DLG2_MOUSE
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 03-AUG-2022, entry version 172.
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; 20.
DR DIP; DIP-31569N; -.
DR IntAct; Q91XM9; 20.
DR MINT; Q91XM9; -.
DR STRING; 10090.ENSMUSP00000102814; -.
DR iPTMnet; Q91XM9; -.
DR PhosphoSitePlus; Q91XM9; -.
DR SwissPalm; Q91XM9; -.
DR jPOST; Q91XM9; -.
DR MaxQB; Q91XM9; -.
DR PaxDb; Q91XM9; -.
DR PeptideAtlas; Q91XM9; -.
DR PRIDE; 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; 367 antibodies from 35 providers.
DR DNASU; 23859; -.
DR Ensembl; ENSMUST00000107196; ENSMUSP00000102814; ENSMUSG00000052572. [Q91XM9-1]
DR Ensembl; ENSMUST00000238619; ENSMUSP00000158731; ENSMUSG00000052572. [Q91XM9-4]
DR GeneID; 23859; -.
DR KEGG; mmu:23859; -.
DR UCSC; uc009ihr.2; mouse. [Q91XM9-1]
DR UCSC; uc009ihs.1; mouse. [Q91XM9-5]
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; 807583at2759; -.
DR TreeFam; TF323171; -.
DR BioGRID-ORCS; 23859; 0 hits in 72 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 176 other tissues.
DR ExpressionAtlas; Q91XM9; baseline and differential.
DR Genevisible; Q91XM9; MM.
DR GO; GO:0099031; C:anchored component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005737; C:cytoplasm; ISO: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; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus 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; cd12032; SH3_DLG2; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
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; IPR019583; PDZ_assoc.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 3.
DR SUPFAM; SSF52540; SSF52540; 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.
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
