMDA receptor CC signaling. Regulates surface expression of NMDA receptors in dorsal CC horn neurons of the spinal cord. Interacts with the cytoplasmic tail of CC NMDA receptor subunits as well as inward rectifying potassium channels. CC Involved in regulation of synaptic stability at cholinergic synapses. CC Part of the postsynaptic protein scaffold of excitatory synapses. CC {ECO:0000269|PubMed:12890763}. CC -!- SUBUNIT: Interacts with NOS1/nNOS through second PDZ domain. Interacts CC with KCNJ2/Kir2.1 (via C-terminus) through one of its PDZ domains (By CC similarity). Interacts with KCNJ4 (PubMed:11997254). Interacts with CC FRMPD4 (via C-terminus) (By similarity). Interacts through its PDZ CC domains with NETO1 (PubMed:19243221). Interacts with LRFN1, LRFN2 and CC LRFN4. Interacts with FASLG (By similarity). Interacts with KCNJ4 (By CC similarity). Interacts with ADAM22 (PubMed:20089912). Interacts with CC DGKI (via PDZ-binding motif) (By similarity). CC {ECO:0000250|UniProtKB:Q15700, ECO:0000250|UniProtKB:Q63622, CC ECO:0000269|PubMed:11997254, ECO:0000269|PubMed:19243221, CC ECO:0000269|PubMed:20089912}. CC -!- INTERACTION: CC Q91XM9; Q62108: Dlg4; NbExp=6; IntAct=EBI-400138, EBI-300895; CC Q91XM9; Q4ACU6: Shank3; NbExp=4; IntAct=EBI-400138, EBI-771450; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11997254}; CC Lipid-anchor {ECO:0000250|UniProtKB:Q63622}. Postsynaptic density CC {ECO:0000250|UniProtKB:Q63622}. Synapse {ECO:0000250}. Membrane CC {ECO:0000250|UniProtKB:Q63622}. Cell projection, axon CC {ECO:0000250|UniProtKB:Q63622}. Perikaryon CC {ECO:0000250|UniProtKB:Q63622}. Note=Concentrated in soma and CC postsynaptic density of a subset of neurons. CC {ECO:0000250|UniProtKB:Q63622}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Name=1; Synonyms=PSD93-alpha; CC IsoId=Q91XM9-1; Sequence=Displayed; CC Name=2; Synonyms=PSD93-beta; CC IsoId=Q91XM9-2; Sequence=VSP_015520; CC Name=3; Synonyms=PSD93-gamma; CC IsoId=Q91XM9-3; Sequence=VSP_015517, VSP_015522; CC Name=4; Synonyms=PSD93-delta; CC IsoId=Q91XM9-4; Sequence=VSP_012869; CC Name=5; CC IsoId=Q91XM9-5; Sequence=VSP_012869, VSP_012870, VSP_012871; CC Name=6; Synonyms=PSD93 epsilon; CC IsoId=Q91XM9-6; Sequence=VSP_015518, VSP_015521; CC Name=7; Synonyms=PSD93 zeta; CC IsoId=Q91XM9-7; Sequence=VSP_015519, VSP_015523; CC Name=8; CC IsoId=Q91XM9-8; Sequence=VSP_015524; CC -!- TISSUE SPECIFICITY: Brain. Highest levels of isoform 1 in cortex, CC olfactory bulb, thalamus, hypothalamus, striatum and hippocampus. CC Highest level of isoform 2 in olfactory bulb. Reduced levels in cortex CC and hippocampus. Highest level of isoform 4 in spinal cord. Low levels CC of isoform 4, isoform 6, and isoform 7 in superior cervical ganglion. CC {ECO:0000269|PubMed:12890763, ECO:0000269|PubMed:15304517}. CC -!- DOMAIN: Isoform 7 has an L27 domain close to N-terminus. CC -!- PTM: Palmitoylation of isoform 1 and isoform 2 is not required for CC targeting to postsynaptic density. {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Mice do not respond to persistent pain. CC Postsynaptic surface expression of NMDA receptors and NMDA receptor- CC mediated synaptic function are reduced in dorsal horn neurons of the CC spinal chord. {ECO:0000269|PubMed:12890763}. CC -!