ID   DLG2_RAT                Reviewed;         852 AA.
AC   Q63622; P70548; Q62939;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 194.
DE   RecName: Full=Disks large homolog 2;
DE   AltName: Full=Channel-associated protein of synapse-110;
DE            Short=Chapsyn-110 {ECO:0000303|PubMed:11997254};
DE   AltName: Full=Postsynaptic density protein PSD-93;
GN   Name=Dlg2; Synonyms=Dlgh2;
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] (ISOFORM 1).
RX   PubMed=8755482; DOI=10.1016/s0896-6273(00)80284-6;
RA   Kim E., Cho K.-O., Rothschild A., Sheng M.;
RT   "Heteromultimerization and NMDA receptor-clustering activity of Chapsyn-
RT   110, a member of the PSD-95 family of proteins.";
RL   Neuron 17:103-113(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RX   PubMed=8625413; DOI=10.1016/s0092-8674(00)81053-3;
RA   Brenman J.E., Chao D.S., Gee S.H., McGee A.W., Craven S.E.,
RA   Santillano D.R., Wu Z., Huang F., Xia H., Peters M.F., Froehner S.C.,
RA   Bredt D.S.;
RT   "Interaction of nitric oxide synthase with the postsynaptic density protein
RT   PSD-95 and alpha1-syntrophin mediated by PDZ domains.";
RL   Cell 84:757-767(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Irie M., Hata Y., Takai Y.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND 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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 5), SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH NOS1.
RX   PubMed=8922396; DOI=10.1523/jneurosci.16-23-07407.1996;
RA   Brenman J.E., Christopherson K.S., Craven S.E., McGee A.W., Bredt D.S.;
RT   "Cloning and characterization of postsynaptic density 93, a nitric oxide
RT   synthase interacting protein.";
RL   J. Neurosci. 16:7407-7415(1996).
RN   [6]
RP   MUTAGENESIS OF CYS-5 AND CYS-7, AND PALMITOYLATION AT CYS-5 AND CYS-7.
RX   PubMed=10779526; DOI=10.1074/jbc.m909919199;
RA   El-Husseini A.E., Topinka J.R., Lehrer-Graiwer J.E., Firestein B.L.,
RA   Craven S.E., Aoki C., Bredt D.S.;
RT   "Ion channel clustering by membrane-associated guanylate kinases.
RT   Differential regulation by N-terminal lipid and metal binding motifs.";
RL   J. Biol. Chem. 275:23904-23910(2000).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11095503; DOI=10.1097/00001756-200011090-00016;
RA   Firestein B.L., Craven S.E., Bredt D.S.;
RT   "Postsynaptic targeting of MAGUKs mediated by distinct N-terminal
RT   domains.";
RL   NeuroReport 11:3479-3484(2000).
RN   [8]
RP   INTERACTION WITH KCNJ4, AND SUBCELLULAR LOCATION.
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   [9]
RP   INTERACTION WITH LRFN1.
RX   PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA   Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K.,
RA   Kim E.;
RT   "SALM synaptic cell adhesion-like molecules regulate the differentiation of
RT   excitatory synapses.";
RL   Neuron 50:233-245(2006).
RN   [10]
RP   INTERACTION WITH FRMPD4.
RX   PubMed=19118189; DOI=10.1523/jneurosci.3112-08.2008;
RA   Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B.,
RA   Eom S.H., Kim H., Kim E.;
RT   "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
RT   regulates dendritic spine morphogenesis.";
RL   J. Neurosci. 28:14546-14556(2008).
RN   [11]
RP   INTERACTION WITH ADAM22, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND TISSUE SPECIFICITY.
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   [12]
RP   INTERACTION WITH DGKI.
RX   PubMed=21119615; DOI=10.1038/emboj.2010.286;
RA   Yang J., Seo J., Nair R., Han S., Jang S., Kim K., Han K., Paik S.K.,
RA   Choi J., Lee S., Bae Y.C., Topham M.K., Prescott S.M., Rhee J.S.,
RA   Choi S.Y., Kim E.;
RT   "DGKiota regulates presynaptic release during mGluR-dependent LTD.";
RL   EMBO J. 30:165-180(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-365; SER-406;
RP   SER-414; SER-528 AND SER-530, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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: 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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts through its PDZ domains with NETO1. Interacts with
CC       NOS1/nNOS through second PDZ domain (PubMed:8922396). Interacts with
CC       KCNJ2/Kir2.1 (via C-terminus) through one of its PDZ domains (By
CC       similarity). Interacts with KCNJ4 (By similarity). Interacts with
CC       FRMPD4 (via C-terminus) (PubMed:19118189). Interacts with LRFN1
CC       (PubMed:16630835). Interacts with LRFN2 and LRFN4. Interacts with FASLG
CC       (By similarity). Interacts with ADAM22 (PubMed:20089912). Interacts
CC       with DGKI (via PDZ-binding motif) (PubMed:21119615).
CC       {ECO:0000250|UniProtKB:Q15700, ECO:0000250|UniProtKB:Q91XM9,
CC       ECO:0000269|PubMed:11997254, ECO:0000269|PubMed:16630835,
CC       ECO:0000269|PubMed:19118189, ECO:0000269|PubMed:20089912,
CC       ECO:0000269|PubMed:21119615, ECO:0000269|PubMed:8922396}.
CC   -!- INTERACTION:
CC       Q63622; F1MAB7: Dgki; NbExp=2; IntAct=EBI-396947, EBI-8523614;
CC       Q63622; O08560: Dgkz; NbExp=4; IntAct=EBI-396947, EBI-8570505;
CC       Q63622; P34926: Map1a; NbExp=4; IntAct=EBI-396947, EBI-631571;
CC       Q63622; Q01814-1: ATP2B2; Xeno; NbExp=2; IntAct=EBI-396947, EBI-1174262;
CC       Q63622; P23634-6: ATP2B4; Xeno; NbExp=2; IntAct=EBI-396947, EBI-1174437;
CC       Q63622; P34998: CRHR1; Xeno; NbExp=2; IntAct=EBI-396947, EBI-3870393;
CC       Q63622; O60333-3: KIF1B; Xeno; NbExp=3; IntAct=EBI-396947, EBI-465669;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10779526};
CC       Lipid-anchor {ECO:0000269|PubMed:10779526}. Postsynaptic density
CC       {ECO:0000269|PubMed:11095503}. Synapse. Cell projection, axon
CC       {ECO:0000269|PubMed:20089912}. Membrane {ECO:0000269|PubMed:11997254,
CC       ECO:0000269|PubMed:20089912}. Perikaryon {ECO:0000269|PubMed:11095503}.
CC       Note=Concentrated in soma and postsynaptic density of a subset of
CC       neurons (PubMed:11095503). {ECO:0000269|PubMed:11095503}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1; Synonyms=PSD-93b;
CC         IsoId=Q63622-1; Sequence=Displayed;
CC       Name=2; Synonyms=PSD-93a;
CC         IsoId=Q63622-2; Sequence=VSP_015528;
CC       Name=3; Synonyms=PSD-93c;
CC         IsoId=Q63622-3; Sequence=VSP_015527, VSP_015529, VSP_015530;
CC       Name=4; Synonyms=PSD-93-delta;
CC         IsoId=Q63622-4; Sequence=VSP_015526;
CC       Name=5; Synonyms=PSD-93d;
CC         IsoId=Q63622-5; Sequence=VSP_015525;
CC       Name=6;
CC         IsoId=Q63622-6; Sequence=VSP_015531, VSP_015533;
CC       Name=7;
CC         IsoId=Q63622-7; Sequence=VSP_015532;
CC   -!- TISSUE SPECIFICITY: Detected in juxtaparanodal zones in the central
CC       nervous system and at nerve terminal plexuses of basket cells in the
CC       cerebellum (at protein level) (PubMed:20089912). Brain. High levels in
CC       cerebellar Purkinje cells. Expressed in pyramidal cells of the Ammons's
CC       horn and granular cells of the dentate gyrus in the hippocampus as well
CC       as cerebral cortex and striatum. High levels in dorsal horn of spinal
CC       cord. {ECO:0000269|PubMed:15304517, ECO:0000269|PubMed:20089912,
CC       ECO:0000269|PubMed:8922396}.