- MISCELLANEOUS: [Isoform 8]: Incomplete sequence. {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; AF388675; AAK64496.1; -; mRNA. DR EMBL; AK046525; BAC32772.1; -; mRNA. DR EMBL; AK039754; BAC30440.1; -; mRNA. DR EMBL; AC100322; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC101784; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC108818; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC108832; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC109506; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC112262; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC118621; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC119218; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC121261; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC122002; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC127299; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC127683; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC140196; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC141890; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC161490; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC162304; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS40021.1; -. [Q91XM9-1] DR RefSeq; NP_001229976.1; NM_001243047.1. DR RefSeq; NP_035937.2; NM_011807.3. [Q91XM9-1] DR PDB; 2WL7; X-ray; 2.03 A; A=95-188. DR PDBsum; 2WL7; -. DR AlphaFoldDB; Q91XM9; -. DR SMR; Q91XM9; -. DR BioGRID; 204763; 26. DR DIP; DIP-31569N; -. DR IntAct; Q91XM9; 22. DR MINT; Q91XM9; -. DR STRING; 10090.ENSMUSP00000102814; -. DR GlyGen; Q91XM9; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q91XM9; -. DR PhosphoSitePlus; Q91XM9; -. DR SwissPalm; Q91XM9; -. DR jPOST; Q91XM9; -. DR MaxQB; Q91XM9; -. DR PaxDb; 10090-ENSMUSP00000102814; -. DR PeptideAtlas; Q91XM9; -. DR ProteomicsDB; 279675; -. [Q91XM9-1] DR ProteomicsDB; 279676; -. [Q91XM9-2] DR ProteomicsDB; 279677; -. [Q91XM9-3] DR ProteomicsDB; 279678; -. [Q91XM9-4] DR ProteomicsDB; 279679; -. [Q91XM9-5] DR ProteomicsDB; 279680; -. [Q91XM9-6] DR ProteomicsDB; 279681; -. [Q91XM9-7] DR ProteomicsDB; 279682; -. [Q91XM9-8] DR ABCD; Q91XM9; 11 sequenced antibodies. DR Antibodypedia; 8247; 429 antibodies from 35 providers. DR DNASU; 23859; -. DR Ensembl; ENSMUST00000107196.10; ENSMUSP00000102814.3; ENSMUSG00000052572.20. [Q91XM9-1] DR Ensembl; ENSMUST00000238619.2; ENSMUSP00000158731.2; ENSMUSG00000052572.20. [Q91XM9-4] DR GeneID; 23859; -. DR KEGG; mmu:23859; -. DR UCSC; uc009ihr.2; mouse. [Q91XM9-1] DR UCSC; uc009ihs.1; mouse. [Q91XM9-5] DR AGR; MGI:1344351; -. DR CTD; 1740; -. DR MGI; MGI:1344351; Dlg2. DR VEuPathDB; HostDB:ENSMUSG00000052572; -. DR eggNOG; KOG0708; Eukaryota. DR GeneTree; ENSGT00940000155156; -. DR HOGENOM; CLU_001715_4_2_1; -. DR InParanoid; Q91XM9; -. DR OrthoDB; 2879721at2759; -. DR TreeFam; TF323171; -. DR Reactome; R-MMU-438066; Unblocking of NMDA receptors, glutamate binding and activation. DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade. DR Reactome; R-MMU-6794361; Neurexins and neuroligins. DR BioGRID-ORCS; 23859; 1 hit in 77 CRISPR screens. DR ChiTaRS; Dlg2; mouse. DR EvolutionaryTrace; Q91XM9; -. DR PRO; PR:Q91XM9; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q91XM9; Protein. DR Bgee; ENSMUSG00000052572; Expressed in caudate-putamen and 178 other cell types or tissues. DR ExpressionAtlas; Q91XM9; baseline and differential. DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC. DR GO; GO:0043194; C:axon initial segment; IDA:MGI. DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central. DR GO; GO:0030054; C:cell junction; IDA:MGI. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0044224; C:juxtaparanode region of axon; IDA:MGI. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0014069; C:postsynaptic density; IDA:ARUK-UCL. DR GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI. DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI. DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI. DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI. DR GO; GO:0019900; F:kinase binding; ISO:MGI. DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI. DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0098919; F:structural constituent of postsynaptic density; IDA:SynGO. DR GO; GO:0099641; P:anterograde axonal protein transport; IGI:ARUK-UCL. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0035865; P:cellular response to potassium ion; IDA:ARUK-UCL. DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI. DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; IDA:MGI. DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central. DR GO; GO:0045161; P:neuronal ion channel clustering; ISO:MGI. DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; IDA:SynGO. DR GO; GO:0043113; P:receptor clustering; ISO:MGI. DR GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central. DR GO; GO:0099642; P:retrograde axonal protein transport; IGI:ARUK-UCL. DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI. DR CDD; cd00071; GMPK; 1. DR CDD; cd00992; PDZ_signaling; 3. DR CDD; cd12032; SH3_DLG2; 1. DR Gene3D; 2.30.42.10; -; 3. DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR019583; DLG1-4_PDZ_assoc. DR InterPro; IPR016313; DLG1-like. DR InterPro; IPR019590; DLG1_PEST_dom. DR InterPro; IPR035759; DLG2_SH3. DR InterPro; IPR008145; GK/Ca_channel_bsu. DR InterPro; IPR008144; Guanylate_kin-like_dom. DR InterPro; IPR020590; Guanylate_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR23119; DISCS LARGE; 1. DR PANTHER; PTHR23119:SF6; DISKS LARGE HOMOLOG 2; 1. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF10608; MAGUK_N_PEST; 1. DR Pfam; PF00595; PDZ; 3. DR Pfam; PF10600; PDZ_assoc; 1. DR Pfam; PF00018; SH3_1; 1. DR PIRSF; PIRSF001741; MAGUK_DLGH; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM01277; MAGUK_N_PEST; 1. DR SMART; SM00228; PDZ; 3. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 3. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS50106; PDZ; 3. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q91XM9; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cell projection; KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome; KW Repeat; SH3 domain; Synapse. FT CHAIN 1..852 FT /note="Disks large homolog 2" FT /id="PRO_0000094554" FT DOMAIN 98..185 FT /note="PDZ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 193..280 FT /note="PDZ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 421..502 FT /note="PDZ 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 536..606 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 662..837 FT /note="Guanylate kinase-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100" FT MOD_RES 28 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087" FT MOD_RES 58 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18034455, FT ECO:0007744|PubMed:21183079" FT MOD_RES 65 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18034455, FT ECO:0007744|PubMed:21183079" FT MOD_RES 307 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 328 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63622" FT MOD_RES 365 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 406 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63622" FT MOD_RES 414 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16452087" FT MOD_RES 505 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18034455" FT MOD_RES 528 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63622" FT MOD_RES 530 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63622" FT MOD_RES 553 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 732 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18034455" FT MOD_RES 737 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18034455" FT LIPID 5 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT LIPID 7 