CC   -!- DEVELOPMENTAL STAGE: High levels in developing brain and spinal chord,
CC       sensory neurons of dorsal root and trigeminal ganglia, myenteric
CC       neurons of the intestine as well as in non-neuronal cells of adrenal,
CC       thymus and submandibular glands of 15 dpc embryos.
CC       {ECO:0000269|PubMed:8922396}.
CC   -!- PTM: Palmitoylation of isoform 1 and isoform 2 is not required for
CC       targeting to postsynaptic density. {ECO:0000269|PubMed:10779526}.
CC   -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR   EMBL; U49049; AAB53243.1; -; mRNA.
DR   EMBL; U50717; AAC52643.1; -; mRNA.
DR   EMBL; U53368; AAB48562.1; -; mRNA.
DR   PIR; T10811; T10811.
DR   RefSeq; NP_071618.1; NM_022282.1. [Q63622-1]
DR   PDB; 4H11; X-ray; 1.67 A; A/B=93-188.
DR   PDBsum; 4H11; -.
DR   AlphaFoldDB; Q63622; -.
DR   SMR; Q63622; -.
DR   BioGRID; 248965; 11.
DR   CORUM; Q63622; -.
DR   IntAct; Q63622; 19.
DR   MINT; Q63622; -.
DR   STRING; 10116.ENSRNOP00000052268; -.
DR   iPTMnet; Q63622; -.
DR   PhosphoSitePlus; Q63622; -.
DR   SwissPalm; Q63622; -.
DR   PaxDb; 10116-ENSRNOP00000052268; -.
DR   ABCD; Q63622; 3 sequenced antibodies.
DR   Ensembl; ENSRNOT00000108774.1; ENSRNOP00000092409.1; ENSRNOG00000022635.8. [Q63622-7]
DR   Ensembl; ENSRNOT00000110277.1; ENSRNOP00000097641.1; ENSRNOG00000022635.8. [Q63622-1]
DR   GeneID; 64053; -.
DR   KEGG; rno:64053; -.
DR   UCSC; RGD:619895; rat. [Q63622-1]
DR   AGR; RGD:619895; -.
DR   CTD; 1740; -.
DR   RGD; 619895; Dlg2.
DR   eggNOG; KOG0708; Eukaryota.
DR   GeneTree; ENSGT00940000155156; -.
DR   InParanoid; Q63622; -.
DR   OrthoDB; 2879721at2759; -.
DR   Reactome; R-RNO-438066; Unblocking of NMDA receptors, glutamate binding and activation.
DR   Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR   PRO; PR:Q63622; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0043194; C:axon initial segment; ISO:RGD.
DR   GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR   GO; GO:0030054; C:cell junction; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
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; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR   GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR   GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD.
DR   GO; GO:0019900; F:kinase binding; ISO:RGD.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0098919; F:structural constituent of postsynaptic density; ISO:RGD.
DR   GO; GO:0099641; P:anterograde axonal protein transport; ISO:RGD.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0035865; P:cellular response to potassium ion; ISO:RGD.
DR   GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0045163; P:clustering of voltage-gated potassium channels; ISO:RGD.
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; IMP:RGD.
DR   GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:RGD.
DR   GO; GO:0043113; P:receptor clustering; IMP:RGD.
DR   GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
DR   GO; GO:0099642; P:retrograde axonal protein transport; ISO:RGD.
DR   GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
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.
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_0000094555"
FT   DOMAIN          98..184
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          193..279
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          421..501
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:0000250|UniProtKB:Q91XM9"
FT   MOD_RES         58
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT   MOD_RES         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT   MOD_RES         360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         365
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         414
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         505
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT   MOD_RES         528
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         530
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         553
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT   MOD_RES         732
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT   MOD_RES         737
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91XM9"
FT   LIPID           5
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:10779526"
FT   LIPID           7
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:10779526"
FT   VAR_SEQ         1..246
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:8922396"
FT                   /id="VSP_015525"
FT   VAR_SEQ         1..68
FT                   /note="MFFACYCALRTNVKKYRYQDEDGPHDHSLPRLTHEVRGPELVHVSEKNLSQI
FT                   ENVHGYVLQSHISPLK -> MNAYLTKQHSCSRGSDGMDAGRGVPTLIRDAHCACGWQR
FT                   NAQGLGYSSQTMPSSGPGGPASNRTKLVTLWDSVRKSPHKTSTKGKGNCGERCACPHGW
FT                   FSPAQ (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_015526"
FT   VAR_SEQ         1..61
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:8922396"
FT                   /id="VSP_015527"
FT   VAR_SEQ         1..13
FT                   /note="MFFACYCALRTNV -> MICHCKVACTNNTLSLMFGC (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:8922396"
FT                   /id="VSP_015528"
FT   VAR_SEQ         62..68
FT                   /note="SHISPLK -> MQHAFIP (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:8922396"
FT                   /id="VSP_015529"
FT   VAR_SEQ         341..392
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:8922396"
FT                   /id="VSP_015530"
FT   VAR_SEQ         450..454
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:8625413"
FT                   /id="VSP_015531"
FT   VAR_SEQ         626..641
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:8625413"
FT                   /id="VSP_015533"
FT   VAR_SEQ         626..641
FT                   /note="GDIPGLGDDGYGTKTL -> GSFNDKRKKSFIFSRKFPFYKNKEQSEQETSD
FT                   PE (in isoform 7)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_015532"
FT   MUTAGEN         5
FT                   /note="C->S: Loss of palmitoylation and targeting to
FT                   postsynaptic density."
FT                   /evidence="ECO:0000269|PubMed:10779526"
FT   MUTAGEN         7
FT                   /note="C->S: Loss of palmitoylation and targeting to
FT                   postsynaptic density."
FT                   /evidence="ECO:0000269|PubMed:10779526"
FT   CONFLICT        181..182
FT                   /note="VR -> IL (in Ref. 2; AAC52643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        228
FT                   /note="I -> M (in Ref. 2; AAC52643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        326
FT                   /note="R -> K (in Ref. 2; AAC52643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="D -> E (in Ref. 3; AAB48562)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464..465
FT                   /note="GD -> RK (in Ref. 2; AAC52643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        474
FT                   /note="D -> H (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        476
FT                   /note="R -> P (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        478
FT                   /note="A -> D (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        484..486
FT                   /note="AAA -> LP (in Ref. 2; AAC52643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        506
FT                   /note="A -> S (in Ref. 2; AAC52643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        569
FT                   /note="H -> N (in Ref. 2; AAC52643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        586
FT                   /note="L -> Q (in Ref. 2; AAC52643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        627..630
FT                   /note="DIPG -> TSR (in Ref. 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        639
FT                   /note="K -> A (in Ref. 3; AAB48562)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        726
FT                   /note="F -> L (in Ref. 1; AAB53243)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        733
FT                   /note="N -> Y (in Ref. 2; AAC52643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        749
FT                   /note="E -> V (in Ref. 1; AAB53243)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        756
FT                   /note="L -> H (in Ref. 2; AAC52643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        791..792
FT                   /note="KR -> NG (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        794
FT                   /note="T -> M (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   STRAND          93..102
FT                   /evidence="ECO:0007829|PDB:4H11"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:4H11"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:4H11"
FT   STRAND          127..132
FT                   /evidence="ECO:0007829|PDB:4H11"
FT   HELIX           137..141
FT                   /evidence="ECO:0007829|PDB:4H11"
FT   STRAND          149..153
FT                   /evidence="ECO:0007829|PDB:4H11"
FT   HELIX           163..172
FT                   /evidence="ECO:0007829|PDB:4H11"
FT   STRAND          175..184
FT                   /evidence="ECO:0007829|PDB:4H11"
SQ   SEQUENCE   852 AA;  94934 MW;  F8D414A8B9CF5B09 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 PKHMLVEDDY TRPPEPVYST VNKLCDKPAS
     PRHYSPVECD KSFLLSTPYP HYHLGLLPDS DMTSHSQHST ATRQPSVTLQ RAISLEGEPR
     KVVLHKGSTG LGFNIVGGED GEGIFVSFIL AGGPADLSGE LQRGDQILSV NGIDLRGASH
     EQAAAALKGA GQTVTIIAQY QPEDYARFEA KIHDLREQMM NHSMSSGSGS LRTNQKRSLY
     VRAMFDYDKS KDSGLPSQGL SFKYGDILHV INASDDEWWQ ARRVILDGDS 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
//