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT VAR_SEQ 1..68 FT /note="MFFACYCALRTNVKKYRYQDEDGPHDHSLPRLTHEVRGPELVHVSEKNLSQI FT ENVHGYVLQSHISPLK -> MNAYLTKQHSCSRGSDGMDIGRSAPTLIRDAHCACGWQR FT NAQGLGYSSQTMPSSGPGGPASNRTKLVTLWDSVRKSPHKTSTKGKGNCGERCACPHGW FT FSPAQ (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_012869" FT VAR_SEQ 1..61 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_015517" FT VAR_SEQ 1..42 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_015518" FT VAR_SEQ 1..14 FT /note="MFFACYCALRTNVK -> MPVKKKDTDRALSLLEEYCKKLRKPEEQLLKNAV FT KKVMSIFKSSLFQALLDIQEFYEVTLLNSQKSCEQKIEEANHVAQKWEKTLLLDSCRDS FT LQKSSEHASCSGPKENALYIEQNKENQCSENETEEKTCQNQGKCPAQNCSVEAPTWMPV FT HHCT (in isoform 7)" FT /evidence="ECO:0000305" FT /id="VSP_015519" FT VAR_SEQ 1..13 FT /note="MFFACYCALRTNV -> MICHCKVACTNNTLSLMFGC (in isoform FT 2)" FT /evidence="ECO:0000305" FT /id="VSP_015520" FT VAR_SEQ 43..67 FT /note="HVSEKNLSQIENVHGYVLQSHISPL -> MFASIWYAKKLGRRFVHNARKAK FT SE (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_015521" FT VAR_SEQ 62..68 FT /note="SHISPLK -> MQHAFIP (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_015522" FT VAR_SEQ 69..86 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000305" FT /id="VSP_015523" FT VAR_SEQ 394 FT /note="S -> RYCMRFLTSSSPVACVSTRMDGWNSSPPTSLALSTFLVERCSASMVR FT WEKLRTWLFCSFCCAH (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_012870" FT VAR_SEQ 395..852 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_012871" FT VAR_SEQ 465..503 FT /note="DQILSVNGIDLRGASHEQAAAALKGAGQTVTIIAQYQPE -> VINASVNRT FT GDRRIWHQGNGKAASSVSCLLPALFPNFVL (in isoform 8)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_015524" FT CONFLICT 107 FT /note="G -> S (in Ref. 2; BAC32772)" FT /evidence="ECO:0000305" FT CONFLICT 123 FT /note="D -> G (in Ref. 1; AAK64496)" FT /evidence="ECO:0000305" FT CONFLICT 213 FT /note="N -> D (in Ref. 1; AAK64496)" FT /evidence="ECO:0000305" FT CONFLICT 301 FT /note="M -> T (in Ref. 1; AAK64496)" FT /evidence="ECO:0000305" FT CONFLICT 323 FT /note="S -> P (in Ref. 1; AAK64496)" FT /evidence="ECO:0000305" FT CONFLICT 585 FT /note="T -> I (in Ref. 1; AAK64496)" FT /evidence="ECO:0000305" FT CONFLICT 776 FT /note="I -> T (in Ref. 1; AAK64496)" FT /evidence="ECO:0000305" FT STRAND 94..102 FT /evidence="ECO:0007829|PDB:2WL7" FT TURN 104..106 FT /evidence="ECO:0007829|PDB:2WL7" FT STRAND 110..114 FT /evidence="ECO:0007829|PDB:2WL7" FT STRAND 127..132 FT /evidence="ECO:0007829|PDB:2WL7" FT HELIX 137..141 FT /evidence="ECO:0007829|PDB:2WL7" FT STRAND 149..153 FT /evidence="ECO:0007829|PDB:2WL7" FT HELIX 163..172 FT /evidence="ECO:0007829|PDB:2WL7" FT STRAND 175..184 FT /evidence="ECO:0007829|PDB:2WL7" SQ SEQUENCE 852 AA; 94880 MW; 632914AE45ACEBB6 CRC64; MFFACYCALR TNVKKYRYQD EDGPHDHSLP RLTHEVRGPE LVHVSEKNLS QIENVHGYVL QSHISPLKAS PAPIIVNTDT LDTIPYVNGT EIEYEFEEIT LERGNSGLGF SIAGGTDNPH IGDDPGIFIT KIIPGGAAAE DGRLRVNDCI LRVNEVDVSE VSHSKAVEAL KEAGSIVRLY VRRRRPILET VVEIKLFKGP KGLGFSIAGG VGNQHIPGDN SIYVTKIIDG GAAQKDGRLQ VGDRLLMVNN YSLEEVTHEE AVAILKNTSD VVYLKVGKPT TIYMTDPYGP PDITHSYSPP MENHLLSGNN GTLEYKTSLP PISPGRYSPI PKHMLGEDDY TRPPEPVYST VNKLCDKPAS PRHYSPVECD KSFLLSTPYP HYHLGLLPDS DMTSHSQHST ATRQPSVTLQ RAISLEGEPR KVVLHKGSTG LGFNIVGGED GEGIFVSFIL AGGPADLSGE LQRGDQILSV NGIDLRGASH EQAAAALKGA GQTVTIIAQY QPEDYARFEA KIHDLREQMM NHSMSSGSGS LRTNQKRSLY VRAMFDYDKS KDSGLPSQGL SFKYGDILHV INASDDEWWQ ARRVTLDGDS EEMGVIPSKR RVERKERARL KTVKFNAKPG VIDSKGDIPG LGDDGYGTKT LRGQEDLILS YEPVTRQEIN YTRPVIILGP MKDRINDDLI SEFPDKFGSC VPHTTRPKRD YEVDGRDYHF VISREQMEKD IQEHKFIEAG QYNDNLYGTS VQSVRFVAER GKHCILDVSG NAIKRLQVAQ LYPIAIFIKP KSLEPLMEMN KRLTEEQAKK TYDRAIKLEQ EFGEYFTAIV QGDTLEDIYN QCKLVIEEQS GPFIWIPSKE KL //